Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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D3Z8E6 | CAMP1_RAT | MVDAGGRSAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQAATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKPGLEHAVMHCMLEPVDFARVVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCFYLTLEDMLYAPLVLKPNVMVFIAELFWWFENVKPDFVQPRDIQELKDAKTVLQQKSSRPPVPISNATKRSFLGSPAAMSPADLPPSTQPLTEGSHRYHLHSEEPECLGKGASTFSPSHPLLPLRQKQQKVSQAEEIPDQRHRSNSLTRADGQPRGAAIAWPDKKNRPVSQPTSFALHHAASCDVDPSSGDSISLARSISKDSLASNIIHLTPQNQPHPSAGKTNGKSLLSNVNIEDDEEEELVAIIRTDVSPHSPEIPRTSPQAPGLVASIRSPQRQADTLESKPDSFYLEPLMPAVLRPAKEKQIITKEDERGEGRPRTIMAKRPSEGSQPLVRKKVTGSHGSRDLNRTFTPIPCSEFAASIDPTEVGPQSTEATGEGQPLALGRFDPVPQGQVADGFFLHVGRAEEDEGRWYVGSQSPSSHDSEPWTILRQDSDSDVVDVEDAEQDFIGEDHPVVIPRYAGEEESAKLQEDMKVKEHEDKDDASGRSSPCLSTTSQLSSMSMASGSVKMTSFAERKLQRLNSCETKSSTSSSQKTTPDASESCPAPLTTWRQKREQSPSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKKGKADGAPQPLRPEHFTKEFTQHNGEDLDDGTCKTEGFLVKEEQRDLSDSQDVAFVQLHKPRDPATLHDGEKHRVISAALLEDSVGEVDVNECDLSIEKLNETISTLQQAILKISQQQEQLLMKSPTVPTSGTKNNCQDQKVKAPVHFVEPLSPTGVPGHRKPPRLGQGRNSRSGRPAELKVPKDRQQGCSRSKTPTPSVETLPHSRSLPPSTHPRSPLDPGGELPEKCLFDSYRLHDESNHRTFGLSSCKDANIVSEQMNFKEGLDTSVQEAELSSSAITGKEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLELGGESDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQGLGKPKSKPKKPRPKSVHREESCSDSGTKCSSTPDNLSQTHSGSSLSLASAATTEPESVHSGGTPSHRVESLEALPILSRNPSRSTDRDWETASAASSLASVAEYTGPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTGPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPTVPKKTQTRK | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; neuron projection development [GO:0031175]; regulation of cell morphogenesis [GO:0022604]; regulation of microtubule polymerization [GO:0031113] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:24117850). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (By similarity). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850). {ECO:0000250|UniProtKB:Q5T5Y3, ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:24117850}. | Rattus norvegicus (Rat) |
D3Z8K2 | CCD39_RAT | MSSEFLSELHWEDGFAIPVANQENKILEDQLAKLHKEKSNLQDQLRDYEDRINSMSSHLKNVNQEFLFTQSLYKARECEIESEEHFKAIAERELGRVKDEIQQLEKEMAIILERKNDKENAIFKATQKLDGLKCQMNWDQQALEAWLEESAHKDSDSLTLQKYSQQDNNKIRALTLKLEKLTMECNEKRKLLDNELTETLSAQLELDKAAQDFRKIHVERQELIQQWENTIEQMQRRDQEIDNCALALARIKQEAREKEGVVREKIKFLENEVGNNVEYERRISIAERKVSKCRMEYQRQEANRNQLKDELDTLKTTLNRTSSDLEALRKNISKVKKDILDETGRLQKLKHHNEIVKHKLKMITEKTISIEEKATNMEDMLKEEEKNLKEVEVQLNIVKGVLFKKVQELQSAITKEKALGSEIEGTRSSLKHLNQRLHKLDFETLKQQEIMYSQDFYIQQVERRMSRLKGEINSEEKQALEVKIVELRKTMEERKSTLSLLEEQIKKLHNDLYFIKKSNGKNKDEKESLMNKIGELHLFVDRSEKELNKAKAVKEDLMIEDNLLKLQVKRARELLYSKAEEVLSLEKRKQQLCTAMEERVEEIKVHKAMLTSQIRYVDQQRQTVSSEFHERLSKIDKLKNRYEILTVVMLPPEGEEEKTQSYYVIKAAQEKEELQREGDSLDAKISKAEKEIYALQNTLQVLSSCNNNYKQSFKKVTPSSDEYGIKIQLEEQKRSADEKYRCKQRQIRELQEDIQSMENTFEVIEHLANNAREKLSEKQTLSFQLRKETEEQKPKIQRVTKQCGRLRREIRILRQTNDETLEEQDIQLREIIQFHKDIDQMLVNAMENAEIHVIFQTYFQQNGLELPTAKGPSSRSSSQSSLSSIRSLEDSIPISPPTAKVIELRFPGPPARSDSSRSSSGSNSNIPKGKKLNK | null | null | axonemal dynein complex assembly [GO:0070286]; brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; cilium-dependent cell motility [GO:0060285]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of left/right symmetry [GO:0007368]; determination of liver left/right asymmetry [GO:0071910]; determination of pancreatic left/right asymmetry [GO:0035469]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of left/right asymmetry [GO:0061966]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; heart development [GO:0007507]; heart looping [GO:0001947]; inner dynein arm assembly [GO:0036159]; lung development [GO:0030324]; motile cilium assembly [GO:0044458]; protein localization to cilium [GO:0061512]; regulation of cilium beat frequency [GO:0003356] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576] | null | null | null | CCDC39 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UFE4}. Note=CCDC40 is required for localization to axonemes. {ECO:0000250|UniProtKB:Q9UFE4}. | null | null | null | null | null | FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly. {ECO:0000250|UniProtKB:A8IQT2, ECO:0000250|UniProtKB:Q9UFE4}. | Rattus norvegicus (Rat) |
D3Z8L7 | RRAS_RAT | MSSGAASGTGRGRPRGGGPGPRDPPPGETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICTVDGIPARLDILDTAGQEEFGAMREQYMRAGNGFLLVFAINDRQSFIEVSKLFTQILRVKDRDDFPIVLVGNKADLETQRQVLRSEASSFSASHHMTYFEASAKLRLNVDEAFEQLVRTVRKYQEQELPPSPPSAPRKKDGRCPCVLL | 3.6.5.- | null | cell migration [GO:0016477]; face morphogenesis [GO:0060325]; leukocyte differentiation [GO:0002521]; negative regulation of Schwann cell migration [GO:1900148]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matrix adhesion via fibronectin [GO:1904906]; positive regulation of vasculogenesis [GO:2001214]; Ras protein signal transduction [GO:0007265]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; Schwann cell migration [GO:0036135] | plasma membrane [GO:0005886] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: S-palmitoylated by ZDHHC19, leading to increased association with membranes and with rafts/caveolae as well as enhanced cell viability. {ECO:0000250|UniProtKB:P10301}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P62070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P62070}; | null | null | null | null | FUNCTION: Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity. {ECO:0000250|UniProtKB:P10301}. | Rattus norvegicus (Rat) |
D3Z902 | FBXW7_RAT | MNQELLSVGSKRRRTGGSLRGNASSSQVDEEQMNRVVEEDPQQQPRHQEEEHTARNGELVGADPRPGAQNDSQQGQVEENNNRFVSVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEEEEMDQESDDFDQSDDSSREDEHTHNSNVTNCTSVVDLPINQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKIIKPGFIHSPWKSAYIRQHRIDTNWRRGELRSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPSKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; lung development [GO:0030324]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast development [GO:2001205]; Notch signaling pathway [GO:0007219]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903378]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein destabilization [GO:0031648]; protein K63-linked ubiquitination [GO:0070534]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of cell migration involved in sprouting angiogenesis [GO:0090049]; regulation of circadian rhythm [GO:0042752]; regulation of mitophagy [GO:1901524]; rhythmic process [GO:0048511]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; sister chromatid cohesion [GO:0007062]; ubiquitin recycling [GO:0010992]; vasculogenesis [GO:0001570] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; Parkin-FBXW7-Cul1 ubiquitin ligase complex [GO:1990452]; perinuclear region of cytoplasm [GO:0048471]; SCF ubiquitin ligase complex [GO:0019005] | cyclin binding [GO:0030332]; identical protein binding [GO:0042802]; phosphothreonine residue binding [GO:0050816]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin binding [GO:0043130]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activator activity [GO:0097027] | PF12937;PF00400; | 1.20.1280.50;2.130.10.10; | null | PTM: Phosphorylation at Thr-211 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation. Phosphorylated by ATM at Ser-26 in response to DNA damage, promoting recruitment to DNA damage sites and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4. {ECO:0000250|UniProtKB:Q969H0}.; PTM: Ubiquitinated: autoubiquitinates following phosphorylation at Thr-211 and subsequent interaction with PIN1. Ubiquitination leads to its degradation. {ECO:0000250|UniProtKB:Q969H0}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q969H0}. Chromosome {ECO:0000250|UniProtKB:Q969H0}. Note=Localizes to site of double-strand breaks following phosphorylation by ATM. {ECO:0000250|UniProtKB:Q969H0}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q969H0}. | null | null | FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination (By similarity). Identified substrates include cyclin-E (CCNE1 or CCNE2), JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, MLST8, RICTOR and probably PSEN1 (By similarity). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (By similarity). SCF(FBXW7) complex mediates the ubiquitination and subsequent degradation of NFE2L1 (By similarity). Involved in bone homeostasis and negative regulation of osteoclast differentiation (By similarity). Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination (By similarity). Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage (By similarity). The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining (By similarity). {ECO:0000250|UniProtKB:Q8VBV4, ECO:0000250|UniProtKB:Q969H0}. | Rattus norvegicus (Rat) |
D3Z9H7 | NFAC4_RAT | MGAASCEDEELEFKLVFGEEKEAPPLGPGGPGEELDSEDAPPCCRLALGEPLPYGAAPIGIPRPPPPRPGMHSPPPRPAPSPGTWESQPPRSVRLGGPGGTAGGTGGGRVLECPSIRITSISPTPDPPTSLEDAPETWGDGSPRDYPPPEGFGGYREAGGQGGGAFFSPSPGSSSLSSWSFFSDASDEAALYAACDEVESELNEAASRFGLSSPLPSPRASPRPWTPEDPWSLYGPSSGGRAPEDSWLLLSAPGPIPASPRPASPCGKRRYSSSGTPSSASPALSRRGSLGEEGPEPPPPPPLPLVRDPSSSGPFDYVGAPPTESVPQKTRRTSSEQAVALPRSEEPASCNGKLPSGTEDSVAAPGALRKEMAGMDYLAVPSPLAWSKARIGGHSPIFRTSALPPLDWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYNEKPLTLQMFIGTADERSLRPHAFYQVHRITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIECSQRSAQELPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEAAVNRLQSSEVTLTLTIPEYSNKRVSRPVQVYFYVSNGRRKRSPTQSFKFLPVIFKEEPLPDSSLRGFPSTSGPPFGPDMDFSPPRPPYPSYPHEDPAYETPYLSEGFGYSTPALYPQTGPPPSYRSGLRMFPETGGTTGCARLPSVSFLPRPFPGDQYGGQGSSFPLGLPFSPPAPFRPPLPSSPPLEDPFNPQSAVHPLPAEGYNEVGPGYTPGEGASEQEKSRGGYGSGFRDNVPIQGITLEEVSEIIGRDLSGFPARPGEEPPA | null | null | brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; branching involved in blood vessel morphogenesis [GO:0001569]; calcineurin-NFAT signaling cascade [GO:0033173]; cellular respiration [GO:0045333]; cellular response to lithium ion [GO:0071285]; cellular response to UV [GO:0034644]; dendrite morphogenesis [GO:0048813]; heart development [GO:0007507]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of synapse maturation [GO:2000297]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of DNA-templated transcription [GO:0006355]; regulation of synaptic plasticity [GO:0048167]; regulation of transcription by RNA polymerase II [GO:0006357]; synapse maturation [GO:0060074]; transcription by RNA polymerase II [GO:0006366]; vascular associated smooth muscle cell development [GO:0097084]; vascular associated smooth muscle cell differentiation [GO:0035886] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; peroxisome proliferator activated receptor binding [GO:0042975]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976] | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated by NFATC-kinases; dephosphorylated by calcineurin/PPP3CA. Phosphorylated on Ser-168 and Ser-170 by MTOR, IRAK1, MAPK7/ERK5 and MAPK14/p38, on Ser-213 and Ser-217 by MAPK8 and MAPK9, and on Ser-289 and Ser-344 by RPS6KA3 (By similarity). Phosphorylated by GSK3B; this phosphorylation markedly increases NFATC4 ubiquitination (PubMed:19026640). Phosphorylation by MAPK8/JNK1, MAPK9/JNK2 and RPS6KA3 may stimulate NFATC4 transcriptional activity. Phosphorylation at Ser-168 and Ser-170 is stimulated by UV irradiation (By similarity). {ECO:0000250|UniProtKB:Q14934, ECO:0000250|UniProtKB:Q8K120, ECO:0000269|PubMed:19026640}.; PTM: Ubiquitinated, leading to degradation by the proteasome. Ubiquitination may be stimulated by GSK3B-dependent phosphorylation. Polyubiquitin linkage mainly occurs through 'Lys-48'. {ECO:0000269|PubMed:19026640}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K120}. Nucleus {ECO:0000250|UniProtKB:Q8K120}. Note=When hyperphosphorylated, localizes in the cytosol. When intracellular Ca(2+) levels increase, dephosphorylation by calcineurin/PPP3CA leads to translocation into the nucleus. MAPK7/ERK5 and MTOR regulate NFATC4 nuclear export through phosphorylation at Ser-168 and Ser-170. {ECO:0000250|UniProtKB:Q14934}. | null | null | null | null | null | FUNCTION: Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems. Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4 (PubMed:12370307). Along with NFATC3, involved in embryonic heart development. Following JAK/STAT signaling activation and as part of a complex with NFATC3 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (PubMed:19538478). Involved in mitochondrial energy metabolism required for cardiac morphogenesis and function. Transactivates many genes involved in heart physiology. Along with GATA4, binds to and activates NPPB/BNP promoter (PubMed:9568714). Activates NPPA/ANP/ANF and MYH7/beta-MHC transcription (PubMed:19026640). Binds to and transactivates AGTR2 gene promoter. Involved in the regulation of adult hippocampal neurogenesis. Involved in BDNF-driven pro-survival signaling in hippocampal adult-born neurons. Involved in the formation of long-term spatial memory and long-term potentiation. In cochlear nucleus neurons, may play a role in deafferentation-induced apoptosis during a developmental critical period when auditory neurons depend on afferent input for survival (By similarity). Binds to and activates the BACE1/Beta-secretase 1 promoter, hence may regulate the proteolytic processing of the amyloid precursor protein (APP). Plays a role in adipocyte differentiation. May be involved in myoblast differentiation into myotubes (By similarity). Binds the consensus DNA sequence 5'-GGAAAAT-3' (By similarity). In the presence of CREBBP, activates TNF transcription. Binds to PPARG gene promoter and regulates its activity (By similarity). Binds to PPARG and REG3G gene promoters (By similarity). {ECO:0000250|UniProtKB:Q14934, ECO:0000250|UniProtKB:Q8K120, ECO:0000269|PubMed:12370307, ECO:0000269|PubMed:19026640, ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:9568714}. | Rattus norvegicus (Rat) |
D3Z9Z9 | SMRCD_RAT | MNLFNLDRFRFEKRSKIEEAPEAAPQPSQPGPSSPISLSAEEENAEGEVSRANTPDSDVTEKTEDSSVPEPPDNESKASLSCFQNQRTIQEYIDLSSDSEDVSPNCSSTVQEKKFSKDTVIIVSEPSEDEESHDLPSATRRNDISELEDLSELEDLKDAKLQTLKELFPQRSDSDLLKLIDSTSTMDGAIAAALLKFGDAGGGPRKRKLSSSSEAYEEDEANDDQSLKKPRGDRREESNESAEASSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDVQCASQSEVTNGKEVARNQNYSKNAAKIKMKQKISMKPQNGFNKKRKKNVFNPKKAVEDSEYDSGSDAGSSLDEDYSSCEEVMEDGYKGKILHFLQDASIGELTLIPKCSQKKAQKIIELRPFNNWETLFTKMSKINGLSEDLIWNCKTVIQERDVVIRLMNKCEDISNKLTKQVTMLTGNGGGWNIEQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQYYTAEKLKEMSQLMLKEPTHCEANPDLIFEDMEVMTDFELHVLCKQYQHINSYQLDMDLILDSGKFRTLGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLEQDMTTVDEADEGSMPADIATLLKTSMGL | 3.6.4.12 | null | chromatin remodeling [GO:0006338]; chromosome separation [GO:0051304]; DNA double-strand break processing [GO:0000729]; regulation of DNA recombination [GO:0000018] | heterochromatin [GO:0000792]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; ubiquitin binding [GO:0043130] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZA12 | CHD6_RAT | MKMKIQKKEKQLSKLRALNHSPMSDASVNFDYKSPSPFDCSPDQGENIEEAANHCLPQKDFYTTEEEADTLFSRKLMSHNGMEDNGGRGTGVKKKRKKKEPGEQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPVERKKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEKDPRIAQKIKRFRNKQAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPEVKPVERPASDAWQKLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLINGAEEKILEDFRKAHSSEASDFQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKESLVIDRPRVRKQTKHYNSFEEDELMEFSELDSDSDERPTRSRRLSDKARRYLRAECFRVEKNLLTFGWGRWKDILTHGRFKWPLNEKDMEVICRALLVYCVKHYKGDEKIKSFIWELITPSKDGQVQTLQNHSGLSAPVPRGRKGKKTKNQLLLPELKTADWLATCNPEVVLHDDGYKKHLKQHCNKVLLRVRMLYYLKAEILGEAADKAFEGTPARELDVLLPDIDYVEIPVDWWDAEADKSLLIGVFKHGYERYNAMRADPALCFLEKVGMPDEKSLSAEQGVTDGTSDIPERGNIDKEDSAEDKVDGLQKQTASPSDGSDGIFGEKKDDSQAVSSALTARLRRLVTIYQRCNRKELCRPEILGPGNQGYWVQEEVFRRTSDMDLINKEAQKRWTRREQADFYRTVSSFGVVYDQEKEAFDWTQFRAISRLDKKSDENLEHYFHSFVAMCRNVCRLPTWKDDGPPDASIYVEPITEERAAKTLYRIELLRKVREQVLTCPQLHERLQLCRPSLYLPVWWECGKHDRDLLIGTAKHGLNRTDYYIMNDPQLSFLDAYRNYAQHKRTDTQAPGSLCCLYQGNSKLYESLTYTPMSRTSESLESEPENLVKMDSRDDHLCLPEAGLPDITCENFVSKVQEVISLDHDESLLPESLENMMYGKTGLSQEPRSFQEAPSTNMQSRKKTVTVSASRDESCQLPGIEAEITSASSLMSSLEAGVAKMNIKNGKHLLVSISEEGEPCCSETGRSPESRGRLEARCLASPTLDTGHESGFVDLCSLSVYDSKRNFSSDQQLIDLLENKSLENKLILNQSDEEEEENEKETLAIVASTTEKPAVLDFTQPTASIPRGKNLSFHQDEAKKGRLEVGSKTPGPQRAFPPSANQCHCKHIERWAHGLGSEESEGEKPKAYEPDPYRSKANNTTVEGEPAIIPTEPFKLKHELLKEPWKESSEGGKSFSMYVPEGSEPKSEEMDFENKDDYEKDGACHSQDYPGKYSEEESKSSASGIAGDLGEEAQEVRAPTIAQLLQEKTLYSFSEWPKDRVIINRLDNICHVVLKGKWPCSHQYEPSGALPTPVLSSSAGSRSSLSEPEATEHSFSNGAALAAQIQKESFLAPVFTKDEQKHRRPYEFEVERDAKARSLEEYSASHGRPPIVLNGWHGESAIDLSCSSEGSPGATSPFPVSASTPKIGAISSLQGALGMDLSGILQAGLIHPVTGQIVNGSLRRDDAAMRRRRGRRKHIEGGMDLIFLKEQTLQAGILEVHEDAGQTTLNTTHPEGPGAASSASEPTAAASSQAEKAVPSKSLLDWLRQQADYSLDVPGFGASFSDKPKQRRPRCKEPGKLDIGSLGGEERVSAVPKEPGLRGFLPESKFNHTLAEPVLRDAGPRRRGRRPRNELLKAPAIVADSPSGMGPLFMNGLIAGMDLVGLQNVRNIPGIPLTGLVGFPAGFATMPTGEDVKNTLSMLPMMLPGMATVPQMFGVGGLLNTPMATTCTTTASASLASTKSGASATEKTTEDELSGRDVKADSLVEDKPGPSPFSDQSEPTITTSSPVAFNPFLIPGVSPGLIYPSMFLSPGMGMALPAMQQGRHSEMAGLETQKRKKKKTKGDNPTPEPASVCEREPGSDQNCTESSVTVSPEREHVAQAREEGLKDSNDDTN | 3.6.4.12 | null | cell redox homeostasis [GO:0045454]; chromatin remodeling [GO:0006338]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; transcription coregulator binding [GO:0001221] | PF00385;PF00271;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA synthesis. {ECO:0000250|UniProtKB:Q8TD26}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q8TD26}; | null | null | null | null | FUNCTION: DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000250|UniProtKB:Q8TD26}. | Rattus norvegicus (Rat) |
D3ZAA9 | MPP2_RAT | MPVAATNSESAMQQVLDNLGSLPNATGAAELDLIFLRGIMESPIVRSLAKAHERLEETKLEAVRDNNLELVQEILRDLAELAEQSSTAAELARILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRSASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLIPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPTSGTLCGSLSGKKKKRMMYLTTKNAEFDRHELLIYEEVARMPPFRRKTLVLIGAQGVGRRSLKNKLILWDPDRYGTTVPYTSRRPKDSEREGQGYSFVSRGEMEADIRAGRYLEHGEYEGNLYGTRIDSIRGVVASGKVCVLDVNPQAVKVLRTAEFVPYVVFIEAPDFETLRAMNRAALESGVSTKQLTEADLRRTVEESSRIQRGYGHYFDLSLVNSNLERTFRELQTAMEKLRTEPQWVPVSWVY | null | null | excitatory postsynaptic potential [GO:0060079]; long-term synaptic potentiation [GO:0060291]; maintenance of postsynaptic density structure [GO:0099562]; postsynapse organization [GO:0099173]; protein homooligomerization [GO:0051260] | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; Schaffer collateral - CA1 synapse [GO:0098685] | PDZ domain binding [GO:0030165]; structural constituent of postsynaptic density [GO:0098919]; transmembrane transporter binding [GO:0044325] | PF00625;PF02828;PF00595;PF07653; | 2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40; | MAGUK family | PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:Q14168}. | SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic density {ECO:0000269|PubMed:27756895}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14168}. Membrane {ECO:0000250|UniProtKB:Q14168}. Note=Prominently expressed in the postsynaptic densities of dendritic spines, is also detected in dendritic shafts. {ECO:0000250|UniProtKB:Q9WV34}. | null | null | null | null | null | FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (PubMed:27756895). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression (By similarity). Seems to negatively regulate SRC function in epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q14168, ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:27756895}. | Rattus norvegicus (Rat) |
D3ZAR1 | ARH_RAT | MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAQMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTSVATGNLLDLEELAKAPLSTVSANTKNMDDALRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDIHYAQCLSPTDWDKPDSSGFDQDDVFSF | null | null | amyloid precursor protein metabolic process [GO:0042982]; cellular response to cytokine stimulus [GO:0071345]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle clearance [GO:0034383]; positive regulation of low-density lipoprotein particle clearance [GO:1905581]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; receptor-mediated endocytosis involved in cholesterol transport [GO:0090118]; regulation of protein localization to plasma membrane [GO:1903076] | axon [GO:0030424]; basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; early endosome [GO:0005769]; neurofilament [GO:0005883]; recycling endosome [GO:0055037] | amyloid-beta binding [GO:0001540]; AP-1 adaptor complex binding [GO:0035650]; AP-2 adaptor complex binding [GO:0035612]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphotyrosine residue binding [GO:0001784]; signaling adaptor activity [GO:0035591]; signaling receptor complex adaptor activity [GO:0030159] | PF00640; | 2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C142}. | null | null | null | null | null | FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytosis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface (By similarity). Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (PubMed:23836931). {ECO:0000250|UniProtKB:Q8C142, ECO:0000269|PubMed:23836931}. | Rattus norvegicus (Rat) |
D3ZAW2 | PISD_RAT | MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; | lipid droplet formation [GO:0140042]; mitochondrial protein catabolic process [GO:0035694]; phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540]; regulation of mitochondrion organization [GO:0010821] | lipid droplet [GO:0005811]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | phosphatidylserine decarboxylase activity [GO:0004609] | PF02666; | null | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. | SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}. Cytoplasm {ECO:0000250|UniProtKB:Q9UG56}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:6862014}.; SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UG56}. Lipid droplet {ECO:0000250|UniProtKB:Q9UG56}. Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions. {ECO:0000250|UniProtKB:Q9UG56}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for phosphatidylserine {ECO:0000269|PubMed:2618245}; Vmax=77 nmol/h/mg enzyme {ECO:0000269|PubMed:2618245}; | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis. {ECO:0000305|PubMed:2618245}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:2618245}; | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity). {ECO:0000250|UniProtKB:A0A8H4BVL9, ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245}. | Rattus norvegicus (Rat) |
D3ZAZ5 | BCAR3_RAT | MAAGKFASLPRHMPVNHQFPLASSMDLLSSKSPLAEHRTEAYPDVSIHGTLPRKKKGPPPIRSCDSASHMGTLPHSKSPRQSSPLTQDLILEKPLPDWKGDSFAFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSFAEGRPDVVKRLSLTTGGIQARDHSLPRGNLLRNKDKSGSQPACLDHVQDRKAATLKAHQSESHLPIGCKLPPQSPSVDTSPCPNSPVFRTGSEPTLSPALVRRFSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPPSPSPWLNSEANYCELNPAFAVGCDRGAKLLSQALDSHEMLLTAKQNGASGPRNSGINYSILDGDDQGRHWDPLAVQTDEGQEDETKFVPPVMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDMKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAMELKDTMGDLYSFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASSVSVPLLMPLVTLMERQAVTFEGTDMWEKNDESCEIMLSHLATARFMAEASESYRMNAERVLADFQPDEEMTEILKTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL | null | null | endothelin receptor signaling pathway [GO:0086100]; epidermal growth factor receptor signaling pathway [GO:0007173]; insulin receptor signaling pathway [GO:0008286]; lens morphogenesis in camera-type eye [GO:0002089]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of GTPase activity [GO:0043547]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; small GTPase-mediated signal transduction [GO:0007264] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; membrane [GO:0016020] | guanyl-nucleotide exchange factor activity [GO:0005085]; kinase binding [GO:0019900]; phosphotyrosine residue binding [GO:0001784] | PF00617;PF00017; | 1.10.840.10;3.30.505.10; | null | PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q9QZK2}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}. | null | null | null | null | null | FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promotes insulin-mediated membrane ruffling (PubMed:24216110). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (By similarity). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB/SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). {ECO:0000250|UniProtKB:O75815, ECO:0000250|UniProtKB:Q9QZK2, ECO:0000269|PubMed:24216110}. | Rattus norvegicus (Rat) |
D3ZB51 | TUTLB_RAT | MIWYVATLIASVISTRGLVAQVAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLSASGKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLTVQYPARVLNMPPVIYVPVGIHGYIRCPVDAEPPATVVKWNKDGRPLQVEKNLGWTLMEDGSIRIEEATEEALGTYTCVPYNTLGTMGQSAPARLVLKDPPYFTVLPGWEYRQEAGRELLIPCAAAGDPFPVITWRKVGKPSRSKHNALPSGSLQFRALSKEDHGEWECVATNVVTSITASTHLTVIGTSPHAPGSVRVHVSMTTANVSWEPGYDGGYEQTFSVWMKRAQFGPHDWLSLSVPLGPSWLLVDSLEPETAYQFSVLAQNRLGTSAFSEVVTVNTLAFPVTTPEPLVLVTPPRCLTANRTQQGVLLSWLPPANHSFPIDRYIMEFRVGERWEMLDDAIPGTDGEFFAKDLSQDTWYEFRVLAVMQDLISEPSNIAGVSSTDIFPQPDLTDDGLARPVLAGIVATICFLAAAILFSTLAACFVNKQRKRKLKRKKDPPLSITHCRKSLESPLSSGKVSPESIRTLRAPSESSDDQGQPAAKRMLSPTREKELSLYKKTKRAISSRKYSVAKAEAEAEATTPIELISRGPDGRFVMGPSEMEPSVKGRRIEGFPFAEETDMYPEFRQSDEENEDPLVPTSVAALKPQLTPMSSSQDSYLPPPAYSPRFQPRGLEGPSGLGGRLQATGQARPPAPRPFQHGQYYGYLSSSSPGEVEPPPFYMPEVGSPLSSVMSSPPLHTEGPFGHPTIPEENGENASNSTLPLTQTPTGGRSPEPWGRPEFPFGGLETPAMMFPHQLHPCDVAESLQPKPCLPRGLPPAPLQVPAAYPGMLSLEAPKGWVGKSPGRGPIPAPPATKWQERPMQPLVSQGQLRHTSQGMGIPVLPYPEPAEPGGHGGPSTFGLDTRWYEPQPRPRPSPRQARRAEPSLHQVVLQPSRLSPLTQSPLSSRTGSPELAARARPRPGLLQQAEMSEITLQPPAAVSFSRKSTPSSTGSPSQSSRSGSPSYRPTMGFTTLATGYPSPPPGPAPPAPGDNLDVFGQTPSPRRMGEEPLRPEPPTTLPTSG | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; nervous system development [GO:0007399]; positive regulation of inhibitory postsynaptic potential [GO:0097151]; synaptic membrane adhesion [GO:0099560] | dendrite [GO:0030425]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; postsynaptic specialization of symmetric synapse [GO:0099629] | kinase binding [GO:0019900] | PF13895;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, Turtle family | PTM: N-glycosylated and sialylated. Not significantly O-glycosylated. {ECO:0000269|PubMed:23751499}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:23751499}; Single-pass membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000269|PubMed:23751499}. | null | null | null | null | null | FUNCTION: Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development (PubMed:23751499). May mediate homophilic cell adhesion (By similarity). {ECO:0000250|UniProtKB:E9PZ19, ECO:0000269|PubMed:23751499}. | Rattus norvegicus (Rat) |
D3ZB94 | GFRAL_RAT | MLVFIFLAVRLSSENESSSQTNDCAYFMRQCLTDTDGCKQSWRSMEDACLVSGDSCKINNPLPCNLSIQSLVEKHFQFKGCLCTDDLHCTVNKIFGKKCTNKTDSMKKDNKYKRNLTTPLYHDTGFKQMQSCLEVTEACVGDVVCNAQLALYLKACTANGNLCDVKHCQAAIRFFYQNMPFNTAQMLAFCDCAQSDIPCQQSKETLHSKPCALNVVPPPTCLSVIHTCRNDELCRTYYRTFQTECWPHVAGKCREDETCISMLGKQDLTCSGSDSCRAAYLGTFGTVLQVPCACRSITQGEEPLCMAFQHMLHSKSCFNYPTPNVKDISSYERKHSKEITLTGFNSPFSGELIYVVVCMVVTSGILSLVMLKLRIPSKKRDPAPIEIAGAVIIQ | null | null | GDF15-GFRAL signaling pathway [GO:0160144]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; negative regulation of appetite [GO:0032099]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; reduction of food intake in response to dietary excess [GO:0002023]; stress-activated protein kinase signaling cascade [GO:0031098] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | glial cell-derived neurotrophic factor receptor activity [GO:0016167]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor activity [GO:0038023] | PF02351; | null | GDNFR family | PTM: Cleaved and inactivated by MMP14, inhibiting the GDF15-GFRAL aversive response. {ECO:0000250|UniProtKB:Q6UXV0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28846098}; Single-pass membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:28846098}. | null | null | null | null | null | FUNCTION: Brainstem-restricted receptor for GDF15 hormone, which triggers an aversive response, characterized by nausea, vomitting, and/or loss of appetite in response to various stresses (PubMed:28846098, PubMed:28846099, PubMed:31928886, PubMed:37060902). The aversive response is both required to reduce continuing exposure to those stresses at the time of exposure and to promote avoidance behavior in the future (By similarity). The GDF15-GFRAL aversive response is triggered by stresses, such as anticancer drugs (camptothecin or cisplatin), cancers or drugs such as metformin (PubMed:37060902). Upon interaction with its ligand, GDF15, mediates the GDF15-induced autophosphorylation and activation of the RET tyrosine kinase receptor, leading to activation of MAPK- and AKT- signaling pathways (By similarity). Ligand-binding activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem (By similarity). The GDF15-GFRAL signal induces expression of genes involved in metabolism, such as lipid metabolism in adipose tissues (By similarity). {ECO:0000250|UniProtKB:Q6SJE0, ECO:0000269|PubMed:28846098, ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:31928886, ECO:0000269|PubMed:37060902}. | Rattus norvegicus (Rat) |
D3ZBE5 | NEK7_RAT | MDEQPQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRASCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALDHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNICINPDPEKRPDIAYVYDVAKRMHACTASS | 2.7.11.34 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8TD19}; | cellular response to potassium ion [GO:0035865]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; protein phosphorylation [GO:0006468]; regulation of mitotic cell cycle [GO:0007346] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molecular function activator activity [GO:0140677]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | PTM: Phosphorylation at Ser-195 required for its activation. {ECO:0000250|UniProtKB:Q8TDX7}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TDX7}. Note=Present at centrosome throughout the cell cycle. Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (By similarity). Interaction with ANKS3 prevents its translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8TDX7}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.34; Evidence={ECO:0000269|PubMed:11516946}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q8TDX7}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.34; Evidence={ECO:0000269|PubMed:11516946}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q8TDX7}; | null | null | null | null | FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:11516946). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (By similarity). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity). Phosphorylates RPS6KB1 (PubMed:11516946). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (By similarity). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (By similarity). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (By similarity). {ECO:0000250|UniProtKB:Q8TDX7, ECO:0000269|PubMed:11516946}. | Rattus norvegicus (Rat) |
D3ZBN0 | H15_RAT | MSETAPAETTAPAPVEKSPAKKKTKKAGAAKRKATGPPVSELITKAVSASKERGGVSLPALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKVASGEAKPKAKKTGAAKAKKPTGATPKKPKKTAGAKKTVKKTPKKAKKPAAAGVKKVTKSPKKAKAAAKPKKATKSPARPKAVKSKASKPKVTKPKAAKPKAAKVKKAVSKKK | null | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; establishment of protein localization to chromatin [GO:0071169]; muscle organ development [GO:0007517]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; protein stabilization [GO:0050821] | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P16401}.; PTM: Citrullination at Arg-53 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000250|UniProtKB:P43276}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P16401}. Chromosome {ECO:0000250|UniProtKB:P16401}. Note=Mainly localizes with heterochromatin (By similarity). Associates with actively transcribed chromatin and not heterochromatin (By similarity). {ECO:0000250|UniProtKB:P16401}. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZBP4 | MICA1_RAT | MASPTSTNPAHDHFETFVQAQLCQDVLSSFQGLCRALGVESGGGLPQYHKIKAQLNYWSAKSLWAKLDKRASQPAYQQGQACTNTKCLVVGAGPCGLRAAVELALLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGFTFTGLQPPPKKGSGWRARIQPSPPAQLASYEFDVLISAGGGKFVPEGFTIREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQKFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLRQDLPETDQLLGKANVVPEALQQFARAAADFATQGKLGKLEFAQDARGRPDVAAFDFTSMMRSESSARIQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGTGPLELLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVQDLYDIMDKEHARKKSDETDARKTTTGSAGTEELLHWCQEQTAGFPGVSVTDFSSSWADGRALCALVHRLQPGLLEPSELQGMSALEATAWALRVAEYELGIIPVLSAQAVVAGSDPLGLIAYLSHFHSAFKNTPHSSGLVSQPHGTPSAILFLGKLQRSLQRTRTKVEEETPCTEEPPVSEPSVPPALPSEHEEAGAEDVCELCGKRLYILERFCVDGHFFHRGCFCCRTCEATLRPGGYGQYPGDGYFYCLQHLPQEDQKEADNNGSPENQELPTPGDSTTQSGPSSPVPPVTEASPVPSPSQPARRLIRLSSVERLRLSSLNIIPDSGVEPPPKPPRSCLDLAQESLKSSFMGWGVLRAPQVPEAIEKGEEEEEEEEEEEEEEEELPPPLALEVEQSLLTLAKNSGDMTKYPTWRRTLMRRAKEEEMKRFCKAQAIQRRLNEIEAAMRELETEGMKLEVALRKESSSPEKQKKLWLEQLLQLIQKKNSLVTEEAELMITVQELDLEEKQRQLDHEFRGINREETLKTQADRLSEDRVLRKLLDVVNQRDALIQFQEERRLREMPV | 1.14.13.225; 1.6.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; | actin filament depolymerization [GO:0030042]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein phosphorylation [GO:0001933]; regulation of regulated secretory pathway [GO:1903305]; sulfur oxidation [GO:0019417] | actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; hippocampal mossy fiber expansion [GO:1990026]; intercellular bridge [GO:0045171]; midbody [GO:0030496] | actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; NADPH oxidase H202-forming activity [GO:0106294]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; small GTPase binding [GO:0031267] | PF12130;PF00307;PF01494;PF00412; | 1.10.418.10;2.10.110.10;3.50.50.60; | Mical family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDZ2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDZ2}. Endosome membrane {ECO:0000250|UniProtKB:Q8TDZ2}. Midbody {ECO:0000250|UniProtKB:Q8TDZ2}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044, ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.225; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; | null | null | null | null | FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of secretory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels. May act as Rab effector protein and play a role in vesicle trafficking. Promotes endosomal tubule extension by associating with RAB8 (RAB8A or RAB8B), RAB10 and GRAF (GRAF1/ARHGAP26 or GRAF2/ARHGAP10) on the endosomal membrane which may connect GRAFs to Rabs, thereby participating in neosynthesized Rab8-Rab10-Rab11-dependent protein export (By similarity). {ECO:0000250|UniProtKB:Q8TDZ2}. | Rattus norvegicus (Rat) |
D3ZCM3 | ABCG4_RAT | MAEKALEAVGCGLGPGAVAMAVALEDGAEPPVLTTHLKKVENHITEAQRFSHLPKRSAVDIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAHGGRTVICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPMLFRAVQNGLCTMAEKKSSPEKNEVPAHCPTCPPELDPIESHTFATSTLTQFCILFRRTFLSILRDTVLTHLRFMSHVLIGVLIGLLYLHIGDDASKVFNNTGFLFFSMLFLMFAALMPTVLTCELICLAKMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALSIATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGLILTIYGMERGHLTCLEDHCPFRDPQIILHELDVEEAKLYMDFLVLGIFFLALRLLAYLVLRYRVKSER | 7.6.2.- | null | cellular response to high density lipoprotein particle stimulus [GO:0071403]; cellular response to leukemia inhibitory factor [GO:1990830]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of cholesterol efflux [GO:0010875]; regulation of DNA-templated transcription [GO:0006355]; sterol transport [GO:0015918]; transmembrane transport [GO:0055085] | cytoplasmic vesicle [GO:0031410]; endosome [GO:0005768]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886] | ABC-type sterol transporter activity [GO:0034041]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Eye pigment precursor importer (TC 3.A.1.204) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H172}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91WA9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; Evidence={ECO:0000250|UniProtKB:Q91WA9}; CATALYTIC ACTIVITY: Reaction=ATP + desmosterol(in) + H2O = ADP + desmosterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:67932, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91WA9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67933; Evidence={ECO:0000250|UniProtKB:Q91WA9}; | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL) (By similarity). May play an important role in the removal of amyloid-beta peptides from brain,in a process that can be antagonized by desmosterol. However it is unclear whether ABCG4 can directly transport amyloid-beta peptides or whether peptide export may be facilitated due to changes in the membrane lipid environment (By similarity). Induces apoptosis in various cells (By similarity). {ECO:0000250|UniProtKB:Q91WA9, ECO:0000250|UniProtKB:Q9H172}. | Rattus norvegicus (Rat) |
D3ZD32 | CHD5_RAT | MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKAKRKKRDEDEEDNEDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQPLPVRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEPEDSDLDNASIHSSSVRSECSAALGKKNKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDEEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPEVEPGMPPPRPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMVHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDEIDIPYYDNLKQTYWGHRELMLGEDARLPKRLVKKGKKLKDDKQEKPPDTPIVDPTVKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRGGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPMLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPTTPIPDVQSTKGGSLAAGAKKKHGGTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREVIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLVPEGPEGKKPGEVISSDPNTPVPASPAQLPPAPLGLPDKMEAQLGYTDEKESGTQKPKKSLEIQALPTALDRVEAEDKHQSSDSKDRAREERMEEVEKAQGSPEQPLKEETLPDKEPVPDKLELSLSHSNDFRPDDPKAEEKEPTETQQNGDREEDEEGKKEDKNGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYEIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEVHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQGAFGSSQMYNNSFGPNFRGPGPGGIVNYNQMPLGPYVTGR | 3.6.4.12 | null | cerebral cortex neuron differentiation [GO:0021895]; chromatin remodeling [GO:0006338]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; regulation of cell differentiation [GO:0045595]; regulation of transcription by RNA polymerase II [GO:0006357]; sperm DNA condensation [GO:0035092]; transcription by RNA polymerase II [GO:0006366] | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; NuRD complex [GO:0016581] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; H3K27me3 modified histone binding [GO:0061628]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872] | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | PTM: Methylated at Gln-1388 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21931736}. Chromosome {ECO:0000250|UniProtKB:A2A8L1}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. {ECO:0000250|UniProtKB:A2A8L1, ECO:0000269|PubMed:21931736}. | Rattus norvegicus (Rat) |
D3ZDI6 | MYLIP_RAT | MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVGKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNDQSPPSSPLKSSDSSMSCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI | 2.3.2.27 | null | cholesterol homeostasis [GO:0042632]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of neuron projection development [GO:0010977]; nervous system development [GO:0007399]; positive regulation of protein catabolic process [GO:0045732]; protein destabilization [GO:0031648]; protein ubiquitination [GO:0016567]; regulation of low-density lipoprotein particle receptor catabolic process [GO:0032803]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF09380;PF00373;PF09379;PF13920; | 1.20.80.10;2.30.29.30;3.30.40.10; | null | PTM: Autoubiquitinated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WY64}. Cell membrane {ECO:0000250|UniProtKB:Q8WY64}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR. {ECO:0000250|UniProtKB:Q8BM54}. | Rattus norvegicus (Rat) |
D3ZDK2 | UB2D1_RAT | MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM | 2.3.2.23; 2.3.2.24 | null | negative regulation of TORC1 signaling [GO:1904262]; positive regulation of protein polyubiquitination [GO:1902916]; positive regulation of protein ubiquitination [GO:0031398]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51668}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51668}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:P51668, ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P51668}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4 (By similarity). Mediates ubiquitination of PEX5. {ECO:0000250|UniProtKB:P51668, ECO:0000269|PubMed:18359941}. | Rattus norvegicus (Rat) |
D3ZDK7 | PGP_RAT | MAEAEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMGPEAGLEVFGTAYCSALYLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADLLPALQG | 3.1.3.21; 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8}; | glycerol biosynthetic process [GO:0006114]; glycerophospholipid metabolic process [GO:0006650]; negative regulation of gluconeogenesis [GO:0045721] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ADP phosphatase activity [GO:0043262]; glycerol-1-phosphatase activity [GO:0000121]; glycerol-3-phosphatase activity [GO:0043136]; magnesium ion binding [GO:0000287]; phosphoglycolate phosphatase activity [GO:0008967]; protein tyrosine phosphatase activity [GO:0004725] | PF13344;PF13242; | 3.40.50.1000; | HAD-like hydrolase superfamily, CbbY/CbbZ/Gph/YieH family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:26755581}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:26755581}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=47 nmol/min/mg enzyme with glycerol-3-phosphate as substrate {ECO:0000269|PubMed:26755581}; | null | null | null | FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol (PubMed:26755581). Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (By similarity). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity). {ECO:0000250|UniProtKB:A6NDG6, ECO:0000250|UniProtKB:Q8CHP8, ECO:0000269|PubMed:26755581}. | Rattus norvegicus (Rat) |
D3ZDM7 | OXDD_RAT | MDTVRIAVVGAGVIGLSTAACVSQLVPRCSVTVISDRFTPDTTSNVAAGMLIPPTYPDTPVPTLKRWFRETFQHLSEIARSAEAVDAGIHLVSGWQIFRSVPTEEVPFWADVVLGFREMTEAELKRFPQYEFGQAFTTLKCETSAYLPWLEKRIKGSGGLLLTRRIEDLWELQPSFDIVVNCSGLGSRRLVGDATVSPVRGQVLQAQAPWVKHFIRDGGGLTYVYPGTSYVTLGGSRQTGDWNLSPDAELSREIFSRCCALEPSLHRACDIKEKVGLRPSRPGVRLQKEILVRGEQRLPVVHNYGHGSGGISVHWGSALEATRLVMECVHTLRTPASLSKL | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32376478}; | aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; D-amino acid catabolic process [GO:0019478]; grooming behavior [GO:0007625]; hormone metabolic process [GO:0042445]; insemination [GO:0007320]; nervous system process [GO:0050877]; regulation of cell communication [GO:0010646] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:12209855, ECO:0000269|PubMed:1991137}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99489}. Note=Active in the peroxisomal matrix. {ECO:0000250|UniProtKB:Q99489}. | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32376478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12513; Evidence={ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32376478}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000250|UniProtKB:Q99489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000250|UniProtKB:Q99489}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.26 mM for D-aspartate (at 37 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:25747990}; Note=kcat is 31.1 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3). {ECO:0000269|PubMed:25747990}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3-12.5. {ECO:0000269|PubMed:29292239}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:29292239}; | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:1991137, PubMed:25747990, PubMed:29292239, PubMed:32376478). Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity). Protects the organism from the toxicity of D-amino acids (PubMed:7903300). May also function in the intestine (By similarity). {ECO:0000250|UniProtKB:Q922Z0, ECO:0000269|PubMed:1991137, ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32376478, ECO:0000269|PubMed:7903300}. | Rattus norvegicus (Rat) |
D3ZE55 | PCDH8_RAT | MSPVKRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQSPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSESAPVGTRIPLEVPVDEDVGANGLQSVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQASYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFTFGARTPPEARHLFRLDPRSGRLTLAGQVDYERQDTYELDVRAQDRGPGPRTATCKVIVRIRDVNDNAPDISITPLAAPGAPATSPFAAAAAAAALGGADAASSAGSGTQETGVTSLVPEGAARESLVALVSTSDRDSGANGQVRCALYGHEHFRLQPAYAGSYLVVTAASLDRERIAEYNLTLVAEDRGAPPLRTVRPYTVRVGDENDNAPLFTKPVYEVSVRENNPPGAYLATVAARDPDLGRNGQVTYRLVEAEVGRSGEAVSTYVSVDPATGAIYALRSFDYETLRQLDVRVQASDGGSPQLSSNALVQVRVLDQNDHSPVLVHPAPANGSLEVAVPGRSTKDTAVARIQARDADEGANGELAFDLLQQEPREAFSIGRHTGEIVLTGDLSQEPPGRVFKALLVISDGGRPPLTTTATVSFVVTAGGGSAVPASAGSPEHFRPPGSRLAPSGPSLQWDTPLIVIIVLAGSCTLLLAAIIAIATTCNRRKKEVRKGGALREERPGAAGGGASAPGSPDETARGTGPRPNMFDVLTFPGSGKAPFGSPAADAPPPAVAAAEVPGSEGGSATGESACHFEGQQRLRGAHAEPYSASPGFGKEPAPPVAVWKGHSFNTISGREAEKFSGKDSGKGDSDFNDSDSDISGDALKKDLINHMQSGLWACTAECKILGHSDRCWSPSCAGPNTHPPPHPPAQMSTFCKSTSLPRDPLRRDNYYQAQLPKTVGLQSVYEKVLHRDYDRTVTLLSPPRPGRLPDLQEIGVPLYESPPGGRYVSPKKGTNENV | null | null | cell adhesion [GO:0007155]; chemical synaptic transmission [GO:0007268]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; long-term memory [GO:0007616]; modulation of chemical synaptic transmission [GO:0050804]; morphogenesis of embryonic epithelium [GO:0016331]; regulation of synaptic membrane adhesion [GO:0099179]; somitogenesis [GO:0001756] | dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | calcium ion binding [GO:0005509] | PF00028;PF08266; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:10383464}. Presynaptic cell membrane {ECO:0000269|PubMed:10383464}. Postsynaptic cell membrane {ECO:0000269|PubMed:10383464}. Note=Also expressed in the cell bodies of neurons of the hippocampus and cortex. Localized to excitatory, but not with inhibitory, synapses. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein. May play a role in activity-induced synaptic reorganization underlying long term memory. Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis. {ECO:0000269|PubMed:10383464, ECO:0000269|PubMed:17988630}. | Rattus norvegicus (Rat) |
D3ZEF4 | CUL7_RAT | MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDSSQVDCKAEHILLWMTDDEIYANCHKMLGEDGQVIRPSQESAEAGALDKSVLGEMETDVKSLIQRALRQLEECVGAVPPAPLLHTVHVLSAYASIEPLTGVFKDRRVLDLVMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLPQVPGRLLFSLVKRYLCVTFLLDRLNGNAEDQDAQNNFIPEELNAGRGRVELEFSMAMGTLISELVQAMRWDWASSRSESSSPIFQPPPTEFFRPRAQRFRRSRRFRPRTAFASVNTYALYVRDTLRPGMRVRMLEDFEEISAGDEGQFRQSNDGMPPVQVLWDSTGHTYWVHWHMLEILGFEEDIEDVVDIDDQGAMVHGGLGVAPPFQHWKPIAQLFAEPYVVPEEEDREEREHLTQAEWWELFFFIKKLNAEERQHVVELLQEFLEGEHVLDFEILPELTVPVELAQDLMLSLPQQLDDSALRDLFNCYVYRKYGPEVLVGKRNRPFVLDDQLNLFRIETDSEAQDPPSQSASPALRQLVEGLGPSGKLLVDLERALSSEAPQENEVKPCLLQLQEEPQPFLTLMRSLDTPASNKALHLTALRILMQLVNFPEALLLPWHEAMDACMTCLRSPNTDREVLQELIFFLHRLTSTSRDYAVILNQLGARDAISKVLEKHRGKLELAQELRDMVFKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFDVFLRYLCQGSSAEVKKNKYWEKVEVSSNPHRASRLTDRNAKTYWESNGTAGSHFITVHMRPGVLIRQLTLLVAGEDSSYMPAWVVVCGGDSISSVNTELNAVNVMPHASRVILLENLTRFWPIVQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRQEQNFADRFLPDEEAALALSKTCWEALVSPLVQNITSPDEDSTSSLGWLLNQYLECREAAYNPQSRAAAFSSRVRHLTHLLVHVEPCEAAPPVVAISQSKGRNRSHDWSSLTTRGLPSSIMRNLTRCWRSVVEEQVNKFLTSSWKDDDFVPRYCERYYILQKSSSELFGPRAAFLLAMRNGCADALLRLPFLRAAHVSEQFARHIDQRIQGSRMGGARGMEMLAQLQRCLESVLILSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPGRLPQQMLQTLNISEELQRRFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGKEHKSKKEDAAGETAAVAMADEEEEEGKKEEGEEEEGEGEEELEEEEERYYEGTMPEVCVLVLSPRFWPVASVCHMLNPTTCLPSYLRGTINHYSNFYSKSQSHSGLEKESPRQLQWTWQGRAEVQFGDQILHVSTVQMWLLLHLNHLKAVSVESLQALSELPPEVLNKAIGPLTSSRGPLDLQEQKNIPGGVLKIRDDSEEPRPRRGNVWLIPPQTYLKAEDEEGRNLEKRRNLLNCLVVRILKAHGDEGLHIDQLVHLVLEAWEKGPCPPRGLVSSLGRGAACRSSDVLSCILHLLGKGTLRRHDDRPQMLFYAVPITVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTGTQTFSTFR | null | null | epithelial to mesenchymal transition [GO:0001837]; Golgi organization [GO:0007030]; microtubule cytoskeleton organization [GO:0000226]; mitotic cytokinesis [GO:0000281]; placenta development [GO:0001890]; positive regulation of dendrite morphogenesis [GO:0050775]; protein ubiquitination [GO:0016567]; regulation of mitotic nuclear division [GO:0007088]; ubiquitin-dependent protein catabolic process [GO:0006511]; vasculogenesis [GO:0001570] | 3M complex [GO:1990393]; centrosome [GO:0005813]; Cul7-RING ubiquitin ligase complex [GO:0031467]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471] | ubiquitin protein ligase binding [GO:0031625] | PF03256;PF11515;PF00888; | 2.30.30.30;2.60.120.260;1.10.10.10; | Cullin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21572988}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. {ECO:0000250}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:21572988}. | null | null | FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). {ECO:0000250, ECO:0000269|PubMed:21572988}. | Rattus norvegicus (Rat) |
D3ZEH5 | SIDT2_RAT | MIAWRLPLCVLLVAAVESHLGALGPKNVSQKDAEFERTYADDVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGLYQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVNRVDNFVLRTGELFTFNTTAAQPQYFKYEFPDGVDSVIVKVTSKKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFVEDEPVDQGHRQKTLSVLVSQAVTSEAYVGGMLFCLGIFLSFYLLTVLLACWENWRQRKKTLLVAIDRACPESGHPRVLADSFPGSAPYEGYNYGSFENGSGSTDGLVESTGSGDLSYSYQDRSFDPVGARPRLDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLCVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLYALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSVIHIISTLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYTDRMVLLVMGNIINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVLLTLDDDLDTVQRDKIYVF | null | null | cell morphogenesis [GO:0000902]; glucose homeostasis [GO:0042593]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; response to glucose [GO:0009749]; RNA catabolic process [GO:0006401]; RNA transport [GO:0050658]; type B pancreatic cell development [GO:0003323]; type B pancreatic cell proliferation [GO:0044342] | lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | AP-1 adaptor complex binding [GO:0035650]; AP-2 adaptor complex binding [GO:0035612]; DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; nucleic acid transmembrane transporter activity [GO:0051032]; RNA transmembrane transporter activity [GO:0051033] | PF13965; | null | SID1 family | PTM: Glycosylated. {ECO:0000269|PubMed:20965152}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBJ9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBJ9}. Cell membrane {ECO:0000250|UniProtKB:Q8NBJ9}. Note=Mainly localizes to lysosomes and only partly to the plasma membrane (By similarity). Lysosomal localization is required for SIDT2-mediated intracellular degradation of endogenous RNA (By similarity). {ECO:0000250|UniProtKB:Q8CIF6, ECO:0000250|UniProtKB:Q8NBJ9}. | null | null | null | null | null | FUNCTION: Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. Involved in the uptake of single-stranded oligonucleotides by living cells, a process called gymnosis (By similarity). In vitro, mediates the uptake of linear DNA more efficiently than that of circular DNA, but exhibits similar uptake efficacy toward RNA and DNA. Binds long double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than 100 bp (By similarity). {ECO:0000250|UniProtKB:Q8CIF6, ECO:0000250|UniProtKB:Q8NBJ9}. | Rattus norvegicus (Rat) |
D3ZEN0 | MILK2_RAT | MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFNALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVALKIPDRLSILTYVSQYYNYFHGRSPIGGMAGMKRPSSDSTEELSGKKKVPSQPAKLSSPVPTQRLPLSPARTNPVVQRNEGVSERPSPKAAPGTVGSSVSSICGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHHSSEAVSVSPKLSNLASRQPGGGIADTRPIGVSQKVLETNGEATPLRARTAAWEHAGGNRAAKGFVQTELTPPATSRVHVGSPAGPRLPMSTVTTTSANSKATTHVTNSSPVGWSSSAQSSTGTSGSRPVVSPSALGAHLSVPQGQAASKGVKTQLNSSTDSSSTAPTPAWTSSSSRTQQAREKFFHNLSPAPAPAPASSSSSHASRVPTVVTAPSGKVSPLVNTSTSKVPSATVVTVPTSKASTVVTAPTSKAPTVVTVPISKAPTVVTAPTSKVSTVVTVPTSKASTVVTAPTSKASTVVTVPTGRGHVVVNTSASKVSGVVDNPAQESSREQALSVLRKALPGLTRAGSQAPSRSSPATSSVLITLPKNEVPPKVPSAKLSHSTTQAFSPTPKMEPTAPLSVGSTSWTSVSLQAGKKSPGISPGIGKTSAVSRPQAEVKGTSGPGPTSQEGQEEGPEGWRARLKPVDKSIPSARALEQKEPVLAEPRAGDTPRKASSSSDSSIHITLTPIQQKRTPCLADSGSSLAAPSPPSRRKKLVVPPTLDVSADWLQPELKKQDDQTRSCKEKTATWGTRESSAILDNDLVSPDEAVTSPVRLHPNYISQEELQRQLQDIERQLDALELRGVELEKRLRAAEGDASEDGLMVDWFRLIHEKQLLLRRESELMYKSKDQCLEERQLDLQGELRRLMEKPEGLKSPQDRKREQELLNQYVNTVNDRSDIVDNLDEDRLREQEEDQMLESMIQNLGLQRKKSKSFLSKIWSSKSKSGQT | null | null | actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; bicellular tight junction assembly [GO:0070830]; endocytic recycling [GO:0032456]; neuron projection development [GO:0031175]; substrate adhesion-dependent cell spreading [GO:0034446] | actin filament bundle [GO:0032432]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | actin filament binding [GO:0051015]; actinin binding [GO:0042805]; filamin binding [GO:0031005]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF12130;PF00307;PF00412; | 1.10.418.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell projection {ECO:0000269|PubMed:20008558}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth. {ECO:0000269|PubMed:20008558}. | Rattus norvegicus (Rat) |
D3ZER2 | BFSP2_RAT | MSERRVAMDLPSGSNASMPLQRHRVSSLRGTRSPSSLDSPPASRTSAVGSLVRAPGVYVGVAPSGGIGGLGARVTRRALGISSVFLQGLRSSGLATAPAPGPERNHATAEDLGGCLVEYMTKVHALEQVSQELETQLRAHLESKAKRSGGWDALRASWASSYQQVGEAVLENARLMLQMETIQAGADDFKERYENEQPFRKAAEEEVSSLYKVIDEANLTKTDLEHQIESLKEELGSLSRSYEEDVKVLYKQLAGSELEQTDVPMGTGLDDVLETIRVQWERDVEKNRAEAGAVLQAKQQTEVVHVSQTQEEKLAAALSVELHDTSRQVQSLQAETESLRALKRGLENTLHDAKHWHDMELQNLGAVVGRLEAELAEIHSETEQQQQERAHLLACKGQLQKDVASYHALLDREESN | null | null | cell maturation [GO:0048469]; cytoskeleton organization [GO:0007010]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109]; lens fiber cell development [GO:0070307]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | structural constituent of eye lens [GO:0005212] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18449355}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm {ECO:0000269|PubMed:18449355}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q28177}. Note=Expressed primarily at the plasma membrane in peripheral lens fiber cells, however also localizes to the cytoplasm in mature lens fiber cells. {ECO:0000250|UniProtKB:Q28177}. | null | null | null | null | null | FUNCTION: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Plays a role in maintenance of retinal lens optical clarity (By similarity). {ECO:0000250|UniProtKB:Q6NVD9}. | Rattus norvegicus (Rat) |
D3ZEY4 | DGKQ_RAT | MATAAESGARTWPGSGSPRLGSPAGSPVLGISGRARPGSGPERTGRAIGSVAPGHSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKQVKTPCTSIAPSLVRVPVAHCFGSLGLYKRKFCVVCRKSLEVPAFRCEVCELHVHPDCVPFACSDCRQCHQDGQHDYDTYHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSVCSTALTPECTFGRLRSMVLPPSCVRLLSRNFSKMHCFRIPETMVLELGDGDDGLDGSAAVGTGREVSAATESTKQTLKIFDGNDSMRKNQFRLVTVSRLARNEEVMEAALRAYYINEDPKDFQLQALPLTLLSGNAQALGKAGTTEEETSKDSGPGDSVPEAWVIRSLPRTQEILKIYPDWLKVGVAYVSIRVNSQSTARSVVQEVLPLFGRQVEDQERFQLIEVLMSSRQVQRTVLVDEEPLLDRLRDIRQTSVRQASQTRFYVAEARAVTPHVSLFVGGLPPGLSPQDYSNLLHEAMATKAAVVSVSHVYSLQGAVVLDVTCFAEAERLYMLARDTAVHGRPLTALVLPDVLHTKLPPDCCPLLVFVNPKSGGLKGRELLCSFRKLLNPHQVFELTNGGPLPGFHLFSQVPCFRVLVCGGDGTVGWVLAALEETRRHLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLVSVDEADAVLMDRWTILLDAHEIDSTENNVVETEPPKIVQMNNYCGIGIDAELSLDFHQAREEEPGKFTSRFHNKGVYVRVGLQKISHSRSLHKEIRLQVEQQEVELPSIEGLIFINIPSWGSGADLWGSDSDSRFEKPRIDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWIQAPGHMIISATAPKVHMLRKAKQKPRKAGAIRDTRVDTLPAPEGNPL | 2.7.1.107; 2.7.1.93 | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP-mediated signaling [GO:0019933]; diacylglycerol metabolic process [GO:0046339]; G protein-coupled receptor signaling pathway [GO:0007186]; glycerolipid metabolic process [GO:0046486]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; negative regulation of gene expression [GO:0010629]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; phosphatidic acid biosynthetic process [GO:0006654]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; protein kinase C signaling [GO:0070528]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of cholesterol metabolic process [GO:0090181]; regulation of cortisol biosynthetic process [GO:2000064]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of gluconeogenesis [GO:0006111]; regulation of progesterone biosynthetic process [GO:2000182]; regulation of synaptic vesicle endocytosis [GO:1900242]; regulation of TORC1 signaling [GO:1903432]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ATP [GO:0033198]; response to cAMP [GO:0051591]; thrombin-activated receptor signaling pathway [GO:0070493] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; vesicle membrane [GO:0012506] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; DNA-binding transcription factor binding [GO:0140297]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; phospholipase binding [GO:0043274]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297] | PF00130;PF00609;PF00781;PF00788; | 2.60.200.40;3.30.60.20; | Eukaryotic diacylglycerol kinase family | PTM: Phosphorylated by PRKCE and PRKCH in vitro. {ECO:0000250|UniProtKB:P52824}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52824}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P5E8}. Cell membrane {ECO:0000250|UniProtKB:P52824}. Synapse {ECO:0000250|UniProtKB:Q6P5E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus {ECO:0000269|PubMed:15337525}. Nucleus speckle {ECO:0000269|PubMed:15337525}. Nucleus matrix {ECO:0000269|PubMed:15337525}. Note=Translocates to the plasma membrane in response to steroid hormone receptor stimulation. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH. Translocates to the nucleus in response to thrombin stimulation (By similarity). Association with the nuclear matrix is regulated by nerve growth factor (PubMed:15337525). {ECO:0000250|UniProtKB:P52824, ECO:0000269|PubMed:15337525}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:15337525}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000305|PubMed:15337525}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014, ChEBI:CHEBI:456216; EC=2.7.1.93; Evidence={ECO:0000250|UniProtKB:P52824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938; Evidence={ECO:0000250|UniProtKB:P52824}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595, ChEBI:CHEBI:73332, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P52824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073; Evidence={ECO:0000250|UniProtKB:P52824}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15337525}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000305|PubMed:15337525}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P52824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673; Evidence={ECO:0000250|UniProtKB:P52824}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936, ChEBI:CHEBI:78385, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P52824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677; Evidence={ECO:0000250|UniProtKB:P52824}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P52824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000250|UniProtKB:P52824}; | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:15337525}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:15337525). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:15337525). Within the adrenocorticotropic hormone signaling pathway, produces phosphatidic acid which in turn activates NR5A1 and subsequent steroidogenic gene transcription (By similarity). Also functions downstream of the nerve growth factor signaling pathway being specifically activated in the nucleus by the growth factor (PubMed:15337525). Through its diacylglycerol activity also regulates synaptic vesicle endocytosis (By similarity). {ECO:0000250|UniProtKB:P52824, ECO:0000269|PubMed:15337525}. | Rattus norvegicus (Rat) |
D3ZF77 | AK1CA_RAT | MDLKHSRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY | 1.1.1.-; 1.1.1.216 | null | steroid metabolic process [GO:0008202] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; farnesol dehydrogenase activity [GO:0047886]; ketosteroid monooxygenase activity [GO:0047086]; steroid dehydrogenase activity [GO:0016229] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH; Xref=Rhea:RHEA:14697, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:16619, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.216; Evidence={ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for 4-nitrobenzaldehyde {ECO:0000269|PubMed:17574202}; KM=3.1 uM for benzaldehyde {ECO:0000269|PubMed:17574202}; KM=20 uM for pyridine-4-aldehyde {ECO:0000269|PubMed:17574202}; KM=25 uM for 2-phenyl-2-propenal {ECO:0000269|PubMed:17574202}; KM=2.4 uM for NADP(+) {ECO:0000269|PubMed:17574202}; KM=1430 uM for NAD(+) {ECO:0000269|PubMed:17574202}; KM=0.6 uM for NADPH {ECO:0000269|PubMed:17574202}; KM=43 uM for NADH {ECO:0000269|PubMed:17574202}; KM=0.3 uM for 1-decanal {ECO:0000269|PubMed:17574202}; KM=0.9 uM for 1-nonanal {ECO:0000269|PubMed:17574202}; KM=1.1 uM for 1-octanal {ECO:0000269|PubMed:17574202}; KM=1.1 uM for 1-hexanal {ECO:0000269|PubMed:17574202}; KM=112 uM for D-lactoaldehyde {ECO:0000269|PubMed:17574202}; KM=125 uM for L-lactoaldehyde {ECO:0000269|PubMed:17574202}; KM=225 uM for 4-methylpentanal (isocaproaldehyde) {ECO:0000269|PubMed:17574202}; KM=0.4 uM for all-trans-retinal {ECO:0000269|PubMed:17574202}; KM=3.5 uM for trans-2,4-nonadienal {ECO:0000269|PubMed:17574202}; KM=3.3 uM for trans-2-nonenal {ECO:0000269|PubMed:17574202}; KM=2.3 uM for 9-cis-retinal {ECO:0000269|PubMed:17574202}; KM=2.5 uM for 4-hydroxy-2-nonenal (HNE) {ECO:0000269|PubMed:17574202}; KM=0.8 uM for 6-tert-butyl-2,3-epoxy-4-benzoquinone (TBE) {ECO:0000269|PubMed:17574202}; KM=2.7 uM for 1,4-naphthoquinone {ECO:0000269|PubMed:17574202}; KM=14 uM for 5-hydroxy-1,4-naphthoquinone (juglone) {ECO:0000269|PubMed:17574202}; KM=22 uM for 1-indanone {ECO:0000269|PubMed:17574202}; KM=22 uM for 3-hydroxy-2-butanone {ECO:0000269|PubMed:17574202}; KM=0.5 uM for 1H-indole-2,3-dione (isatin) {ECO:0000269|PubMed:17574202}; KM=0.6 uM for 16-ketoestrone {ECO:0000269|PubMed:17574202}; KM=2 uM for 2,3-hexanedione {ECO:0000269|PubMed:17574202}; KM=5.5 uM for butane-2,3-dione (diacetyl) {ECO:0000269|PubMed:17574202}; KM=16 uM for methylglyoxal {ECO:0000269|PubMed:17574202}; KM=30 uM for 21-dehydrocortisol {ECO:0000269|PubMed:17574202}; KM=12 uM for S-indan-1-ol {ECO:0000269|PubMed:17574202}; KM=32 uM for farnesol {ECO:0000269|PubMed:17574202}; KM=5.6 uM for farnesal {ECO:0000269|PubMed:17574202}; KM=16 uM for geranylgeraniol {ECO:0000269|PubMed:17574202}; KM=0.2 uM for geranylgeranial {ECO:0000269|PubMed:21187079}; KM=15 uM for 1-nonanol {ECO:0000269|PubMed:17574202}; KM=8.2 uM for 1-decanol {ECO:0000269|PubMed:17574202}; KM=11 uM for 5-beta-androstane-3,17-dione (etiocholanedione) {ECO:0000269|PubMed:17574202}; KM=8.7 uM for 5-alpha-androstane-3,17-dione (androstanedione) {ECO:0000269|PubMed:17574202}; KM=5.6 uM for 4-androstene-3,17-dione {ECO:0000269|PubMed:17574202}; KM=36 uM for 5-alpha-androstan-3alpha-ol-17-one {ECO:0000269|PubMed:17574202}; KM=8.7 uM for 5-beta-androstan-3alpha-ol-17-one {ECO:0000269|PubMed:17574202}; KM=8.5 uM for 5-beta-androstane-3alpha,17beta-diol {ECO:0000269|PubMed:17574202}; KM=12 uM for 5-beta-androstan-17beta-ol-3-one {ECO:0000269|PubMed:17574202}; KM=6.9 uM for 5-alpha-androstane-3-alpha,17-beta-diol {ECO:0000269|PubMed:17574202}; KM=18 uM for testosterone {ECO:0000269|PubMed:17574202}; KM=18 uM for 5-alpha-androstan-17beta-ol-3-one {ECO:0000269|PubMed:17574202}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 for the dehydrogenase activity. Optimum pH is 6 for the reductase activity. {ECO:0000269|PubMed:17574202}; | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of substrates including aromatic and aliphatic aldehydes, quinones, ketones, dicarbonyl compounds and 17-ketosteroids (PubMed:17574202). Catalyzes the NADP(+)-dependent oxidation of aromatic, alicyclic and aliphatic alcohols, and 17beta-hydroxysteroids (PubMed:17574202). To a lesser extent, can also catalyze the reduction of some aldoses and ketoses and the oxidation of some sugar alcohols (PubMed:17574202). In the stomach, lung and colon tissues, mediates the reduction of farnesal and geranylgeranial into farnesol and geranylgeraniol respectively (PubMed:21187079). By reducing 4-hydroxy-2-nonenal (HNE), produced during lipid peroxidation, into 1,4-dihydro-2-nonene (DHN), protects vascular endothelial cells from damage elicited by oxidized lipoproteins (PubMed:21187080). {ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079, ECO:0000269|PubMed:21187080}. | Rattus norvegicus (Rat) |
D3ZF92 | TNR21_RAT | MGTSASSITALASCSRIAGQVGATMVAGSLLLLGFLSTITAQPEQKTLSLTGTYRHVDRTTGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPSGTFTRHENGIERCHDCSQPCPRPMIERLPCAALTDRECICPPGMYQSNGTCAPHTVCPVGWGVRKKGTENEDVRCKQCARGTFSDVPSSVMKCRAHTDCLGQNLMVVKQGTKETDNVCGVHLSSSSTTPSSPGIATFSHPEHTESHDVPSSTYEPQGMNSTDSNSTASVRTKVPSDIQEETVPDNTSSTSGKESTNRTLPNPPQLTHQQGPHHRHILKLLPSSMEATGEKSSTAIKAPKRGHPRQNPHKHFDINEHLPWMIVLFLLLVLVLIVVCSIRKSSRTLKKGPRQDPSAIMEKAGLKKSLTPTQNREKWIYYRNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNVKLENSTLLTVEPSPLDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHILNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL | null | null | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; B cell apoptotic process [GO:0001783]; cellular response to tumor necrosis factor [GO:0071356]; humoral immune response [GO:0006959]; myelination [GO:0042552]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of myelination [GO:0031642]; negative regulation of T cell proliferation [GO:0042130]; neuron apoptotic process [GO:0051402]; oligodendrocyte apoptotic process [GO:0097252]; regulation of oligodendrocyte differentiation [GO:0048713]; T cell receptor signaling pathway [GO:0050852] | axon [GO:0030424]; plasma membrane [GO:0005886] | null | PF00531;PF00020; | 1.10.533.10;2.10.50.10; | null | PTM: Oxidized in response to reactive oxygen species (ROS), leading to endocytosis. {ECO:0000250|UniProtKB:O75509}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75509}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75509}. Note=Endocytosed following oxidation in response to reactive oxygen species (ROS). {ECO:0000250|UniProtKB:O75509}. | null | null | null | null | null | FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B (By similarity). Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm (By similarity). Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning (By similarity). Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP) (By similarity). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity). Negatively regulates oligodendrocyte survival, maturation and myelination (PubMed:21725297). Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation (By similarity). Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells (By similarity). Negatively regulates the production of IgG, IgM and IgM in response to antigens (By similarity). May inhibit the activation of JNK in response to T-cell stimulation (By similarity). Also acts as a regulator of pyroptosis: recruits CASP8 in response to reactive oxygen species (ROS) and subsequent oxidation, leading to activation of GSDMC (By similarity). {ECO:0000250|UniProtKB:O75509, ECO:0000269|PubMed:21725297}. | Rattus norvegicus (Rat) |
D3ZFB6 | PRRT2_RAT | MAASSSEVSEMKGVEDSSNTHSEGPRHSEEGMGPVQVVAENLDQPEALQSGPDTTAAPVDSGPKAELAPETTETPVETPETVQATDLSVNPGEDSKTCPSPKEACQEPASRPEVNREATAEQGAEQQSAAPPEPTSEQALQLNTQSDPQPTSQPPPKPPLQAEPPTQENPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK | null | null | negative regulation of short-term synaptic potentiation [GO:1905513]; negative regulation of SNARE complex assembly [GO:0035544]; neuromuscular process controlling posture [GO:0050884]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629] | axon terminus [GO:0043679]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; vesicle [GO:0031982] | SH3 domain binding [GO:0017124]; syntaxin-1 binding [GO:0017075] | PF04505; | null | CD225/Dispanin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon {ECO:0000250|UniProtKB:Q7Z6L0}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:27172900}. Postsynaptic density membrane {ECO:0000269|PubMed:27172900}. Cell projection, dendritic spine {ECO:0000269|PubMed:27172900}. | null | null | null | null | null | FUNCTION: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation. {ECO:0000250|UniProtKB:E9PUL5}. | Rattus norvegicus (Rat) |
D3ZFD0 | MY18A_RAT | MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSMRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSIILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLMQHSGLGIPRPGPRSRVPELVTKRFPADLRLPALVPPPPPALRELELQRRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRTGEGHRREPTDAKTEEQIAAEEAWYETEKVWLVHRDGFSLASQLKSEELSLPEGKVRVKLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSSQHLVQYLATIAGTSGNKVFSVEKWQALATLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASVQTMLLEKLRVARRPASEATFNVFYYLLACGDSTLRTELHLNHLAENNVFGIVPLSKPEEKQRAAQQFSKLQTAMKVLAISPEEQKACWLILASIYHLGAAGATKAVFSCGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGLGEGTGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQKLFHERTFLQELERYKEDNIELAFDDLEPVTDDSVAAVDQASHQSLVRSLAHADEARGLLWLLEEEALVPGATEDTLLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQNSVVECLPSKRKALGSVLSSEKKKRKKKKKKKCPESANSVAHTYSLSTQTLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRSASSRRVSSSSELDLPPGDPCEAGLLQLDVSLLRAQLRGSRLLDAIRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIMVDEKRAVEELLESLDLEKSSCCMGLSRVFFRAGTLARLEEQRDEETSRHLTLFQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDEEIQQLRNKLEKVEKERNELRLNSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEAMDMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQNRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLRQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQLEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLESMASRLKENMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKRKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDGSLKSSSPTSHWKSLAPDLSDDEHDPVDSISRPRFSHNYLSDSDTEAKLTETNA | null | null | actomyosin structure organization [GO:0031032]; asymmetric Golgi ribbon formation [GO:0090164]; canonical NF-kappaB signal transduction [GO:0007249]; cell migration [GO:0016477]; cellular response to type II interferon [GO:0071346]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; Golgi vesicle budding [GO:0048194]; negative regulation of apoptotic process [GO:0043066]; positive regulation of opsonization [GO:1903028]; positive regulation of protein secretion [GO:0050714]; regulation of macrophage activation [GO:0043030] | actomyosin [GO:0042641]; brush border [GO:0005903]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi membrane [GO:0000139]; microtubule organizing center [GO:0005815]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; phagocytic vesicle [GO:0045335]; trans-Golgi network [GO:0005802] | actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; cytoskeletal motor activity [GO:0003774] | PF00063;PF01576;PF00595; | 1.10.10.820;1.20.5.340;1.20.58.530;2.30.42.10;3.30.70.1590;3.40.850.10;1.20.120.720;4.10.270.10;1.20.5.1160; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92614}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92614}. Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Note=Recruited to the Golgi apparatus by GOLPH3 (By similarity). Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (PubMed:31522887). {ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:31522887}. | null | null | null | null | null | FUNCTION: May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (By similarity). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking. Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages. Strongly enhances natural killer cell cytotoxicity (By similarity). {ECO:0000250|UniProtKB:Q92614, ECO:0000250|UniProtKB:Q9JMH9}. | Rattus norvegicus (Rat) |
D3ZFJ3 | 3BP1_RAT | MMKRQLHRMRQLAHTGSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYANYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAAPFSRVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEVLIQNADTLFPGDINFSVSGIFSGLAPQEKPNSQQVSEELAPVAVPATAATPTPTPAPTPAPASMTVKERTESELPKPASPKVSRSPTDTTALAEDMTRKTKRPAPARPTMPPPQPSSSRSSPPALSLPAGSVSPGTPQALPRRLVGTSLRAPTVPPPLPPAPPQPARRQSRRLPVSPCPASPVISNMPAQVDQGAATEDRGGPEAVGGHPPTPVLPPQPRPRGLISETD | null | null | actin filament organization [GO:0007015]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; establishment of epithelial cell apical/basal polarity [GO:0045198]; filopodium assembly [GO:0046847]; negative regulation of small GTPase mediated signal transduction [GO:0051058]; phagocytosis, engulfment [GO:0006911]; positive regulation of GTPase activity [GO:0043547]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of actin filament depolymerization [GO:0030834]; regulation of blood vessel endothelial cell migration [GO:0043535]; regulation of Rac protein signal transduction [GO:0035020]; ruffle assembly [GO:0097178]; semaphorin-plexin signaling pathway [GO:0071526] | adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell leading edge [GO:0031252]; cytosol [GO:0005829]; exocyst [GO:0000145]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic cup [GO:0001891] | GTPase activator activity [GO:0005096]; semaphorin receptor binding [GO:0030215]; SH3 domain binding [GO:0017124] | PF03114;PF00620; | 1.20.1270.60;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:21658605}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9Y3L3}. Nucleus {ECO:0000250|UniProtKB:Q9Y3L3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3L3}. Note=Localizes at the leading edge of migrating cells (PubMed:21658605). Accumulation at forming phagocytic cups is PI3 kinase/bPI3K-dependent and is specific for sites of large particles engagement and their phosphatidylinositol 3,4,5-triphosphate membrane content (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3, ECO:0000269|PubMed:21658605}. | null | null | null | null | null | FUNCTION: GTPase activating protein/GAP which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration (PubMed:21658605). Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3, ECO:0000269|PubMed:21658605}. | Rattus norvegicus (Rat) |
D3ZG27 | UBIA1_RAT | MAAVQAPGEKINIQAGETTQVGDTDQQRNDWPEEDRLPERSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSQGVLDPRLLLGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVRFGVFLYTLGCVCAAYLYYLSTLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLVILITFGPLAVMFAYAVQVGSLAIFPLVYAIPLALSTEAILHSNNTRDMESDREAGIVTLAILIGPTLSYILYNTLLFLPYLIFTILATHCSISLALPLLTSPMAFSLERQFRSQAFNKLPQRTAKLNLLLGLFYVFGIILAPAGSLPRL | 2.5.1.-; 2.5.1.39 | null | circulatory system development [GO:0072359]; endothelial cell development [GO:0001885]; menaquinone biosynthetic process [GO:0009234]; phylloquinone biosynthetic process [GO:0042372]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate [GO:0032194]; vitamin K biosynthetic process [GO:0042371] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; antioxidant activity [GO:0016209]; prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-hydroxy-3-all-trans-decaprenylbenzoate + diphosphate; Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}. | null | null | FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress. {ECO:0000250|UniProtKB:Q9Y5Z9}. | Rattus norvegicus (Rat) |
D3ZG83 | M3K10_RAT | MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPTDLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREGSSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGSSGGSGTWSRSGPPKKEELVGGKKKGRTWGPSSTLQKERAGGEERLKALGEGSKQWSSSAPNLGKSPKHTPMAPGFASLNEMEEFAEADEGNNVPPSPYSTPSYLKVPLPAEASPCAQPPWEPPAATPSRPGHGARRRCDLALLGCATLLSAVGLGADVAEARAGDGEEQRGWLDGLFFPRPGRFPRGLSPTGRPGGRREETAPGFGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPTAPSPPPSLLPPSPSTNPLVDVELESFKKDPRQSLTPTHVTAAHAVSRGHRRTPSDGALRQREPPELTNHGPRDPLDFPRLPDPQALFPTRRRPLEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLSISPPSRPDTPESPGPLSVQPTLLDMDMEGQSQDNTVPLCGAYGSH | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | negative regulation of DNA-templated transcription [GO:0045892]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JNK cascade [GO:0046330]; smoothened signaling pathway [GO:0007224] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; bHLH transcription factor binding [GO:0043425]; JUN kinase kinase kinase activity [GO:0004706]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transcription corepressor activity [GO:0003714] | PF07714;PF14604; | 2.30.30.40;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; | null | null | null | null | FUNCTION: Activates the JUN N-terminal pathway. {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZGB1 | NFAT5_RAT | MPSDFISLLSADLDLESPKSLYSRDSLKLHPSQNFHRAGLLEESVYDLLPKELQLPPPRETSAASMSQTSGGEAGSPPPAVVAADASSAPSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTGNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLDSQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKEVDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCTQPAGVPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVGIYVVTNAGRSHDVQPFTYTPDPAAGALSVNVKKEISSPARPCSFEEALKAMKTTGCNVDKVTILPNALITPLISSSMIKTEDVTPMEVTSEKRSSPIFQTTKTVGSTQQTLETISNIAGNASFSSPSSSHLSPENENQQQLQPKAYNPETLTTIQTQDISQPGTFPAVSASSQLPSSDALLQQAAQFQTRDAQSRDTMQSDSVVNLSQLTEAPQQQQSPLQEQAQIPSNIFPSPNSVSQLQSTIQQLQAGSFTGSTASGSNGSVDLVQQVLEAQQQLSSVLFSTPDGNENVQEQLNADIFQVSQIQNSVSPGMFSSTESAVHTRPDNLLPGRADSVHQQTENTLSSQQQQQQQQQQQQQQQVIESSAAMVMEMQQSICQAAAQIQSELFPSAASANGSLQQSPVYQQPSHMMSALPTSEDMQMQCELFSSPPAVSGNETSTTTTPQVATPGSTMFQPPNSGDGEETGAQAKQIQSSVFQTMVQMQHSGDSQPQVNLFSSTKNIMSVQSNGTQQQGNSLFQQGSEMLSLQSGSFLQQSSHSQAQLFHPQNPIADAQSLSQETQGPMFHSANPIVHSQTSTASSEQLQPSMFHSQSTIAVLQGSSVPQDQQSPNIYLSQSSISNLQTNTVAQEEQISFFSAQNSISPLQSTSNTEQQAAFQQQPPISHIQTPLLSQEQAQPSQQGLFQPQVALGSLPANPMPQNQQGPIFQTQRPIVGMQSNSPSQEQQQQQQQQQQQQQQQQQQSILFSNQNAMATMASQKQPPPNMIFSPNQNPMASQEQQNQSIFHQQSNMAPMNQEQQPMQFQNQPTVSSLQNPGPTPSESPQTSLFHSSPQIQLVQGSPSSQEQQVTLFLSPASMSALQTSINQPDMQQSPLYSPQNNIPGIQGSTSSPQPQAALFHNTTGGTINQLQNSPGSSQQTSGMFLFGIQNNCSQLLTSGPATLPEQLMAINQPGQPQNEGQSSVTTLLSQQMPESAPLASSVNNSQNMEKIDLLVSLQSQGNNLTGSF | null | null | calcineurin-NFAT signaling cascade [GO:0033173]; cellular response to cytokine stimulus [GO:0071345]; DNA damage response [GO:0006974]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of transcription by RNA polymerase II [GO:0045944]; R-loop processing [GO:0062176]; regulation of calcineurin-NFAT signaling cascade [GO:0070884]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated. Phosphorylated at Thr-152 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization. {ECO:0000250|UniProtKB:O94916}.; PTM: Poly-ADP-ribosylated by PARP1 in response to DNA damage, promoting recruitment to sites of R-loop-associated DNA damage. {ECO:0000250|UniProtKB:O94916}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23233732}. Cytoplasm {ECO:0000269|PubMed:23233732}. Chromosome {ECO:0000250|UniProtKB:O94916}. Note=Nuclear distribution increases under hypertonic conditions (By similarity). Recruited to sites of R-loop-associated DNA damage following poly-ADP-ribosylation by PARP1 (By similarity). {ECO:0000250|UniProtKB:O94916, ECO:0000250|UniProtKB:Q9WV30}. | null | null | null | null | null | FUNCTION: Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes (PubMed:23233732). Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3'. Mediates the transcriptional response to hypertonicity. Positively regulates the transcription of LCN2 and S100A4 genes; optimal transactivation of these genes requires the presence of DDX5/DDX17. Also involved in the DNA damage response by preventing formation of R-loops; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity). {ECO:0000250|UniProtKB:O94916, ECO:0000269|PubMed:23233732}. | Rattus norvegicus (Rat) |
D3ZGQ5 | NEK8_RAT | MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNIHTDVGSVRMRRAEKCLTPGTPMAPGSTGSRATSARCRGVPRGPVRPAIPPPLSSVYAWGGGLSIPLRLPMPNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGTGGGTLLPGAVELPQPQFVSRFLEGQSGVTIKHVACGDLFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSADGELFAWGRGDGGRLGLGTRESHNCPQQVPMVPGQEAQRVVCGIDCSMILTSPGRVLACGSNRFNKLGLDCLSLEEEPVPHQQVEEALSFTPLGSAPLDRETLLCVDLGTAHSAAVTASGACYTFGSNQHGQLGTSSRRVSRAPCRVQGLEGIKMVMVACGDAFTVAIGAEGEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | animal organ morphogenesis [GO:0009887]; determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; phosphorylation [GO:0016310]; regulation of hippo signaling [GO:0035330] | centrosome [GO:0005813]; ciliary base [GO:0097546]; ciliary inversin compartment [GO:0097543]; cilium [GO:0005929]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00415; | 2.130.10.30;1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZR4}. Cell projection, cilium {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q86SG6}. Note=Predominantly cytoplasmic. Localizes to the proximal region of the primary cilium and is not observed in dividing cells (By similarity). {ECO:0000250|UniProtKB:Q91ZR4}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia. Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZGS3 | OCRL_RAT | MEPRLPIGAQPLACLHMVAGLEMKGPLREPCVLTLARRNGQYELIIQLHGKEQHVQDIIPINSHFRCVQEAEETLLIDIASNSGCKIRVQGDWTRERHFEIPDEERCLKFLSEVLAAQEAQSQLLVPEQKDSSNWYQKLDTKDKPAYSGLLGFEDNFSSMNLDKKMNTQNPPTGIHREPPPPPSSNRMLPREKEALNKEQPKVTNTMRKLFAPNSQSGQREGLIKHILAKREKEYVNIQSFRFFVGTWNVNGQSPDSSLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWAMAVERGLPSKAKYKKVQLVRLVGMMLLVFAKKDQCQYIRDIATETVGTGIMGKMGNKGGVAMRFVFHNTTFCIVNSHLAAHVEEFERRNQDYKDICARMSFSVPNQTLPQVNIMKHDVVIWLGDLNYRLCMPDANEVKSLINKNELQKLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYDSKTDRWDSSGKCRVPAWCDRILWRGINVNQLHYRSHMELKTSDHKPVSALFHIGVKVVDERRYRKVFEDIVRIMDRMENDFLPSLDLSRREFMFENVKFRQLQKEKFQISNNGQVPCHFSFIPKLNDTQYCKPWLRAEPFEGYLEPNETIDISLDVYVSKDSVTILNSGEDKIEDILVLHLDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQMVPLDEGTSERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETIPGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAHDPRICKQVISQLPRCHRNVFRYLMAFLRELLKFSDYNNVSTNMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLVFLLGSEED | 3.1.3.36; 3.1.3.56; 3.1.3.86 | null | cilium assembly [GO:0060271]; in utero embryonic development [GO:0001701]; phosphatidylinositol dephosphorylation [GO:0046856]; signal transduction [GO:0007165] | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; nucleus [GO:0005634]; phagocytic vesicle membrane [GO:0030670]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | GTPase activator activity [GO:0005096]; inositol phosphate phosphatase activity [GO:0052745]; inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; small GTPase binding [GO:0031267] | PF21310;PF16726;PF00620; | 2.30.29.110;3.60.10.10;2.60.40.10;1.10.555.10; | Inositol 1,4,5-trisphosphate 5-phosphatase type II family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q01968}. Early endosome membrane {ECO:0000250|UniProtKB:Q01968}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium {ECO:0000250|UniProtKB:Q01968}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19795375}. Endosome {ECO:0000269|PubMed:19795375}. Cytoplasmic vesicle {ECO:0000269|PubMed:19795375}. Note=Also found on macropinosomes. {ECO:0000250|UniProtKB:Q01968}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniProtKB:Q01968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765; Evidence={ECO:0000250|UniProtKB:Q01968}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000250|UniProtKB:Q01968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529; Evidence={ECO:0000250|UniProtKB:Q01968}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414; EC=3.1.3.56; Evidence={ECO:0000250|UniProtKB:Q01968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393; Evidence={ECO:0000250|UniProtKB:Q01968}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:203600; EC=3.1.3.56; Evidence={ECO:0000250|UniProtKB:Q01968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19798; Evidence={ECO:0000250|UniProtKB:Q01968}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2. Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of inositol 1,3,4,5-tetrakisphosphate. Regulates traffic in the endosomal pathway by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with endosomes. Involved in primary cilia assembly. Acts as a regulator of phagocytosis, hydrolyzing PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K signaling. {ECO:0000250|UniProtKB:Q01968}. | Rattus norvegicus (Rat) |
D3ZHA0 | FLNC_RAT | MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNVGMALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDNTFRCTYRPVMEGPHTVHVAFAGAPITRSPFPVHVAEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVIPGKYVVTITWGGYAIPRSPFEVQVSPEAGAQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDRGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHIQPAPPDCFPDKVKAFGPGLEPTGCIVDRPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTVIISWGGVNVPKSPFRVNVGEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGHYTIMVLFANQEIPASPFHIKVDPSHDASKVKAEGPGLSRTGVEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNVAPPLDLSKVKVQGLNSKVAVGEEQAFLVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGSGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEGVLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATIQPVFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPIPKFPTRVHVQPAVDTSGIKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGVTEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYVPFTPGDYDVNITFGGQPIPGSPFRVPVKDVVDPGKVKCSGPGLGTGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKVLPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHALPTGDASKCLVTVSIGGHGLGACLGPRIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLACDPLPHVEEPAEVLQLHQPYAPLRPGTCPTHWATEEPVVPVEPLESMLRPFNLVIPFTVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVDAINSGHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKITGDDSMRTSQLNVGTSTDVSLKITEGDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILVGPSEIGDASKVRVWGKGLSEGQTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKVTGEGRMKESITRRRQAPSIATIGSTCDLNLKIPGNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEGEASSQDMTAQVTSPSGKTEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTVGPLGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPVASLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNVP | null | null | muscle cell development [GO:0055001]; sarcomere organization [GO:0045214] | costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; ankyrin binding [GO:0030506]; cytoskeletal protein binding [GO:0008092] | PF00307;PF00630; | 1.10.418.10;2.60.40.10; | Filamin family | PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme. Targeting to developing and mature Z lines is mediated by the intradomain insert (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Muscle-specific filamin, which plays a central role in sarcomere assembly and organization. Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events. {ECO:0000250|UniProtKB:Q14315}. | Rattus norvegicus (Rat) |
D3ZHH1 | DLL4_RAT | MTPGSRSACRWALLLLAVLWPQQRAAGSGIFQLRLQEFANERGMLANGRPCEPGCRTFFRICLKHYQATFSEGPCTFGNVSTPVLGTNSFVIRDKNSGSGRNPLQLPFNFTWPGTFSLNIQAWHTPGDDLRPETSPGNSLISQIIIQGSLAVGKNWKSDEQNNTLTRLRYSYRVVCSDNYYGDSCSRLCKKRDDHFGHYECQPDGSLSCLPGWTGKYCDQPICLSGCHEQNGYCSKPDECNCRPGWQGPLCNECIPHNGCRHGTCTIPWQCACDEGWGGLFCDQDLNYCTHHSPCKNGSTCSNSGPRGYTCTCLPGYTGEHCELELSKCASNPCRNGGSCKDHENSYHCLCPPGYYGQHCEHSTLTCADSPCFNGGSCRERNQGASYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRTCRCRPGFTGTHCELHISDCARSPCAHGGTCHDLENGPVCTCPAGFSGRRCEVRITNDACASGPCFNGATCYTGLSPNNFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLVVLLVLLVMVAVAVRQLRLRRPDDDSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKLQNHTLDYNLAPGFLGRGSTPGKYPHSDKSLGEKVPLRLHSEKPACRISAICSPRDSMYQSVCLISEERNECVIATEV | null | null | angiogenesis [GO:0001525]; aortic valve morphogenesis [GO:0003180]; blood vessel lumenization [GO:0072554]; blood vessel remodeling [GO:0001974]; branching involved in blood vessel morphogenesis [GO:0001569]; cardiac atrium morphogenesis [GO:0003209]; cardiac ventricle morphogenesis [GO:0003208]; cellular response to cholesterol [GO:0071397]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to hypoxia [GO:0071456]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; chondrocyte differentiation [GO:0002062]; dorsal aorta morphogenesis [GO:0035912]; luteolysis [GO:0001554]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of gene expression [GO:0010629]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; Notch signaling pathway [GO:0007219]; pericardium morphogenesis [GO:0003344]; positive regulation of gene expression [GO:0010628]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of neural retina development [GO:0061074]; regulation of neurogenesis [GO:0050767]; T cell differentiation [GO:0030217]; ventral spinal cord interneuron fate commitment [GO:0060579]; ventricular trabecula myocardium morphogenesis [GO:0003222] | plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018] | PF01414;PF00008;PF12661;PF21795;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25700513}; Single-pass type I membrane protein {ECO:0000255|RuleBase:RU280815}. | null | null | null | null | null | FUNCTION: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4 (PubMed:25700513). Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate (By similarity). {ECO:0000250|UniProtKB:Q9JI71, ECO:0000250|UniProtKB:Q9NR61, ECO:0000269|PubMed:25700513}. | Rattus norvegicus (Rat) |
D3ZHP7 | ULK3_RAT | MAGSGWGLPRLDGFILTERLGSGTYATVYKAYAKKATREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPSHRISFQDFFAHPWVDLEHMPSGESLAQATALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTTGQELLREMARDKPRLLAALEVASAAMAKEEEAGKEQDALDLYQHSLGELLLLLAAEAPGRRRELLHTEVQNLMARAEYLKEQIKIRESHWEAESLDKEGLSESVRSSCTLQ | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; fibroblast activation [GO:0072537]; negative regulation of smoothened signaling pathway [GO:0045879]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of smoothened signaling pathway [GO:0045880]; protein autophosphorylation [GO:0046777]; regulation of autophagy [GO:0010506]; response to starvation [GO:0042594]; reticulophagy [GO:0061709]; smoothened signaling pathway [GO:0007224] | autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF04212;PF00069; | 1.20.58.80;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | PTM: Autophosphorylated. Autophosphorylation is blocked by interaction with SUFU (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to pre-autophagosomal structure during cellular senescence. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZHR2 | ABCD1_RAT | MPVLSTPSRPSRVTTLKRTAVVLALTAYGVHKIYPLVRQCLTPARGPQVPAGESTQEASGATTAKAGMNRVFLQRLLVLLRLLFPGVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDMVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYAESDSEAMKKAALEMKEEELVSERTEAFTIARNLLTAAADATERIMSSYKEVTELAGYTARVYEMFQVFEDVQHCRFKRTGDLEEAQAGPGSMVHSGVHIEGPLKIQGQVVDVEQGIICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGISLLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQGRLQELRQILGEAAAPVQPLVPGIPT | 3.1.2.-; 7.6.2.- | null | fatty acid beta-oxidation [GO:0006635]; fatty acid elongation [GO:0030497]; fatty acid homeostasis [GO:0055089]; long-chain fatty acid catabolic process [GO:0042758]; long-chain fatty acid import into peroxisome [GO:0015910]; myelin maintenance [GO:0043217]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; neuron projection maintenance [GO:1990535]; peroxisome organization [GO:0007031]; positive regulation of fatty acid beta-oxidation [GO:0032000]; positive regulation of unsaturated fatty acid biosynthetic process [GO:2001280]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of fatty acid beta-oxidation [GO:0031998]; regulation of mitochondrial depolarization [GO:0051900]; regulation of oxidative phosphorylation [GO:0002082]; sterol homeostasis [GO:0055092]; very long-chain fatty acid catabolic process [GO:0042760]; very long-chain fatty acid metabolic process [GO:0000038]; very long-chain fatty-acyl-CoA catabolic process [GO:0036113] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | ABC-type fatty-acyl-CoA transporter activity [GO:0015607]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; enzyme binding [GO:0019899]; fatty acyl-CoA hydrolase activity [GO:0047617]; identical protein binding [GO:0042802]; long-chain fatty acid transporter activity [GO:0005324]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; very long-chain fatty acyl-CoA hydrolase activity [GO:0052817] | PF06472;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:12176987}. | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Lysosome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. | CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acid(in) + ATP + H2O = a very long-chain fatty acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58950, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12176987}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081; Evidence={ECO:0000305|PubMed:12176987}; CATALYTIC ACTIVITY: Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate; Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + tetracosanoate(in) = ADP + H(+) + phosphate + tetracosanoate(out); Xref=Rhea:RHEA:67088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate; Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + hexacosanoate(in) = ADP + H(+) + hexacosanoate(out) + phosphate; Xref=Rhea:RHEA:67084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31013, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+); Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784; Evidence={ECO:0000250|UniProtKB:P33897}; CATALYTIC ACTIVITY: Reaction=ATP + docosanoate(in) + H2O = ADP + docosanoate(out) + H(+) + phosphate; Xref=Rhea:RHEA:67092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67093; Evidence={ECO:0000250|UniProtKB:P33897}; | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (PubMed:12176987). Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (By similarity). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:25043761). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Controls also the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (By similarity). {ECO:0000250|UniProtKB:P48410, ECO:0000269|PubMed:12176987, ECO:0000269|PubMed:25043761}. | Rattus norvegicus (Rat) |
D3ZHS6 | BAP1_RAT | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNSMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRVKYEARLHVLKGNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPFGLEAGRTPAASECTHTDGAEEVAGSCPQTTTHSPPSKSKLVVKPSGSSLNGVPPTPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPQQYSDDEEDYEDEEEDVQNTSSAIRYKRKGTGKPGSLSNSSDGQLSVLQPNTINVLTEKLQESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSTRSSQGSQGSSSLEEKEVVEVTDSRDKSGLNRSSEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ | 3.4.19.12 | null | cell population proliferation [GO:0008283]; common myeloid progenitor cell proliferation [GO:0035726]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; gene expression [GO:0010467]; granulocyte differentiation [GO:0030851]; hematopoietic stem cell homeostasis [GO:0061484]; in utero embryonic development [GO:0001701]; leukocyte proliferation [GO:0070661]; macrophage homeostasis [GO:0061519]; mitotic cell cycle [GO:0000278]; monoubiquitinated protein deubiquitination [GO:0035520]; myeloid cell apoptotic process [GO:0033028]; negative regulation of DNA-templated transcription [GO:0045892]; neuron cellular homeostasis [GO:0070050]; neutrophil differentiation [GO:0030223]; nucleate erythrocyte differentiation [GO:0043363]; platelet morphogenesis [GO:0036344]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; regulation of cell cycle [GO:0051726]; regulation of cell growth [GO:0001558]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of inflammatory response [GO:0050727]; response to inorganic substance [GO:0010035]; thrombocyte differentiation [GO:0002574]; tissue homeostasis [GO:0001894]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PR-DUB complex [GO:0035517] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cysteine-type deubiquitinase activity [GO:0004843]; histone H2A deubiquitinase activity [GO:0140950] | PF01088;PF18031; | 1.20.58.860;3.40.532.10; | Peptidase C12 family, BAP1 subfamily | PTM: Ubiquitinated: monoubiquitinated at multiple site of its nuclear localization signal (NLS) BY UBE2O, leading to cytoplasmic retention. Able to mediate autodeubiquitination via intramolecular interactions to couteract cytoplasmic retention. {ECO:0000250|UniProtKB:Q92560}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O. {ECO:0000250|UniProtKB:Q92560}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. Acts as a tumor suppressor. {ECO:0000250|UniProtKB:Q92560}. | Rattus norvegicus (Rat) |
D3ZHV2 | MACF1_RAT | MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQKKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGESGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFPKVPEGGEGISATEVDSRWQEYQSRVDSLIPWIRQHTILMSDKSFPQNPVELKALYNQYIHFKETEILAKEREKGRIKELYKLLEVWIEFGRIKLPQGYHPNHVEEEWGKLIVEMLEREKSLRPAVERLELLLQIANKIQNGALNCEEKLTLAKNTLQADAAHLESGQPVQCESDVIMYIQECEGLIRQLQVDLQILRDEKYYQLEELAFRVMRLQDELVTLRLECTNLYRKGHFTSLELVPPSTLTTTHLKAEPLNKTTHSSSTSWFRKPMTRTELVAISSSEDEGSLRFVYELLSWVEEMQMKLERAEWGNDLPSVELQWETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYVETLGKLETQYCKLKETSSFRMRHLQSLHKFVSKATAELIWLNGKEEEELACDWSDSNPNISAKKAYFSELTMELEGKQDVFRSLQDTAELLSLENHPAKQTVEAYSAAVQSQLQWMKQLCLCVEQHIKENAAYFQFFSDARDLESFLRNLQDSIKRKYTCDHNTSLSRLEDLLQDSMDEKEQLIQSKSSVASLVGRSKTIVQLKPRNPDHVLKSTLSVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCLLIPPPNTEAIDVASRVEQSYQKVMALWHQLHINTKSLISWNYLRKDIDAVQTWNLEKLRSSAPGECHQVMKNLQAHYEDFLQDSHDSALFSVADRLRIEEEVEACKTHFQQLMESMENEDKEETLAKVYISELKNIRLRLEECEQRLLKQIQSSASSKTDRDARQDVALRIAEQEHVQEDLKHLRSDLDAVSVKCTTFLQQSPSGSSATTLRSELNLMVEKMDHVYGLSIVCLNKLKTIDVIVRSIQDAELLVKGYEIKLSQEEAVPADLSALESHRTTLQHWLSDVKDKNSVFSVLDEEISKAKAVAEQLHHRAAEPNLDLERYQEKGSQLQERWHRVIAQLETRQSEVESIQEVLRDYRACHGTLIKWIEETTAQQEMMKPGQAEDSRVLSEQLSQQTELFAEIERNQTKLDQCQKLSQQYSTTVKDYELQLMTYKAFVESQQKSPGKRRRMISSSDAITQEFMDLRTRYTALVTLTTQHVKYISDALRRLEEEEKVVEEEKQEHVEKVKDLLGWVSTLARNTQGTTTSSRTSASTDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEREKEQISEQLCALNKTYHDLCDGSANQLQQLQSELAQQTEQKTLQKQQDTCHKKLEDLRSWVRQAERALERHRGRASQQELSALQQNQSDLKDLQGDIQNHSTSFATAVKDIEGFLEENQNKLSPQELTALREKLYQAKEQYEGLQDRTREAQKELEEAVTSALQQETEKSKAATELAENRRKIDALLDWVTSVGSSDRQPQTSLPGTEQFSGACLEKQTLDATDGCVDVNQVPEKLDRQYELMKARHQELLSQQQNFIVATQSAQSFLDQHSHNLTPEERQMLQEKLGELKEQYAASLAQSEAKLRQTQTLRDELQKFLQDHREFENWLERSENELDGMHTGGSSPEALNSLLKRQGSFSEDVISHKGDLRFVTISGQKVLETENNFEEGQEPSPTRNLVNEKLKDATERYTTLHSKCTRLGSHLNMLLGQYQQFQSSADSLQAWMLTCEASVEKLLSDTVASDPGILQQQLATTKQLQEELAEHQVPVEKLQKAAHDLMDIEGEPSLDCTPIRETTESIFSRFQSLSCSLAERSALLQKAIAQSQSVQESMESLLQSMKEVEQNLEGEQVAALSSGLIQEALANNMKLKQDIARQKSSLEATREMVTRFMETADGNSAAVLQDRLAELSQRFHRLQLQQQEKESGLKKLLPQAETFEQLSSKLQQFVEHKNRLLASGNQPDQDIAHFSQHIQELTLEMEDQKENLGTLEHLVTALGSCGFALDLSQHQEKIQNLKKDFTELQKTVQEREKDASNCQEQLDEFRKLIRTFQKWLKETEGNVPPAETFVSAKELEKQIEHLKGLLDDWAGKGVLVEEINTKGTALESLIMDITAPDSQAKTGSVLPSVGSSVGSVNGYHTCKDLTEIQCDMSDVNSKYDKLGDALRERQESLQTVLSRMEEVQKEASSVLQWLESKEEVLKGMDASLSPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLEAYPNSQEAENWRKMQEDLNSRWEKATEVTVARQKQLEESASHLACFQAAESQLRPWLMEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLTEAAQGILTGPGDVSPSASQVHKDLQSISQKWVELTDKLNSRSTQIDQAIVKSTQYQDLLQDLSEKVKAVGQRLSGQSAISTQPDAVKQQLEETSEIRSDLGQLDDEMKEAQTLCQELSLLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDEKQSQQAKNCPISAKLERLQSQLQENEEFQKNLNQHSGSYEVIVAEGESLLLSVPPGEEKKTLQNQLVELKSHWEDLNKKTVDRQSRLKDCMQKAQKYQWHVEDLVPWIKDCKSKMSELQVTLDPVQLESSLLRSKAMLNEAEKRRSLLEILNSAADILINSSEIDEDEIRDEKAGLNQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLKAQREVLQALDPQVDYLRDFTRGLVEDAPDGSDASPLVHQAELAQQEFLEVKQRVNSSCLTMENKLEGIGQFHCRVREMFSQLADLDDELDGMGAIGRDTDSLQSQIEDIRLFLNKIQALRLDIEDSEAECRKMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYSKLKALNDAATAAEEGEALQWIVGTEVDVINQQLADFKMFQKEQVDPLQVKLQQVNGLGQGLIQSAGKTCDVQGLEHDMEEVNTRWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLTDTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQAAELADREKITGQLESLECRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIHQQIIRHKALEEEIENHAADVQQAVKIGQSLSSLICPAEQGIMSEKLDSLQARYSEIQDRCCRKASLLEQALFNARLFGEDEVEVLNWLAEVEDKLSAVFVKDYRQDVLQKQHADHLALNEEIINRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFHSTYEELTGWLREVEEELAASGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSHALLELVPWRAREGLDKLVSDANEQYKLVSDTVGQRVDEIDAAIQRSQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRGEIFSTCGEEQKAVLQEKTECLIQQYEAVSLLNSERYARLERAQVLVNQFWETYEELSPWAEETLALIAQLPPPAVDHEQLRQQQEEMRQLRESIAEHKPHIDKILKIGPQLKELNPEEGKMVEEKYQKAENMYAQIKDEVRQRALALDEAVSQSAQIAEFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNKSATMELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFFWEDIKARSEEREIKFLDVLELAEKFWYDMAALLTTIKDTQEIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVKKSIDEMNNAWENLNRTWKERLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIRLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEELMGWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTLQQAQGFHSEIEEFLLELNRMESQLSASKPTGGLPETAREQLDAHMELHSQLRAKEEIYNQLLDKGRLMLLSRGDSGSGSKTEQSVALLEQKWHVVSSKVEERKSKLEEALSLATEFQNSLQEFINWLTLAEQSLNIASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWKKLIDWLEDAESHLDSELEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTLLADDAQKLDNLLGEVRDKWDTVCGKSVERQHKLEEALLFSGQFMDALQALVDWLYKVEPQLAEDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIESSRDDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQALKQAEEFRDTVHMLLEWLSEAEQTLRFRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNAAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELLAWIQWAETTLIQRDQEPIPQNIDRVKALITEHQSFMEEMTRKQPDVDRVTKTYKRKNIEPTHAPFIEKSRSGSRKSLNQPTPPPMPILSQSEAKNPRINQLSARWQQVWLLALERQRKLNDALDRLEELKEFANFDFDVWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALHPNKDAYRPTTDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRARGRTNIELREKFILPEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR | null | null | cell migration [GO:0016477]; establishment or maintenance of cell polarity [GO:0007163]; Golgi to plasma membrane protein transport [GO:0043001]; intermediate filament cytoskeleton organization [GO:0045104]; mesoderm formation [GO:0001707]; positive regulation of axon extension [GO:0045773]; positive regulation of Wnt signaling pathway [GO:0030177]; post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; regulation of cell migration [GO:0030334]; regulation of epithelial cell migration [GO:0010632]; regulation of focal adhesion assembly [GO:0051893]; regulation of microtubule-based process [GO:0032886]; regulation of neuron projection arborization [GO:0150011]; Wnt signaling pathway [GO:0016055]; wound healing [GO:0042060] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intermediate filament [GO:0005882]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; structural molecule activity [GO:0005198] | PF00307;PF13499;PF02187;PF17902;PF00435;PF18373;PF21019;PF21020;PF21097; | 1.20.58.1060;1.20.58.60;1.10.418.10;1.10.238.10;3.30.920.20;2.30.30.40; | Plakin or cytolinker family | PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UPN3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UPN3}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UPN3}. Cell membrane {ECO:0000250|UniProtKB:Q9UPN3}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9UPN3}. Membrane {ECO:0000269|PubMed:16815997}. Note=The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules. Associated with the minus-end of microtubules via interaction with CAMSAP3. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (By similarity). {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000250|UniProtKB:Q9UPN3}. | null | null | null | null | null | FUNCTION: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000250|UniProtKB:Q9UPN3}. | Rattus norvegicus (Rat) |
D3ZI76 | GPAT2_RAT | METMLKSNPQMQQRNNHSGQETSLWSSGFGMKMEAITPFLGKYRPFMGRCCQTCTPKSWESLFHRSIMDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPTSSDASQMIMENTGVQNILLGKVPGAAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEANLSLDSSEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPGPRLSALGQAWLGLVVQAVQAGIVPDATLVPVATAYDLVPDAPCNMTHDLAPLGLWTGALAIFRRLCNCWGCNRRVCVRVHLAQPFSLQEYTINARSCWGSRQTLEHLLQPIVLGECSVVPDTEKEQEWTPPTSLLLALKEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRVHQGDLVVVPRPGPGLTHLARLSMELLPTFLSEAVGACAVRGLLAGRVPPEGPWELQGIELLSQNELYRQILLLLHLLPQDLLLPQPCQSSYCYCQEVLDRLIQCGLLVAEETPGSRPACDTGRQHLSAKLLWKPSGDFTDSESDDFEEPGGRCFRLSQQSRCPDFFLFLCRLLSPILKAFAQAATFLHLGQLPDSEVGYSEKLLQFLQACAQEEGIFECADPNLAISAIWTFKDLGVLQQIPSPTGPQLHLSPTFASRDNQDKLEQFIRQFICS | 2.3.1.15; 2.3.1.51 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid biosynthetic process [GO:0008654]; piRNA processing [GO:0034587]; triglyceride biosynthetic process [GO:0019432] | mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:22905194}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14DK4}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326; Evidence={ECO:0000250|UniProtKB:Q14DK4}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000250|UniProtKB:Q14DK4}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000250|UniProtKB:Q14DK4}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544, ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence={ECO:0000250|UniProtKB:Q14DK4}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + sn-glycerol 3-phosphate = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37463, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57597, ChEBI:CHEBI:74938; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37464; Evidence={ECO:0000250|UniProtKB:Q14DK4}; | null | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000250|UniProtKB:Q14DK4}. | null | null | FUNCTION: Transfers an acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate producing a lysophosphatidic acid (LPA), an essential step for the triacylglycerol (TAG) and glycerophospholipids. In vitro also transfers an acyl-group from acyl-ACP to the LPA producing a phosphatidic acid (PA). Prefers arachidonoyl-CoA as the acyl donor. Required for primary processing step during piRNA biosynthesis. Molecular mechanisms by which it promotes piRNA biosynthesis are unclear and do not involve its acyltransferase activity. {ECO:0000250|UniProtKB:Q14DK4}. | Rattus norvegicus (Rat) |
D3ZID8 | UBX2A_RAT | MKEVDNLDSIKEEWVCETGPPDNQPLNDNPQKDCEYFVDSLFEEAEKAGAKCLSPTEQKKQVDVNIKLWKNGFTVNDDFRSYSDGASQQFLNSIKKGELPSELQGVFDKDEVDVKVEDKKNEVCMSTKPVFQPFSGQGHRLGSATPRIVSKAKSIEVDNKSTLSAVSLNNLEPITRIQIWLANGERTVQRFNISHRVSHIKDFIEKYQGTQRSPPFALATALPFLRFLDETLTLEEADLQNAVIIQRLQKTAEPFRKL | null | null | autophagosome assembly [GO:0000045]; cellular response to leukemia inhibitory factor [GO:1990830]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; negative regulation of ERAD pathway [GO:1904293]; negative regulation of proteolysis [GO:0045861]; nuclear membrane reassembly [GO:0031468]; positive regulation of protein catabolic process [GO:0045732]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of gene expression [GO:0010468]; regulation of protein catabolic process [GO:0042176]; regulation of protein ubiquitination [GO:0031396] | cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perikaryon [GO:0043204] | acetylcholine receptor binding [GO:0033130]; ubiquitin binding [GO:0043130] | PF08059;PF00789; | 3.30.420.210; | null | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99KJ0}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19474315}. Endoplasmic reticulum {ECO:0000269|PubMed:19474315}. Perikaryon {ECO:0000250|UniProtKB:Q99KJ0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99KJ0}. Nucleus {ECO:0000250|UniProtKB:P68543}. Cytoplasm {ECO:0000269|PubMed:19474315}. Note=Expressed at the axon initial segment. {ECO:0000250|UniProtKB:Q99KJ0}. | null | null | null | null | null | FUNCTION: Acts to repress the ubiquitination and subsequent endoplasmic reticulum-associated degradation of CHRNA3 by the STUB1-VCP-UBXN2A complex in cortical neurons (PubMed:26265139). Also acts to promote the translocation of CHRNA3 to the plasma membrane and subsequently increases plasma membrane acetylcholine-gated ion-channel activation (By similarity). Plays a role in the inhibition of STUB1-mediated TP53 degradation, via its interaction with HSPA9 which acts to inhibit TP53 binding to HSPA9 (By similarity). Positively mediates the ubiquitination and proteosomal degradation of RICTOR, may thereby act as a negative regulator of the mTORC2 pathway (By similarity). {ECO:0000250|UniProtKB:P68543, ECO:0000250|UniProtKB:Q99KJ0, ECO:0000269|PubMed:26265139}. | Rattus norvegicus (Rat) |
D3ZIE4 | FYB1_RAT | MDGKTDVKSLMAKFNTGSNPTEEVSTSSRPFKVAGQNSPSGIQSKKNLFDNQGNASPPAGPSNMSKFGTTKPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPEDKDHGTPSSPFAGVVLKPAASRGSPGLSKNSEEKKEERKTDIPKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKDSATPKQKPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNIKPPLDLKHPINEENQDGVMHSDGTGNLEEEQESDGEMYEDIESSKERDKKREKEEKKRLELERKEQKEREKKEQELRKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVKIDYDSLKRKKNTINAVPPRPVEEDQDVYDDVAEQDAPNSHSQSGSGGMFPPPPADDDIYDGIEEEDADDGSVPQVDEKTNAWSWGILKMLKGKDERKKSIREKPKVSESDSNEGSSFPSPHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGKTKAEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND | null | null | integrin-mediated signaling pathway [GO:0007229]; protein localization to plasma membrane [GO:0072659]; T cell receptor signaling pathway [GO:0050852] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | lipid binding [GO:0008289]; protein-containing complex binding [GO:0044877] | PF14603;PF07653; | 2.30.30.40; | null | PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}. | null | null | null | null | null | FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (PubMed:12681493). {ECO:0000250|UniProtKB:O15117, ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:12681493}. | Rattus norvegicus (Rat) |
D3ZJ25 | AAAT_RAT | MAVDPPKADPKGVVAVDPTANCGSGLKSREDQGAKAGGCCSSRDQVCRCLRANLLVLLTVAAAVAGVVLGLGVSAAGGAEALGHARFTAFAFPGELLLRLLEMIILPLVVCSLIGGAASLDPSALGRLGAWALLFFLVTTLLSSALGVALALALKPGAAFAAINSSVVDSSVHRAPTKEVLDSFLELLRNMFPSNLVSASAAFRIFATSYVSKDINTSGIHPCGACPQRSNATMDQPHCEMKMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPIGILFLVAGKIVEMKDIRQLFIGLGKYIVCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEEKNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLNGMSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAISLPVKDISLILAVDWLVDRSCTVLNVEGDAFGAGLLQSYVDRTKMPSSEPELIQVKNDVSLKPLPLATEEGNPLLKQCREPSGDSSATCEKESVM | null | null | amino acid transmembrane transport [GO:0003333]; erythrocyte differentiation [GO:0030218]; glutamine secretion [GO:0010585]; glutamine transport [GO:0006868]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamine import across plasma membrane [GO:1903803]; L-serine transport [GO:0015825]; neutral amino acid transport [GO:0015804]; protein homotrimerization [GO:0070207]; transport across blood-brain barrier [GO:0150104] | basal plasma membrane [GO:0009925]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamine transmembrane transporter activity [GO:0015186]; L-serine transmembrane transporter activity [GO:0015194]; ligand-gated channel activity [GO:0022834]; metal ion binding [GO:0046872]; neutral L-amino acid transmembrane transporter activity [GO:0015175]; symporter activity [GO:0015293] | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15758}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q15758}. | CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in) + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-glutamine(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:70887, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-threonine(in) + Na(+)(out) = L-glutamine(in) + L-threonine(out) + Na(+)(in); Xref=Rhea:RHEA:70863, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-threonine(out) + Na(+)(out) = L-glutamine(out) + L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:70879, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-asparagine(in) + L-glutamine(out) + Na(+)(out) = L-asparagine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70859, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-asparagine(out) + L-glutamine(in) + Na(+)(out) = L-asparagine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70891, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-alanine(out) + L-glutamine(in) + Na(+)(out) = L-alanine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70867, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-valine(out) + Na(+)(out) = L-glutamine(out) + L-valine(in) + Na(+)(in); Xref=Rhea:RHEA:70871, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-methionine(out) + Na(+)(out) = L-glutamine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70875, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-glutamate(out) + L-glutamine(in) + Na(+)(out) = H(+)(in) + L-glutamate(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70883, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=D-serine(in) + L-glutamine(out) + Na(+)(out) = D-serine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:75307, ChEBI:CHEBI:29101, ChEBI:CHEBI:35247, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=D-serine(in) + L-alanine(out) + Na(+)(out) = D-serine(out) + L-alanine(in) + Na(+)(in); Xref=Rhea:RHEA:75311, ChEBI:CHEBI:29101, ChEBI:CHEBI:35247, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=nitrate(in) = nitrate(out); Xref=Rhea:RHEA:34923, ChEBI:CHEBI:17632; Evidence={ECO:0000269|PubMed:10698697}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:10698697}; CATALYTIC ACTIVITY: Reaction=thiocyanate(in) = thiocyanate(out); Xref=Rhea:RHEA:75347, ChEBI:CHEBI:18022; Evidence={ECO:0000269|PubMed:10698697}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for Na(+) {ECO:0000269|PubMed:10698697}; KM=40 uM for thiocyanate (at -60 mV) {ECO:0000269|PubMed:10698697}; KM=90 uM for thiocyanate (at -20 mV) {ECO:0000269|PubMed:10698697}; | null | null | null | FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:10698697). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (By similarity). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (By similarity). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (By similarity). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (PubMed:10698697). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (By similarity). {ECO:0000250|UniProtKB:Q15758, ECO:0000269|PubMed:10698697}. | Rattus norvegicus (Rat) |
D3ZJ86 | SL9A6_RAT | MTSPKPWARSAGSCQTQRAVRTRKKECREEGESDTEKGPAASSASAQCSFPKRVSFFGWAGALDSSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTCHVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFIAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGTSTEDALDRELTFGDHELVIRGTRLVLPMDDSEPALNSLDDTRHSPA | null | null | axon extension [GO:0048675]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; dendrite extension [GO:0097484]; dendritic spine development [GO:0060996]; establishment of cell polarity [GO:0030010]; glial cell activation [GO:0061900]; neuron projection morphogenesis [GO:0048812]; potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; sodium ion import across plasma membrane [GO:0098719]; synapse organization [GO:0050808] | axon terminus [GO:0043679]; axonal spine [GO:0044308]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | identical protein binding [GO:0042802]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q92581}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92581}. | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92581}. Late endosome membrane {ECO:0000250|UniProtKB:A1L3P4}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Note=Present predominantly in the recycling compartments including early and recycling endosomes, but undergoes plasma membrane localization during vesicular recycling, which is enhanced upon certain stimuli, such as hypoxia (By similarity). Has a major plasmalemmal distribution in a few specialized cells, such as in vestibular hair bundles and osteoblasts (By similarity). {ECO:0000250|UniProtKB:A1L3P4, ECO:0000250|UniProtKB:Q92581}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q92581}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:A1L3P4}; | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo (By similarity). Plays a critical role during neurodevelopment by regulating synaptic development and plasticity (By similarity). Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH (By similarity). Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:A1L3P4, ECO:0000250|UniProtKB:Q92581}. | Rattus norvegicus (Rat) |
D3ZJ96 | UBP28_RAT | MTAELQQDDAAGAADGHGSSCQMLLNQLREITGIQDPSFLHEALKASNGDITQAVSLLTDQRVKEPSHDTAATEPSEVEESATSKDLLAKVIDLTHDNKDDLQAAIALSLLESPNIQTDSRDLNRIHEANSAETKRSKRKRCEVWGENHNPNNWRRVDGWPVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNILENCRSHTEKRNIMFMQELQYLFALLLGSNRKFVDPSAALDLLKGAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSNPRTKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYHNLDECLEGAMVEGDIALLPSDRSVKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQVIYMDRYMYKSKELIRSKRESIRKLKEEIQVLQQKLERYVKYGSGPSRFPLPDMLKYVIEFASTKPASESCLSGSVEHMTLPLPSVHCPISDLTAKESSSPKSCSQNAEGSFSSPEDALPNSEVMNGPFTSPHSSLEMPAPPPAPRTVTDEEMNFVKTCLQRWRSEIEQDIQDLKNCISSTTQAIEQMYCDPLLRQVPYRLHAVLVHEGQASAGHYWAYIYNQPRQIWLKYNDISVTESSWEELERDSYGGLRNVSAYCLMYINDKLPHCSAEAAHGESDQTAEVEALSVELRQYIQEDNWRFEQEVEEWEEEQSCKIPQMESSPNSSSQDFSTSQESSAASSHGVRCLSSEHAVIAKEQTAQAIANTAHAYEKSGVEAALSEVMLSPAMQGVLLAIAKARQTFDRDGSEAGLIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADRNLSYDERSISIMKVAQAKLMEIGPEDMNMEEYKRWHEDYSLFRKVSVYLLTGLELFQKGKYQEALSYLVYAYQSNAGLLVKGPRRGVKESVIALYRRKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGKDIAENLQLCLGEFLPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK | 3.4.19.12 | null | cell population proliferation [GO:0008283]; cellular response to UV [GO:0034644]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647]; response to ionizing radiation [GO:0010212] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cysteine-type deubiquitinase activity [GO:0004843]; deubiquitinase activity [GO:0101005] | PF00443; | 6.10.250.1720;3.90.70.10;1.10.8.10; | Peptidase C19 family, USP28 subfamily | PTM: Degraded upon nickel ion level or hypoxia exposure. {ECO:0000250}.; PTM: Phosphorylated upon DNA damage at Ser-67 and Ser-720, by ATM or ATR. Phosphorylated by PRKD1. {ECO:0000250|UniProtKB:Q96RU2}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBXW7) complex. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells. {ECO:0000250|UniProtKB:Q96RU2}. | Rattus norvegicus (Rat) |
D3ZJP6 | MYO10_RAT | MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEQYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQHSLDLCLQEKSSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVIEAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQISFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHISSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRDLALPEDIRGKCTVLLQFYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKRFLHLKKAAIVFQKQLRGRLARKVYRQLLAEKRELEERKRLEEEKKREEEERERKRAQREADLLRAQQEAETRKQQELEALQKNQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGELSELAENASGEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASVQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRSAKEIIDNTNKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTLHTSVPPLEEVYSLQRLKARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGTVARQKVEEEQMLDMWIKEEICSARASIIDKWKKLQGVSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSLSSQGSSR | null | null | cytoskeleton-dependent intracellular transport [GO:0030705]; positive regulation of cell-cell adhesion [GO:0022409]; regulation of cell shape [GO:0008360]; regulation of filopodium assembly [GO:0051489] | cell cortex [GO:0005938]; cytosol [GO:0005829]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; myosin complex [GO:0016459]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; plus-end directed microfilament motor activity [GO:0060002]; spectrin binding [GO:0030507] | PF00373;PF00612;PF16735;PF00063;PF00784;PF00169;PF18597; | 1.10.10.820;1.20.5.170;1.20.5.190;1.20.58.530;1.20.80.10;6.20.240.20;3.40.850.10;1.20.120.720;1.25.40.530;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, filopodium tip {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, filopodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:21965296}; Peripheral membrane protein {ECO:0000269|PubMed:21965296}; Cytoplasmic side {ECO:0000269|PubMed:21965296}. Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Interacts with microtubules. Undergoes forward and rearward movements within filopodia. Interaction with membranes containing phosphatidylinositol 3,4,5-trisphosphate mediates localization at filopodium membranes (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts (By similarity). {ECO:0000250|UniProtKB:Q9HD67, ECO:0000269|PubMed:21965296}. | Rattus norvegicus (Rat) |
D3ZKB9 | TSH3_RAT | MAAYVSDELKAAALVEDDIEPEEQVADGEPSAKYMCPEKELSKACPSYQNSPAAEFSSHEMDSESHISETSDRMADFESSSIKNEEETKEVQVPLEDTTVSDSLEQMKAVYNNFLSNSYWSNLNLNLHQPSSENNGGGSSSSSSSSSSSCGSGSFDWHQSAMAKTLQQVSQNRMLPEPSLFSTVQLYRQSSKLYGSIFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNHETDNNNPKRWSKPRKRSLLEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVTPVAAKIIPAARKKPSLELELPSSPDSTGGTPKATLSDASDALQKNSNPYITPNNRYGHQNGASYAWHFEARKSQILKCMECGSSHDTLQELTAHMMVTGHFIKVTNSAMKKGKPIMETPVTPTITTLLDEKVQSVPLAATTFTSPSNTPASVSPKLTVEIKKEVDKEKAVLDEKPKEKEKASEEEEKYDISSKYHYLTENDLEESPKGGLDILKSLENTVTSAINKAQNGTPSWGGYPSIHAAYQLPNMMKLSLGSSGKSTPLKPMFGNSEIVSPTKTQTLVSPPSSQTSPMPKTNFHAMEELVKKVTEKVAKVEEKMKEPDSKLSPPKRATPSPCSSEQSEPIKMEASSGSGFKSQENSPSPPRDVCKEASPSAEPVENGKELVKPLSGGSLSGSTAIITDHPPEQPFVNPLSALQSVMNIHLGKAAKPSLPALDPMSMLFKMSNSLAEKAAVATPPPLQAKKAEHLDRYFYHVNNDQPIDLTKGKSDKGCSLGSGLLSPTSTSPATSSSTVTTAKTSAVVSFMSNSPLRENALSDISDMLKNLTESHTSKSSTPSSISEKSDIDGATLEEAEESTPAQKRKGRQSNWNPQHLLILQAQFAASLRQTSEGKYIMSDLSPQERMHISRFTGLSMTTISHWLANVKYQLRRTGGTKFLKNLDTGHPVFFCNDCASQIRTPSTYISHLESHLGFRLRDLSKLSTEQINNQIAQTKSPSEKMVTSSPEEDLGTTYQCKLCNRTFASKHAVKLHLSKTHGKSPEDHLLFVSELEKQ | null | null | in utero embryonic development [GO:0001701]; kidney morphogenesis [GO:0060993]; kidney smooth muscle cell differentiation [GO:0072195]; long-term synaptic potentiation [GO:0060291]; lung development [GO:0030324]; metanephros development [GO:0001656]; musculoskeletal movement [GO:0050881]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of transcription by RNA polymerase II [GO:0006357]; sensory perception of touch [GO:0050975]; smooth muscle tissue development [GO:0048745]; ureter smooth muscle cell differentiation [GO:0072193]; ureteric bud development [GO:0001657]; ureteric peristalsis [GO:0072105] | growth cone [GO:0030426]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872] | PF13912; | 3.30.160.60; | Teashirt C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000269|PubMed:19343227}. Note=Colocalizes with APBB1 in the nucleus (By similarity). Colocalizes with APBB1 in axonal growth cone. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in developmental processes. Functions in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter (By similarity). Involved in the modulation of glutamatergic synaptic transmission and long-term synaptic potentiation (By similarity). {ECO:0000250|UniProtKB:Q8CGV9}. | Rattus norvegicus (Rat) |
D3ZKD3 | ALKB5_RAT | MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGTTKRKYQEDSDPERSDYEEHQLQKEEEARKVKSGIRQIRLFSQDECSKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSTLPPSYASDRLSGNTRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCPEAASSPTRKVKMRRH | 1.14.11.53 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6P6C2}; | cell differentiation [GO:0030154]; gamma-delta T cell proliferation [GO:0046630]; mRNA destabilization [GO:0061157]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; non-membrane-bounded organelle assembly [GO:0140694]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of mRNA stability [GO:0043488]; regulation of translation [GO:0006417]; response to hypoxia [GO:0001666]; spermatogenesis [GO:0007283] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; paraspeckles [GO:0042382] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; oxidative RNA demethylase activity [GO:0035515] | PF13532; | 2.60.120.590; | AlkB family | PTM: Phosphorylated at Ser-88 and Ser-326 in response to reactive oxygen species (ROS), promoting sumoylation and inactivation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Acetylated by KAT8 at Lys-236, promoting interaction with PSPC1, thereby facilitating recognition of N(6)-methyladenosine (m6A) mRNA by ALKBH5. Deacetylated at Lys-236 by HDAC7. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Sumoylated at Lys-87 and Lys-322 by PIAS4 following phosphorylation at Ser-88 and Ser-326 in response to reactive oxygen species (ROS), inhibiting the RNA demethylase activity. Desumoylated by SENP1; relieving RNA demethylase inhibition, leading to N(6)-methyladenosine-containing mRNAs demethylation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Ubiquitinated at Lys-58 via 'Lys-48'-linked polyubiquitin chain, leading to its degradation by the proteasome. Deubiquitinated at Lys-58 by USP9X, promoting its stabilizazion. {ECO:0000250|UniProtKB:Q6P6C2}. | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000250|UniProtKB:Q6P6C2}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=1.14.11.53; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49521; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; | null | null | null | null | FUNCTION: Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (By similarity). Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Demethylation of m6A mRNA affects mRNA processing, translation and export (By similarity). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity). Involved in paraspeckle assembly, a nuclear membraneless organelle, by undergoing liquid-liquid phase separation (By similarity). Paraspeckle assembly is coupled with m6A demethylation of RNAs, such as NEAT1 non-coding RNA (By similarity). Also acts as a negative regulator of T-cell development: inhibits gamma-delta T-cell proliferation via demethylation of JAG1 and NOTCH2 transcripts (By similarity). Inhibits regulatory T-cell (Treg) recruitment by mediating demethylation and destabilization of CCL28 mRNAs (By similarity). {ECO:0000250|UniProtKB:Q3TSG4, ECO:0000250|UniProtKB:Q6P6C2}. | Rattus norvegicus (Rat) |
D3ZKX9 | LOXE3_RAT | MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCLNGRQQYVTAPLCLLWLNPQGVLLPLAIQLSQIPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRRGLIYLMSTGLAHFTYTDFCLPDSLRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPNDACVQQDSELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGNTTMESYLETLPEVNTTCSNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQKCLAQISKDIRARNESLALPYAYLDPPLIENSVSI | 4.2.1.152; 5.4.4.7 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; ceramide biosynthetic process [GO:0046513]; establishment of skin barrier [GO:0061436]; fat cell differentiation [GO:0045444]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; sensory perception of pain [GO:0019233]; sphingolipid metabolic process [GO:0006665] | cytoplasm [GO:0005737] | hepoxilin A3 synthase activity [GO:0051120]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; hydroperoxy icosatetraenoate isomerase activity [GO:0106255]; intramolecular hydroxytransferase activity [GO:0050486]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxyeicosatetraenoate = a hydroxy-epoxy-eicosatetraenoate; Xref=Rhea:RHEA:55560, ChEBI:CHEBI:59720, ChEBI:CHEBI:137328; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55561; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate + H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720, ChEBI:CHEBI:131859; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-hydroxy-(11R,12R)-epoxy-(5Z,9E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:37939, ChEBI:CHEBI:75230, ChEBI:CHEBI:75232; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37940; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:37955, ChEBI:CHEBI:57444, ChEBI:CHEBI:75233; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37956; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (10R)-hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:37951, ChEBI:CHEBI:57444, ChEBI:CHEBI:75234; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37952; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (13R)-hydroxy-(14S,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:37959, ChEBI:CHEBI:57446, ChEBI:CHEBI:75235; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37960; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 7R-hydroxy-5S,6S-epoxy-(8Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:41251, ChEBI:CHEBI:57450, ChEBI:CHEBI:77919; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41252; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 11-hydroxy-(12S,13S)-epoxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:50212, ChEBI:CHEBI:57466, ChEBI:CHEBI:132064; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50213; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=N-[omega-(9R)-hydroperoxy-(10E,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine = N-[omega-(9R,10R)-epoxy-(13R)-hydroxy-(11E)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine; Xref=Rhea:RHEA:40503, ChEBI:CHEBI:134624, ChEBI:CHEBI:134626; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40504; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate octadecasphing-4E-enine = N-acyl-(9R,10R)-epoxy-(13R)-hydroxy-(11E)-octadecenoate (4E)-octadecasphin-4-enine; Xref=Rhea:RHEA:41243, ChEBI:CHEBI:77889, ChEBI:CHEBI:77891; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41244; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37943, ChEBI:CHEBI:15377, ChEBI:CHEBI:75230, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37944; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTIC ACTIVITY: Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = (10R)-hydroxy-(8S,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:37931, ChEBI:CHEBI:75322, ChEBI:CHEBI:75327; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9WV07}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37932; Evidence={ECO:0000250|UniProtKB:Q9WV07}; CATALYTIC ACTIVITY: Reaction=(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37935, ChEBI:CHEBI:15377, ChEBI:CHEBI:57447, ChEBI:CHEBI:75326; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9WV07}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37936; Evidence={ECO:0000250|UniProtKB:Q9WV07}; CATALYTIC ACTIVITY: Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37927, ChEBI:CHEBI:15377, ChEBI:CHEBI:75322, ChEBI:CHEBI:75326; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9WV07}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37928; Evidence={ECO:0000250|UniProtKB:Q9WV07}; | null | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000250|UniProtKB:Q9BYJ1}.; PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q9BYJ1}. | null | null | FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (PubMed:23382512). {ECO:0000250|UniProtKB:Q9BYJ1, ECO:0000250|UniProtKB:Q9WV07, ECO:0000269|PubMed:23382512}. | Rattus norvegicus (Rat) |
D3ZLB7 | FOSB_RAT | MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTSTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGSQRTSGSEQPSDPLNSPSLLAL | null | null | behavioral response to cocaine [GO:0048148]; cellular response to calcium ion [GO:0071277]; cellular response to hormone stimulus [GO:0032870]; female pregnancy [GO:0007565]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to amphetamine [GO:0001975]; response to cAMP [GO:0051591]; response to cocaine [GO:0042220]; response to corticosterone [GO:0051412]; response to ethanol [GO:0045471]; response to mechanical stimulus [GO:0009612]; response to morphine [GO:0043278]; response to progesterone [GO:0032570]; response to xenobiotic stimulus [GO:0009410]; transcription by RNA polymerase II [GO:0006366] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: Phosphorylated; phosphorylation is induced by chronic electroconvulsive seizure (ECS) treatment. {ECO:0000269|PubMed:16687504}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13346}. | null | null | null | null | null | FUNCTION: Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (By similarity). Exhibits transactivation activity in vitro (By similarity). As part of the AP-1 complex, facilitates enhancer selection together with cell-type-specific transcription factors by collaboratively binding to nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex to establish accessible chromatin (By similarity). Together with JUN, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Involved in the display of nurturing behavior towards newborns (By similarity). May play a role in neurogenesis in the hippocampus and in learning and memory-related tasks by regulating the expression of various genes involved in neurogenesis, depression and epilepsy (By similarity). Implicated in behavioral responses related to morphine reward and spatial memory (By similarity). {ECO:0000250|UniProtKB:P13346, ECO:0000250|UniProtKB:P53539}. | Rattus norvegicus (Rat) |
D3ZLH5 | PLXB3_RAT | MLTDFLQAPVMAPWSPFSLHLLLLFLLLLPLTRAHRFSVPNASFNHLVLAPDQGKLYVGAVNHLFQLSPELEMESVAITGPVIDSPDCVPFRDLAECPQAQLTDNANQLLLVSSRAQELVACGQVRQGVCEKRRLGDVTQVLYQAEDPGDGQFVAANTLGVTTVGLVVPLPGRDLLLVARGLAGKLSAGVPPLTVRQLAGPQPFSSEGLGRLVVGDFSDYNNSYVGAFSDAHSAYFVFRRRGARAQTEYRSYVARVCLGDVNLYSYVEVPLTCHGQGLIQAAFLAPDTLLGAFSAGTSQAQAALCAFPLADLDGSMEQARRLCYTTGGQGPNGMEEATVEYGVTSRCVTLPPDSPESYPCGDEHTPSPIAGRQPLEAQPLLQLGQPISAVAALQTDGHTIAFLGDTEGQLHKVFLNSSHGQVYHSQQVGPPGSAISPDLLVDNSGDYLYVLTAQQVDRILVAACPQFPNCTTCLQARDPLCGWCILQGRCTRRAECGRAVQPNQWLWSYEDNHCLHIQSLLPAQHPRQEHGQITLSVPGLPNLAMDEYFYCAFGDYNSLAQVEEHHVVCATPPQDRMPPNPPGSDHVTLPLALMFEDVVLAATTFSFYDCSAIQALEVAAPCRTCVSSLWRCHWCPQSSHCVYGERCPEGEKAVYSAQEVDILVRGPEACPQVKGLASPQLVPVGWESHVTLHIENLHYFRGLPALYYCWLELPGKLRKLPAFLEETSRNSGLIHCQAQQFHPSMSQWELPVPIYVTRGEIQRLDNTGDLHVTLYDCAMGHPDCSHCQAANGSLSCLWCGDGQPACRYGPLCPPGAVEQLCPIPSIDVIEPLTGPPEGGLAITILGSNLGQAFNDVRNAVTVAGQPCNPDPSLYRISARIVCVTSPAPNGTSGPVQVAIKSRPPGISAQHFTYQDPVLLSLNPQWGPQAGGTQLTIHGQYLQTGGNVSAFVGDQPCPIQEPVCPEAIICHTMPQMEPGEAVVFVVFGHVERKLLTTPFRYTANPQLVEAEPSVSFRGGGRVIRVRGTGLDVVWQPLLSVWLEDEFQVKALGVQAQDVNPRRSCGAPAADPQACIHLESGLLQCSTLCSVNSSSLLLCHSPAVPDGALPKRVFFALDNMQVDFASASGGQGFLYQPNPRLAPLSHEGITHPYRLKPGHVLDVEGEGLNLGISKEEVQVHIGDGKCLVKTLTLTHLYCEPPQQAPQPTNGSGTLPQFVVQMGNVRLALGPVQYEAEPMISTFPVEAQVGLGMGAAMLIAAVLLLTLMYRHKSKQALRDYQKVLVQLENLETGVGDQCRKEFTDLMTEMTDLTSDLEASGIPFLDYRTYAERAFFPGHVGCPLQPGLEGPGEEGRRVTVCQGLTQLSNLLNSKLFLLTLIHTLEEQPSFSQRDRCHVASLLSLALHSKLEYLTDIMRTLLGDLAAHYVHKNPKLMLRRTETMVEKLLTNWLSICLYAFLKEVAGEPLYMLFRAIKYQVDKGPVDAVTGKAKRTLNDSHLLREDVEFRPLTLMALVGPGAGGAAGNSEVHRVPARVLDTDTITQVKEKVLDQIYKGTPFSQRPSVHSLDLEWRSGLAGHLTLSDEDLTSVTQNHWKRLNTLQHYKVPDGATVVLIPQLHNGGTVSQSLEQTGCHSGENTPMLEDGEEGGVRLWHLVKATEETEGAKVRRSSLRERERERARAKAIPEIYLTRLLSMKGTLQKFVDDTFQAILSMNRPVPIAVKYLFDFLDELAEKHGIEDPETLHIWKTNSLLLRFWVNALKNPQLIFDVRVSDNEDAILAVIAQTFIDSCMVSEHKVGRDSPVNKLLYAREIPRYKQMVEKYYADIRQSSPASYQEMNSALAELSGNYTSAPNCLEALRELYNHIHRYYDQIISALEEDPVAQKMQLACRLQQVAALVEYKVTDL | null | null | cell chemotaxis [GO:0060326]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell migration [GO:0030336]; negative regulation of GTPase activity [GO:0034260]; negative regulation of lamellipodium assembly [GO:0010593]; positive chemotaxis [GO:0050918]; positive regulation of axonogenesis [GO:0050772]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of neuron projection development [GO:0010976]; regulation of cell shape [GO:0008360]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287] | cell surface [GO:0009986]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | cell-cell adhesion mediator activity [GO:0098632]; protein domain specific binding [GO:0019904]; Rho GDP-dissociation inhibitor binding [GO:0051022]; semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULL4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ULL4}. Note=Colocalizes with RIT2/RIN at the plasma membrane. {ECO:0000250|UniProtKB:Q9ULL4}. | null | null | null | null | null | FUNCTION: Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. {ECO:0000269|PubMed:20696765}. | Rattus norvegicus (Rat) |
D3ZMK9 | PRAG1_RAT | MSACSDFVEHIWKPGSCKNCFCLRSDHQLTAGHPKARASSLPAGARLPARPEICRLEDEGVNGLAYSKPTIAVKPTMMTSETADLWTEASLSAEVPKVNWRRTPGKLLLQKQEDGPIVYLGSFRGMQKAAGPLACTDSNSRCPPAYTMVGLHNLEARVDRNTALQPVNFQEEKAGREELPSAQESFRQKLAAFTGMTSSCLKGPRPCTSPQPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCRPESRDAVHNTEGSGRRRGDCSPICWEQGTCTRPTEEEKQALNFPRECCGQGSTANPPHLGPKKPSLNSEAASSSDGLSCGSSRSGANSPFAPHLENDYCSLVKEPTSVKQQDSGCHLVNSGKYVGQAVDLQPPALPREAVQPEPIYAESAKRKKAAPVPQRPEPKKEQVSSGQVWTGDTWSQKTPSGWSQEREGPNAAPQVATTITVIAAHPEEDHRTIYLSSPDSAVGVQWPRGSLNQDLHGSGEEPLVVQGLSSRESHPHNMTENSSKEKPAIPPKLSKSSPGGSPVSPAAPPLTDHSDGNTSGSSVGSQPSSRVPTNLTSSCQTNGVAAGDPAKCPPQANSSVLDQRRPRYQTGAWSRQCRIEEEEEVGQELLSQSWGRELENGIADHSNSSTWHRLHPIDGASGQNGKTNSGMSKSASFAFEFPKDRGRLESFSPPPPPPKSRHLLKMNKSSSDLEKVSQSSAESLSPSFRGAHVSFTTGSTDSLASDSRTCSDGGPSCEATHSPTISGKKLFAPVPFPSGSTEDVSPSGPAQPPPLPQKKIVSRAASSPDGFFWTQGSPKPRTASPKLNLSHSETNVCAHDEPPLSYSLNSGNHPHHVFSSSEPLEKAFKGSVPWAPALGPANSKGGCGSPNLQGRAATSTSSSQLSVSSQASTGSSQLQLHSLLSSISSKEGTYAKLGGLYTQSLARLVTKCEDLFMGGLKTELRFDENSWSLFKLICNKPCCDSGDAIYYGATCSKDPDSIYAVKICKTPEPKSASYCSPSVPVHFNIQQDCGHFVASVPSSMLAFPDTSSKDPAPAAPSHTPAQEQDCVVVITREVPHQTASDFVRDSVASHRAEPEVYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCNPQSSPGPSANPSVPTTTSRCPSAAPAATTACQGGPGEKHLPRLIISNFLKAKQKPGGTTNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRREDLPPLPTLSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVEQPCPSEEVLCNTLHNWIDMKRALMMMKFAEKAVERRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL | null | null | cell migration [GO:0016477]; negative regulation of neuron projection development [GO:0010977]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of cell motility [GO:2000145]; regulation of cell shape [GO:0008360]; regulation of Notch signaling pathway [GO:0008593] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; protein kinase activity [GO:0004672] | PF00069; | 1.10.510.10; | Protein kinase superfamily | PTM: Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is a primary site of phosphorylation. {ECO:0000269|PubMed:27116701}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21873224, ECO:0000269|PubMed:27116701}. Nucleus {ECO:0000250|UniProtKB:Q571I4}. Cell junction, focal adhesion {ECO:0000269|PubMed:27116701}. Note=Colocalized with NOTCH1 in the nucleus. {ECO:0000250|UniProtKB:Q571I4}. | null | null | null | null | null | FUNCTION: Catalytically inactive protein kinase that acts as a scaffold protein (PubMed:29503074). Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (PubMed:16481321). Promotes Src family kinase (SFK) signallig by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (PubMed:21873224, PubMed:27116701). Acts as a critical coactivator of Notch signaling (By similarity). {ECO:0000250|UniProtKB:Q571I4, ECO:0000269|PubMed:16481321, ECO:0000269|PubMed:21873224, ECO:0000269|PubMed:27116701, ECO:0000269|PubMed:29503074}. | Rattus norvegicus (Rat) |
D3ZML2 | BRSK2_RAT | MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELGHLQLFGNPVSKVRSVAMELVILVQTLAYTSFRLLGTFLPVRYLRHSVLSRPPERARLVLRGAPCTHMGPVWNMVGMAYTQNPPIMGETGVYGSQWVMSSAPSKHYTSLGLSVPSPSCSLSPSLFPFCAPDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP | 2.7.11.1; 2.7.11.26 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | actin cytoskeleton organization [GO:0030036]; axonogenesis [GO:0007409]; cell division [GO:0051301]; DNA damage response [GO:0006974]; ERAD pathway [GO:0036503]; establishment of cell polarity [GO:0030010]; exocytosis [GO:0006887]; G2/M transition of mitotic cell cycle [GO:0000086]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; microtubule cytoskeleton organization involved in establishment of planar polarity [GO:0090176]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; neuron differentiation [GO:0030182]; neuron projection morphogenesis [GO:0048812]; protein phosphorylation [GO:0006468]; regulation of axonogenesis [GO:0050770]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of neuron projection development [GO:0010975]; response to UV [GO:0009411] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; distal axon [GO:0150034]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF00069;PF21115; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-175 by PP2C (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated by the APC complex in conjunction with FZR1, leading to its proteasomal degradation. Targeted for proteasomal degradation by interaction with COPS5. BRSK2 levels change during the cell cycle. BRSK2 levels are low at the G1/S boundary and gradually increase as cells progress into G2 phase. BRSK2 levels decrease rapidly at the end of mitosis (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-175 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-261 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZMM8 | YLAT2_RAT | MEARELGSPTPTYHLLPKANQHTVKEDASSPSQGSPETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLKYTASYGLSLVVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLIVEPTSQAIIAITFANYIIKPSFPTCDPPYVACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQGHTEHFQDAFKGSSWNVGDLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNIQDVHKSDAVAVTFADQTFGMFSWTIPIAVALSCFGGLNASIFASSRLFFVGSREGHLPNLLSMIHIERFTPVPALLFNCTMTLIYLVVKDVFLLINYFSFSYWFFVGLSVVGQLYLRWKEPDWPRPLKLSLFFPIVFCICSLFLVAVPLFSDTINSLIGIGIALSGVPVYFMGVYLPEARRPLFIRKVLATVTRVTQKLCFCVLTELDVAEEKNVERKTD | null | null | amino acid transmembrane transport [GO:0003333]; glycine betaine transport [GO:0031460]; L-arginine transmembrane transport [GO:1903826]; leucine transport [GO:0015820]; neutral amino acid transport [GO:0015804]; nitric oxide biosynthetic process [GO:0006809]; ornithine transport [GO:0015822] | plasma membrane [GO:0005886] | arginine binding [GO:0034618]; basic amino acid transmembrane transporter activity [GO:0015174]; L-amino acid transmembrane transporter activity [GO:0015179]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine:L-arginine antiporter activity [GO:0106439] | PF13520; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, L-type amino acid transporter (LAT) (TC 2.A.3.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L-lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out) + L-leucine(in) + Na(+)(in); Xref=Rhea:RHEA:70831, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-glutamine(out) + Na(+)(out) = L-arginine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70835, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-histidine(out) + Na(+)(out) = L-arginine(out) + L-histidine(in) + Na(+)(in); Xref=Rhea:RHEA:70839, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-cysteine(out) + Na(+)(out) = L-arginine(out) + L-cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:70847, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:35235; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-methionine(out) + Na(+)(out) = L-arginine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70843, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q92536}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55.82 uM for L-arginine {ECO:0000269|PubMed:22401943}; KM=71.06 uM for L-arginine (in astrocytes treated with ammonium chloride) {ECO:0000269|PubMed:22401943}; Vmax=1.301 nmol/min/mg enzyme toward L-arginine {ECO:0000269|PubMed:22401943}; Vmax=1.82 nmol/min/mg enzyme toward L-arginine (in astrocytes treated with ammonium chloride) {ECO:0000269|PubMed:22401943}; | null | null | null | FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux routeby exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (PubMed:22401943, PubMed:26448619). Also exchanges L-arginine with L-lysine in a sodium-independent manner. The transport mechanism is electroneutral and operates with a stoichiometry of 1: 1 (By similarity). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (PubMed:22401943, PubMed:26448619). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (By similarity). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity). {ECO:0000250|UniProtKB:Q8BGK6, ECO:0000250|UniProtKB:Q92536, ECO:0000269|PubMed:22401943, ECO:0000269|PubMed:26448619}. | Rattus norvegicus (Rat) |
D3ZMY7 | 5NTC_RAT | MMTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLNFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE | 2.7.1.77; 3.1.3.5; 3.1.3.99 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:6260203}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49902}; | adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; amide catabolic process [GO:0043605]; dGMP catabolic process [GO:0046055]; dGMP metabolic process [GO:0046054]; GMP catabolic process [GO:0046038]; GMP catabolic process to guanine [GO:0006202]; GMP metabolic process [GO:0046037]; IMP catabolic process [GO:0006204]; IMP metabolic process [GO:0046040]; negative regulation of defense response to virus by host [GO:0050689]; protein K48-linked ubiquitination [GO:0070936] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 5'-nucleotidase activity [GO:0008253]; ATP binding [GO:0005524]; GMP 5'-nucleotidase activity [GO:0050484]; identical protein binding [GO:0042802]; IMP 5'-nucleotidase activity [GO:0050483]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; ubiquitin protein ligase activity [GO:0061630] | PF05761; | 3.40.50.1000; | 5'(3')-deoxyribonucleotidase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside; Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274, ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714, ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate; Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530, ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57464; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531; Evidence={ECO:0000305|PubMed:6260203}; CATALYTIC ACTIVITY: Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584, ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP; Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596, ChEBI:CHEBI:57673, ChEBI:CHEBI:58053; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572, ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053, ChEBI:CHEBI:61194; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588, ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865, ChEBI:CHEBI:58053; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592, ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:60377; Evidence={ECO:0000250|UniProtKB:P49902}; CATALYTIC ACTIVITY: Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P49902}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for IMP {ECO:0000269|PubMed:6260203}; KM=0.7 mM for dIMP {ECO:0000269|PubMed:6260203}; KM=0.7 mM for GMP {ECO:0000269|PubMed:6260203}; KM=1.1 mM for dGMP {ECO:0000269|PubMed:6260203}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:6260203}; | null | FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates (PubMed:6260203). In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (By similarity). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP (PubMed:6260203). Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (By similarity). Through these activities regulates the purine nucleoside/nucleotide pools within the cell (PubMed:6260203). {ECO:0000250|UniProtKB:P49902, ECO:0000269|PubMed:6260203}. | Rattus norvegicus (Rat) |
D3ZN95 | HCFC1_RAT | MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIETLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLVPQAAAAPPSTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPASVRMVVPTQSAQGTVIGSNPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTVAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSAANTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGAHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQEAAASLVTSAVGQQNGNVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTSTATTAMSSMGTGQQRDARRATNTPTVVRITVAPGALERAQGTVKPPCQTQQTNMTSTTMTVQATGAPCSAGPLLRPSVALETGSHSPAFVQLALPSVRVGLSGPSSKDVPTGRQPETYHTYTTNTPTTARSIMVAGELGTARVVPTSQYDCLQASSPSSTMTMTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGAGQPEGGQQPASGHPCETHQTTSTGTTMSVSVGALIPDATPSHGTLESGLEVVAVPTVTSQAGATLLASFSTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVASTQGDSTNITSASAITTTVSSTLPRAVTTVTQSTPVPGPSVPPPEELQVSPGPRQQLPPRQLLQSASTPLMGESAEVLSASQTPELQAAVDLSSTGDPSSVQEPTTSAVVATVVVQPPQPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMGTGEPMDTSEAAAAVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQQLQEAQAQAQQQHHLPTEALAPADSLNDPSIESNCLNELASAVPSTVALLPSTATESLAPSNTFVAPQPVVVASPAKMQAAATLTEVANGIESLGVKPDLPPPPSKAPIKKENQWFDVGVIKGTSVMVTHYFLPPDDAVQSDDDSGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQASGEPKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPASKRPMSSPEM | null | null | blastocyst hatching [GO:0001835]; cell cycle [GO:0007049]; cellular response to organic cyclic compound [GO:0071407]; chromatin remodeling [GO:0006338]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; regulation of protein-containing complex assembly [GO:0043254]; release from viral latency [GO:0019046] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; histone acetyltransferase complex [GO:0000123]; histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; MLL1/2 complex [GO:0044665]; neuronal cell body [GO:0043025]; NSL complex [GO:0044545]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; Set1C/COMPASS complex [GO:0048188] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713] | PF01344;PF13415;PF13854; | 6.10.250.2590;2.60.40.10;2.120.10.80; | null | PTM: Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains. Cleavage is promoted by O-glycosylation. {ECO:0000250|UniProtKB:P51610}.; PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing. {ECO:0000250|UniProtKB:P51610}.; PTM: Ubiquitinated. Lys-1818 and Lys-1819 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein. {ECO:0000250|UniProtKB:P51610}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51610}. Nucleus {ECO:0000250|UniProtKB:P51610}. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER. {ECO:0000250|UniProtKB:P51610}. | null | null | null | null | null | FUNCTION: Transcriptional coregulator (PubMed:24250814). Involved in control of the cell cycle (By similarity). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By similarity). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together (By similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). Modulates expression of homeobox protein PDX1, perhaps acting in concert with transcription factor E2F1, thereby regulating pancreatic beta-cell growth and glucose-stimulated insulin secretion (PubMed:24250814). May negatively modulate transcriptional activity of FOXO3 (PubMed:21909281). {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:21909281, ECO:0000269|PubMed:24250814}. | Rattus norvegicus (Rat) |
D3ZPG5 | UBP30_RAT | MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLSLLKALSCQEVTEEEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNPWKSQHPFHGRLSSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTQNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSQGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPKATESPGSALGVQDTQAAPKPGLSQPAAPKTQFFMNGACSPSLLPALPSPMAFPLPVAPDYSSSMYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYERVLSRVQQQGREYRSEE | 3.4.19.12 | null | mitochondrial fusion [GO:0008053]; negative regulation of mitophagy [GO:1901525]; protein K11-linked deubiquitination [GO:0035871]; protein K6-linked deubiquitination [GO:0044313]; proteolysis [GO:0006508] | cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197] | PF00443; | 3.90.70.10; | Peptidase C19 family | PTM: Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation. {ECO:0000250|UniProtKB:Q70CQ3}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q70CQ3}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q70CQ3}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:24896179). Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (By similarity). Acts as a negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity). {ECO:0000250|UniProtKB:Q3UN04, ECO:0000250|UniProtKB:Q70CQ3, ECO:0000269|PubMed:24896179}. | Rattus norvegicus (Rat) |
D3ZPX4 | PLXA3_RAT | MHTVCLLPLLFFTIGGCLGSSRPFRTFVVTDTTLTHLAVHRVTGEVFVGAVNRVFKLASNLTELRAHVTGPIEDNARCYPPPSMRVCSHRLVPVDNVNKLLLIDYAARRLVACGSIWQGICQFLRLDDLFKLGEPHHRKEHYLSGAQEPDSMAGVIVEQGQGPSKLFVGTAVDGKSEYFPTLSSRKLIDDEDSGDMFSLVYQDEFVSSQIKIPSDTLSLYPAFDIYYIYGFVSASFVYFLTLQLDTQQTLLDTAGEKFFTSKIVRMCAGDSEFYSYVEFPIGCSWRGVEYRLVQSAHLAKPGLLLAQALGVPADEDVLFTIFSQGQKNRANPPRQTILCLFTLSSINAHIRRRIQSCYRGEGTLALPWLLNKELPCINTPMQINGNFCGLVLNQPLGGLHVIEGLPLLADSTDGMASVAAYTYHQHSVVFIGTRSGNLKKVRVDGSQDAQLYETVSVVQGTPILRDLLFSPDHRHIYLLSEKQVSQLPVETCEQYLSCAACLGSGDPHCGWCVLQHRCCREGACPGASAPHGFAEELNKCIQVRVRPNNVSVTSSGVQLTVAMRNVPDLSLGVSCSFEEVTESEAILLPSGELRCPSPSLQELQTLTRGHGATHTVRLQLLSMETGVRFAGVDFVFYNCSALQSCMSCVGSPYPCHWCKYRHVCTSHPHECSFQEGRVHSPEGCPEILPRGDLLIPVGVMQPLTLRAKNLPQPQSGQKNYECVVRVQGRQHRVPAVRFNSSSVQCQNASYFYEGDEFGDTELDFSVVWDGDFPIDKPPSFRALLYKCWAQRPSCGLCLKADPRFNCGWCISEHRCQLRVHCPAPKSNWMHPSQKGARCSHPRITQIHPLTGPKEGGTRVTIVGENLGLTSREVGLRVAGVRCNSIPTEYVSAERIVCEMEESLVPSPPPGPAELCVGDCSADFRTQSQQLYSFVTPTLDRVSPTRGPASGGTRLTISGTSLDAGSRVTVIIRDGECQFVRRDAEAIVCISPISTLGPSQAPIILAIDHANISSTGVIYTYTQDPTVTHLEPTWSIINGSTSITVSGTHLLTVQEPRVRAKYRGIETTNTCQVINDTAMLCKAPGIFLGHPQPRAQGEHPDEFGFLLDHVQAARSLNRSSFTYYPDPSFEPLGPSGVLDVKPGSHVVLKGKNLIPAAAGSSRLNYTVLIGGQPCALTVSDTQLLCDSPSQTGRQPVMVLVGGLEFWLGTLHITADRALTLPAMVGLAAGGGLLLLAITVVLVAYKRKTQDADRTLKRLQLQMDNLESRVALECKEAFAELQTDINELTNHMDGVQIPFLDYRTYAVRVLFPGIEAHPVLKELDTPPNVEKALRLFGQLLHSRAFLLTFIHTLEAQSSFSMRDRGTVASLTMVALQSRLDYATGLLKQLLADLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLHKFLKECAGEPLFLLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLHCVCPESEGSAQVPVKVLNCDSITQAKDKLLDTVYKGIPYSQRPKAEDMDLEWRQGRMARIILQDEDITTKIECDWKRINSLAHYQVTDGSLVALVPKQVSAYNMANSFTFTRSLSRYESLLRAASSPDSLRSRAPMLTPDQEAGTKLWHLVKNHDHADHREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETVFSTAHRGSALPLAIKYMFDFLDEQADQRQISDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYRDIAKMASISDQDMDAYLVEQSRLHANDFNVLSALSELYFYVTKYRQEILTSLDRDASCRKHKLRQKLEQIITLVSSSS | null | null | axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; facial nerve structural organization [GO:0021612]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; hippocampus development [GO:0021766]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of cell adhesion [GO:0007162]; neuron projection extension [GO:1990138]; neuron projection guidance [GO:0097485]; olfactory nerve formation [GO:0021628]; positive regulation of axonogenesis [GO:0050772]; positive regulation of cytoskeleton organization [GO:0051495]; pyramidal neuron development [GO:0021860]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; trigeminal nerve structural organization [GO:0021637] | plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZQF4 | FKBP6_RAT | MSVFSRLRNGIPPSRDDCQSPYERLSQRMLDISGDRGVLKDIIREGAGDPVTPDASVLVKYSGYLEHMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPTYAYGTLGCPPLIPPNATVLFEIELIDFLDSAESDKFCALSAEQQEQFPLQKVLKVAATEREFGNYLFRQNRFCDAKVRYKRALLLLHRRLAICEEQHLVEPAELLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYEQARDFLVRAQKEQPCNHDINNELKKLSSHYRDYVDREREMCHRMFAPCGSGSSVGGN | null | null | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; piRNA processing [GO:0034587]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; regulatory ncRNA-mediated gene silencing [GO:0031047]; siRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141007]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; synaptonemal complex [GO:0000795] | Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802] | PF00254; | 3.10.50.40;1.25.40.10; | FKBP6 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Does not localize to pi-bodies. Localizes to meiotic chromosome cores and regions of homologous chromosome synapsis (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZQF9 | LX12E_RAT | MGKYKILVVTGDSLLAGSTNLVQLWLVGEHAEADLGKQLRPLRGRKTELEIDVPLHLGRLLVVKLRKHKGLLDSDWFCKWITVQGPGIQGEAFFPCYSWVQGKETIYLPEGTALKVNDDTKNLFRKYREQELEDRRNVYRWGSWKEGLILPIAGSTERDLPRNQRFMEDKDLDFSLSLAKVLKDFAIKGTLDFVSRVQHLEDYQKVFPHSKTALAGRVRDSWKEDALFGYQFLNGANPMLLRRSKRLPARLVLPPGMEDLQTQLEKELKAGSLFEADFSLLDGVKPNVIIFKQQHVAAPLVMLKLQSDGRLLPMVIQLQPPRHGCPPPLLFLPSDPPMAWLLAKIWVRSSDFQVHQLQSHLLRGHLMAEVISVATMRSLPSLHPIYKLLAPHFRYTMEINTLARNNLVSEWGIFDLVVSTGSGGHVDILQRATACLTYRSFCPPDDLADRGLLDVKSSLYARDALRLWEIISRYVGRMVELFYKNDREVKEDPELQVWCREVTEIGLLGAQDRGFPLSLESRAQLCRFVTMCIFTCTGQHASTHLGQLDWYSWIPNGPCTMRKPPPTSKNVTEGDILDALPCLQQARMQITFTKFLGRHQPVMVALGQHKEEYFSDPGARAVLKQFQEELAVMDKEIEVRNASLDLPYEYLRPSMVENSVTI | 1.13.11.-; 1.13.11.31 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:23382512}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evidence={ECO:0000305|PubMed:23382512}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:41756, ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:78040; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41757; Evidence={ECO:0000250|UniProtKB:P55249}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(8Z,10E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:41328, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:78047; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41329; Evidence={ECO:0000250|UniProtKB:P55249}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:41324, ChEBI:CHEBI:15379, ChEBI:CHEBI:78043, ChEBI:CHEBI:78046; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41325; Evidence={ECO:0000250|UniProtKB:P55249}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:41315, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78035; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41316; Evidence={ECO:0000250|UniProtKB:P55249}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781; Evidence={ECO:0000250|UniProtKB:P55249}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:41332, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:78048; Evidence={ECO:0000250|UniProtKB:P55249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41333; Evidence={ECO:0000250|UniProtKB:P55249}; | null | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. | null | null | FUNCTION: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:23382512). Shows increasing catalytic activity within the series arachidonic acid < 5,8,11-eicosatrienoic acid < linoleic acid < 8,11,14-eicosatrienoic acid (By similarity). {ECO:0000250|UniProtKB:P55249, ECO:0000269|PubMed:23382512}. | Rattus norvegicus (Rat) |
D3ZQL6 | MILK1_RAT | MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFQSLSKENVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFTSSGQAAASPPKPGKDPAAPSPTSTSPAVQPGEEAQGDDLSPDSLSEQGKPQPPSSACAACGQRVHLVQRYLAEGRLYHRHCFRCRQCSSTLVPGSYSSGPEEGTFVCAERCTRLGLGGRSGTRPLSLQKQQPAAAAEAKDGEDSDLSKSVVVVAAEADGLQASSEVQPHTLTKPPLPSKPQDLASPPVSRPTPAPRKASESSALTPPTPRPRSSLQQDGMVEQSVSGDLVNGRLQELPVPKPRGTPKLSERMTAPRKDPPWITLVQTEPKKKPAPLPPSSGPGPLSQASRQVENGGLEEKTQKSPAAEPEPKPYNPFEEEEEEEEASVPAVPSPAPAPPETTPKSLHPWYNITPTSSPKTKKRPAPKAPSASPLVLHASRLSHSEPPSATPSPALSVESLSSESSSHTANTEPSEPPAVPKSSSDPAVHVPGTPGTSANSVTPSAHSSLSSSGELGQPSGEQMPQARTRGSPGTHSTKPFSGATPTPFLLAGDQKSPAPPMGSSSPQMLIKSSCKENPFNRKPSPSTSPTVRKATKGAKPVRPPAPGHGFPLIKRKVQADQYIPEEDIYGEMDSIERQLDALEHSGVLLEEKLRGGANEGSEDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEFELRCLLNKPEKDWTDDDRAREKVLMQELMTLIEQRDAIVNCLDEDRQREEEEDKMLETMIKKKDFQREAESDSKKKGKFKTMKVLKLLGNKRDAKSKAPTGKS | null | null | actin cytoskeleton organization [GO:0030036]; cellular response to nerve growth factor stimulus [GO:1990090]; endocytic recycling [GO:0032456]; endocytosis [GO:0006897]; neuron projection development [GO:0031175]; plasma membrane tubulation [GO:0097320]; protein localization to endosome [GO:0036010]; protein targeting to membrane [GO:0006612]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; slow endocytic recycling [GO:0032458] | cytoplasmic side of endosome membrane [GO:0010009]; endosome membrane [GO:0010008]; filamentous actin [GO:0031941]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; microtubule organizing center [GO:0005815]; recycling endosome membrane [GO:0055038] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidic acid binding [GO:0070300]; small GTPase binding [GO:0031267] | PF12130;PF00307;PF00412; | 1.10.418.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6 (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth. {ECO:0000269|PubMed:23572513}. | Rattus norvegicus (Rat) |
D3ZQL7 | TPPP_RAT | MADSKAKPTKAANKTPPKSPGDPAKAAKRLSLESEGANEGAAAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O94811}; | astral microtubule organization [GO:0030953]; cell division [GO:0051301]; microtubule bundle formation [GO:0001578]; microtubule nucleation by microtubule organizing center [GO:0051418]; microtubule polymerization [GO:0046785]; myelin assembly [GO:0032288]; negative regulation of tubulin deacetylation [GO:1904428]; oligodendrocyte development [GO:0014003]; oligodendrocyte differentiation [GO:0048709]; positive regulation of myelination [GO:0031643]; positive regulation of protein polymerization [GO:0032273]; positive regulation of protein-containing complex assembly [GO:0031334]; regulation of microtubule cytoskeleton organization [GO:0070507] | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic Golgi apparatus [GO:0150051] | GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule nucleator activity [GO:0140490]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631] | PF05517; | 1.10.238.10; | TPPP family | PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity. Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis. Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase. Phosphorylation by CDK1 inhibits the microtubule polymerizing activity. {ECO:0000250|UniProtKB:O94811}.; PTM: Degraded by the proteasome; zinc-binding inhibits degradation by the proteasome. {ECO:0000250|UniProtKB:O94811}. | SUBCELLULAR LOCATION: Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O94811}. Nucleus {ECO:0000250|UniProtKB:O94811}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O94811}. Note=Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (PubMed:31522887). Mainly localizes to the cytoskeleton. Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences. Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. During mitosis, colocalizes with LIMK2 at the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:O94811, ECO:0000269|PubMed:31522887}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:O94811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:O94811}; | null | null | null | null | FUNCTION: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:19606501). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (By similarity). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (By similarity). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity). {ECO:0000250|UniProtKB:O94811, ECO:0000269|PubMed:19606501}. | Rattus norvegicus (Rat) |
D3ZR10 | DCDC2_RAT | MNGPSPRSSHLSQPVVKSVLVYRNGDPFFAGRRVVIHEKKVSSFDIFLKEVTGGVQAPFGAVRNIYTPRTGHRIRKLDQIESGGNYVAGGQEAFKKLNYLDIGEIKKRPMEAVNTEVKPVIHSKINVSARFRKALHEPCTIFLIANGDLISPASRLLIPRKALNQWDHVLQMVTEKITLRSGAVHRLYTLEGKLVESGAELENGQFYVAVGRDKFKRLPYSELLFDKSAMRRPYGQKASSLPPMVGSRKSKGSGNYRQSKSTIGSSDNSSPQPLKRKGKKDSNSEKPTKVKQSVKSKNSHQAIPDNDEGIFKAGAERSETRGAAEVQEDEDTQVEVPVDQRPAEIVDEEEDGEKTSKDANQKDDFSAMNGEAEDRAGSKVADAPEEEEGIPDQGEKKASPSRVNGGTDEENGEELDQVTEELQPTVDEKGKAEGDNSAQDEAGLDAQRPPRPEVTVTSPQENEGNESNKASSAVA | null | null | cilium assembly [GO:0060271]; dendrite morphogenesis [GO:0048813]; intracellular signal transduction [GO:0035556]; neuron migration [GO:0001764]; neuronal action potential [GO:0019228]; positive regulation of smoothened signaling pathway [GO:0045880]; regulation of cilium assembly [GO:1902017]; regulation of Wnt signaling pathway [GO:0030111]; sensory perception of sound [GO:0007605]; synaptic transmission, glutamatergic [GO:0035249]; visual learning [GO:0008542] | axoneme [GO:0005930]; centriolar satellite [GO:0034451]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinocilium [GO:0060091]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; synapse [GO:0045202] | kinesin binding [GO:0019894] | PF03607; | 3.10.20.230; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium {ECO:0000269|PubMed:25601850}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25601850}. Note=Localizes to the ciliary axoneme and to mitotic spindle fibers in a cell-cycle-dependent manner. {ECO:0000250|UniProtKB:Q9UHG0}. | null | null | null | null | null | FUNCTION: Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex (PubMed:16278297). Involved in the control of ciliogenesis and ciliary length (By similarity). {ECO:0000250|UniProtKB:Q9UHG0, ECO:0000269|PubMed:16278297}. | Rattus norvegicus (Rat) |
D3ZRC4 | PLPL8_RAT | MSINLTLDIYIYFLNNARSFCGKQRSKQLNFLCSKQYWRMNHVNVHREFHTSKKSCKWNRSEAHCSKHWHSSSNHGVHIGIVKLSTSAPKGLTKVSIHMSRIKSTLNSVSKAIFGSQNEMVSRLAQFKPSSRIFRKVSDRGWLKHKNVKQAIESLKNYSDKSAEKNSFAEQKSYFADKEEGSDKHSLYHYAYRITTRFGESFYFLANHINSYFKNKEKMSQIKEDRQLQDKPCLEESKSISPSPDILTDRPDSGPPLNVEDKLSSSTQLPEALPVSTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKSDPKSQPEEEEEPSKTDEPICKDKKAEEKKRVLLQREKIIARVSIDNRTRALVQALRRTTDPKLCITRVEELTFHLLEFPEGKGVAVKEKIIPYLLRLRQIKDETLQAAVREILALIGYVDPVKGRGIRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTQNVIVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGQTPKAFVFRNYGHFPGTNSHYLGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTTTYTSLKTKLSNVISSATDTEEVHIMLDGLLPADTYFRFNPVICENIPLDESRNEKLDQLQLEGMKYLERNDEKMKKLAKILSREKTTLQKISDWIKLKSDMYEGLPFFSKL | 3.1.1.-; 3.1.1.5 | null | arachidonic acid metabolic process [GO:0019369]; arachidonic acid secretion [GO:0050482]; cardiolipin metabolic process [GO:0032048]; fatty acid metabolic process [GO:0006631]; intracellular signal transduction [GO:0035556]; linoleic acid metabolic process [GO:0043651]; lipid homeostasis [GO:0055088]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; prostaglandin biosynthetic process [GO:0001516]; regulation of cellular response to oxidative stress [GO:1900407]; triglyceride homeostasis [GO:0070328] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A1 activity [GO:0008970] | PF01734; | 3.40.1090.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NP80}. Microsome membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NP80}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NP80}. Peroxisome membrane {ECO:0000305|PubMed:15908428}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:44068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:77286, ChEBI:CHEBI:77287; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44069; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40643, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:58168, ChEBI:CHEBI:60000; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:58168, ChEBI:CHEBI:75063; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40820; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40639, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:64381, ChEBI:CHEBI:75069; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40647, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:64381, ChEBI:CHEBI:75067; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40648; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41063, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74963, ChEBI:CHEBI:76085; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41064; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z)-hexadecenyl-2 (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40579, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73850, ChEBI:CHEBI:77292; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40580; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-hexadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:67156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73850, ChEBI:CHEBI:86232; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67157; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:52812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52813; Evidence={ECO:0000250|UniProtKB:Q9NP80}; CATALYTIC ACTIVITY: Reaction=1'-[1-acyl-2-(9-hydroxy-(10E,12Z)-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1,2-diacyl-sn-glycero-3-phospho]-glycerol + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + 9-hydroxy-(10E,12Z)-octadecadienoate + H(+); Xref=Rhea:RHEA:67272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64743, ChEBI:CHEBI:133820, ChEBI:CHEBI:167908; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67273; Evidence={ECO:0000250|UniProtKB:Q9NP80}; | null | PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q9NP80}. | null | null | FUNCTION: Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors. Hydrolyzes phosphatidylethanolamine, phosphatidylcholine and probably phosphatidylinositol with a possible preference for the former. Has also a broad substrate specificity in terms of fatty acid moieties, hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal rates from either the sn-1 or sn-2 position in diacyl phosphatidylcholine. However, has a weak activity toward polyunsaturated fatty acids at the sn-2 position, and thereby favors the production of 2-arachidonoyl lysophosphatidylcholine, a key branch point metabolite in eicosanoid signaling. On the other hand, can produce arachidonic acid from the sn-1 position of diacyl phospholipid and from the sn-2 position of arachidonate-containing plasmalogen substrates. Therefore, plays an important role in the mobilization of arachidonic acid in response to cellular stimuli and the generation of lipid second messengers. Can also hydrolyze lysophosphatidylcholine. In the mitochondrial compartment, catalyzes the hydrolysis and release of oxidized aliphatic chains from cardiolipin and integrates mitochondrial bioenergetics and signaling. It is essential for maintaining efficient bioenergetic mitochondrial function through tailoring mitochondrial membrane lipid metabolism and composition. {ECO:0000250|UniProtKB:Q8K1N1, ECO:0000250|UniProtKB:Q9NP80}. | Rattus norvegicus (Rat) |
D3ZS74 | OMA1_RAT | MNFLYGLQSATRNQFLSGVNTLARRRTWTPPAGCPLASRLPAVNANWGLSTVSHCYSVILLPRNLHFCRTLKNKRSRCLSSAQSKEMGVLTYNWTVWGDASCSPNYAAIREVRSFHTSAPRQAAPVPLLMLILKPVQKLLAIIVGRGIRKWWQALPPDKKALFKDSVKRNKWRLLLGLSAFGLLFVVFYFTHLEVSPVTGRSKLLLVGKEHFRLLSDLEYEVWMEEFKNDLLPEEDPRYLTVKKVVYHLTQCNQDVPGVSEINWVVHVVHSPKVNAFVLPNGQVFVFTGLLNSVTDMHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLGMIFLTMIWAICPRDSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKIGLQLAAKACVDVRASSVFWQQMEFSESLHGYPKLPEWLSTHPSHGNRAEYLDRLIPQALKLREVCNCPPLSGPDPRLLFRLTVKHLLEDSEKEDLNITVKKQKPDALPIQKQEQIPLTYALGKRTAG | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O75844}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844}; | cristae formation [GO:0042407]; diet induced thermogenesis [GO:0002024]; energy homeostasis [GO:0097009]; glucose metabolic process [GO:0006006]; HRI-mediated signaling [GO:0140468]; integrated stress response signaling [GO:0140467]; lipid metabolic process [GO:0006629]; mitochondrial protein processing [GO:0034982]; mitochondrial respiratory chain complex assembly [GO:0033108]; mitochondrion organization [GO:0007005]; negative regulation of mitochondrial fusion [GO:0010637]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cold-induced thermogenesis [GO:0120162]; protein autoprocessing [GO:0016540]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; regulation of cristae formation [GO:1903850]; zymogen activation [GO:0031638] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01435; | 3.30.2010.10; | Peptidase M48 family | PTM: Autocatalytically cleaved in response to mitochondrial depolarization both at the N-terminus and C-terminus to generate the short active form (S-OMA1). Autocatalytic processing at the C-terminus takes place at residues 426-435. The S-OMA1 form is unstable (By similarity). OMA1 pre-processing by AFG3L2 may participate in maturation before OMA1 autocatalytic cleavage (By similarity). Degraded by YMEL1 in response to membrane depolarization (By similarity). Protein turnover is regulated by prohibitin (PHB and PHB2), which promotes degradation of OMA1 in a cardiolipin-binding manner (By similarity). {ECO:0000250|UniProtKB:Q96E52, ECO:0000250|UniProtKB:Q9D8H7}.; PTM: May form a redox-dependent disulfide bond (By similarity). Exists in a semi-oxidized state and is activated by prolonged hypoxia (By similarity). {ECO:0000250|UniProtKB:P36163, ECO:0000250|UniProtKB:Q96E52}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.1 uM for OPA1 {ECO:0000269|PubMed:30926535}; | null | null | null | FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria (PubMed:30926535). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1 (PubMed:30926535). Involved in the fusion of the mitochondrial inner membranes by mediating cleavage of OPA1 at S1 position, generating the soluble OPA1 (S-OPA1), which cooperates with the membrane form (L-OPA1) to coordinate the fusion of mitochondrial inner membranes (By similarity). Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1, leading to excess production of soluble OPA1 (S-OPA1) and negative regulation of mitochondrial fusion (By similarity). Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization (flickering) by catalyzing cleavage of OPA1, leading to excess production of S-OPA1, preventing mitochondrial hyperfusion (By similarity). Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae (By similarity). In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome (By similarity). May also cleave UQCC3 in response to mitochondrial depolarization (By similarity). Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (By similarity). Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions (By similarity). Binds cardiolipin, possibly regulating its protein turnover (By similarity). Required for the stability of the respiratory supercomplexes (By similarity). {ECO:0000250|UniProtKB:Q96E52, ECO:0000250|UniProtKB:Q9D8H7, ECO:0000269|PubMed:30926535}. | Rattus norvegicus (Rat) |
D3ZSI8 | PI51A_RAT | MASASSGPAAAGFSPLDSGVPAGTAASGIKRGTVSEGPYASLMPVKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQREPMNSETQYSIDTRRPAPQKALYSTAMESIQGEARRGGTVETEDHMGGIPARNNKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPTKKFRSGPSFSRRSGPSGNSCTPSQPTASGEHKAQVTTKAEVEPDIHLGRPDVLPQTPPLEEISEGSPVPGPSFSPAVGQPLQILNLSSTLEKLDVAESELTH | 2.7.1.68 | null | actin cytoskeleton organization [GO:0030036]; cell chemotaxis [GO:0060326]; fibroblast migration [GO:0010761]; focal adhesion assembly [GO:0048041]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phospholipid biosynthetic process [GO:0008654]; phosphorylation [GO:0016310]; protein localization to plasma membrane [GO:0072659]; ruffle assembly [GO:0097178] | cytosol [GO:0005829]; lamellipodium [GO:0030027]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]; kinase binding [GO:0019900] | PF01504; | 3.30.810.10;3.30.800.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P70182}. Cytoplasm {ECO:0000250|UniProtKB:P70182}. Nucleus {ECO:0000250|UniProtKB:Q99755}. Nucleus speckle {ECO:0000250|UniProtKB:Q99755}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q99755}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99755}. Note=Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs. {ECO:0000250|UniProtKB:Q99755}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136, ChEBI:CHEBI:77137, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:65356, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, ChEBI:CHEBI:83436, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65357; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376; Evidence={ECO:0000250|UniProtKB:Q99755}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165, ChEBI:CHEBI:77167, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388; Evidence={ECO:0000250|UniProtKB:Q99755}; | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (By similarity). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps. Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (By similarity). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes. Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane. Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (By similarity). {ECO:0000250|UniProtKB:P70182, ECO:0000250|UniProtKB:Q99755}. | Rattus norvegicus (Rat) |
D3ZSZ3 | NLK_RAT | MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner. Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes. {ECO:0000250|UniProtKB:Q9UBE8}. | Rattus norvegicus (Rat) |
D3ZTD8 | SEM5A_RAT | MKGACILAWLFSSLGVWRLARPETQDPAKCQRAEHPVVSYKEIGPWLREFRAENAVDFSRLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVQWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTIRSLSNLTEIHDQISGMARCPYSPQHNSTALLTASGELYAATAMDFPGRDPAIYRSLGTLPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGRDTLVHIIYLATDYGTIKKVRAPLSQSSGSCLLEEIELFPERKSEPIRSLKILHSQSVLFVGLQEHVVKIPLKRCHFHQTRGACIGAQDPYCGWDAVMKKCTSLEESLSMTQWDQSVPTCPTRNLTVDGSFGPWSPWTPCTHTDGTAVGSCLCRSRSCDSPAPQCGGWQCEGPRMEITNCSRNGGWTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHLLCPPHVFWTGWGPWERCTAQCGGGIQARRRTCENGPDCAGCNVEYQPCNTNACPELKKTTPWTPWTPVNISDNGGHYEQRFRYTCKARLPDPNLLEVGRQRIEMRYCSSDGTSGCSTDGLSGDFLRAGRYSAHTVNGAWSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEFQECNILPCPVDGVWSCWSSWSKCSATCGGGHYMRTRSCTNPAPAYGGDICLGLHTEEALCNTQTCPENWSEWSEWSVCDASGTQVRTRQCILLFPVGSQCSGNTTESRPCVFDSNFIPEVSVARSSSVEEKRCGEFNMFHMMAVGLSSSILGCLLTLLVYTYCQRYQQQSHDATVIHPVSPAALNSSITNHINKLDKYDSVEAIKAFNKNNLILEERNKYFNPHLTGKTYSNAYFTDLNNYDEY | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; branching involved in blood vessel morphogenesis [GO:0001569]; branching morphogenesis of an epithelial tube [GO:0048754]; cell chemotaxis [GO:0060326]; detection of light stimulus involved in visual perception [GO:0050908]; diencephalon development [GO:0021536]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of cell adhesion [GO:0007162]; negative regulation of endothelial cell apoptotic process [GO:2000352]; neural crest cell migration [GO:0001755]; neuron projection extension [GO:1990138]; neuron projection guidance [GO:0097485]; positive chemotaxis [GO:0050918]; positive regulation of actin filament depolymerization [GO:0030836]; positive regulation of angiogenesis [GO:0045766]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; semaphorin-plexin signaling pathway [GO:0071526]; signal clustering [GO:1990256] | membrane [GO:0016020]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046]; chemorepellent activity [GO:0045499]; chondroitin sulfate proteoglycan binding [GO:0035373]; heparan sulfate proteoglycan binding [GO:0043395]; semaphorin receptor binding [GO:0030215]; syndecan binding [GO:0045545] | PF01437;PF01403;PF00090; | 3.30.1680.10;2.20.100.10;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis. {ECO:0000250|UniProtKB:Q13591, ECO:0000269|PubMed:15603739, ECO:0000269|PubMed:20696765}. | Rattus norvegicus (Rat) |
D3ZTE0 | FA12_RAT | MTALLFLGSLLMSLDLTLSAPPWKSKEFKDGAGDPSVVLTVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYCLEPKKVKDHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQREKCFESQLLKFFHENEIWFRTGPGGVARCQCKGPQAVCKLLTSQVCRVNPCLNGGTCLLVEDHRLCHCPAGYAGPFCDLDLKATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDNDTRPWCYVWSGDRLSWDYCDLEQCQMPTLTSPVSPESHDMLKPRPPILQSSPRDSTRNQNVVSRTSTVVCGQRFRKRLSSLRRVVGGLVALPGSHPYIAALYWGDSFCAGSLIDPCWVLTAAHCLQKRPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLHEGFSSKTYQHDLALLRLRGRKNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLDRCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQEHTAF | 3.4.21.38 | null | blood coagulation [GO:0007596]; Factor XII activation [GO:0002542]; fibrinolysis [GO:0042730]; plasma kallikrein-kinin cascade [GO:0002353]; positive regulation of blood coagulation [GO:0030194]; positive regulation of fibrinolysis [GO:0051919]; positive regulation of plasminogen activation [GO:0010756]; protein autoprocessing [GO:0016540]; protein processing [GO:0016485]; response to misfolded protein [GO:0051788]; zymogen activation [GO:0031638] | extracellular space [GO:0005615]; rough endoplasmic reticulum [GO:0005791] | calcium ion binding [GO:0005509]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF00039;PF00040;PF00051;PF00089; | 2.10.10.10;2.10.25.10;2.40.20.10;2.40.10.10; | Peptidase S1 family | PTM: O- and N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.; EC=3.4.21.38; | null | null | null | null | FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZTL1 | PO4F3_RAT | MMAMNAKQPFGMHPVLQEPKFSSLHSGSEAMRRVCLPAPQLQGNIFGSFDESLLARAEALAAVDIVSHGKNHPFKPDATYHTMSSVPCTSTSPTVPISHPAALTSHPHHPVHQGLEGDLLEHISPTLSVSGLGAPEHSVMPAQIHPHHLGAMGHLHQAMGMSHPHAVAPHSAMPACLSDVESDPRELEAFAERFKQRRIKLGVTQADVGAALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPVLQAWLEEAEAAYREKNSKPELFNGSERKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAVH | null | null | axon extension [GO:0048675]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; inner ear receptor cell differentiation [GO:0060113]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; retinal ganglion cell axon guidance [GO:0031290]; sensory perception of sound [GO:0007605]; vestibulocochlear nerve development [GO:0021562] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15319}. Cytoplasm {ECO:0000250|UniProtKB:Q15319}. Note=Preferentially localized in the nucleus. {ECO:0000250|UniProtKB:Q15319}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator. Acts by binding to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Involved in the auditory system development, required for terminal differentiation of hair cells in the inner ear. {ECO:0000250|UniProtKB:Q63955}. | Rattus norvegicus (Rat) |
D3ZTT2 | LYPD6_RAT | MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL | null | null | positive regulation of canonical Wnt signaling pathway [GO:0090263] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular region [GO:0005576]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | acetylcholine receptor inhibitor activity [GO:0030550]; acetylcholine receptor regulator activity [GO:0030548] | PF16975; | 2.10.60.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86Y78}. Cytoplasm {ECO:0000250|UniProtKB:Q86Y78}. Cell membrane {ECO:0000269|PubMed:27344019}; Lipid-anchor, GPI-anchor {ECO:0000255}. Synapse, synaptosome {ECO:0000269|PubMed:27344019}. Membrane raft {ECO:0000250|UniProtKB:Q66IA6}. Cell projection, dendrite {ECO:0000269|PubMed:34631692}. Perikaryon {ECO:0000269|PubMed:34631692}. Note=Colocalizes with alpha-3:beta-4- and alpha-7- nicotinic acetylcholine receptors (nAChRs) in the primary cortex and hippocampus. {ECO:0000269|PubMed:34631692}. | null | null | null | null | null | FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain (PubMed:27344019). Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity). {ECO:0000250|UniProtKB:Q66IA6, ECO:0000250|UniProtKB:Q86Y78, ECO:0000269|PubMed:27344019}. | Rattus norvegicus (Rat) |
D3ZTV3 | FLRT2_RAT | MGLQTAKWPSHGTFVLKFWLIMSLGLYSHVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIADGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANLRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNMNLLSCPTTTPGLPVFTPAPSTVSPTTQSPTVSVPSPSRGSVPPAPAPSKLPTIPDWDGRERATPPISERIQLSIHFVNDTSIQVSWLSLFTVMAYKLTWVKMGHSLVGGIVQERIVSGEKQHLSLVNLEPRSTYRICLVPLDAFNYRTVEDTICSEATTHASYLNNGSNTASSHEQTTSHTMGSPFLLAGLIGGAVIFVLVVLLSVFCWHMHKKGRYTSQKWKYNRGRRKDDYCEAGTKKDNSILEMTETSFQIVSLNNDQLLKGDFRLQPIYTPNGGINYTDCHIPNNMRYCNSSVPDLEHCHT | null | null | axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; cell adhesion involved in heart morphogenesis [GO:0061343]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart morphogenesis [GO:0003007]; positive regulation of synapse assembly [GO:0051965]; regulation of neuron migration [GO:2001222] | cell-cell junction [GO:0005911]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202] | chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104] | PF00041;PF13855;PF01463; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLU0}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BLU0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BLU0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BLU0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BLU0}. Synapse, synaptosome {ECO:0000269|PubMed:22405201}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BLU0}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8BLU0}. Microsome membrane {ECO:0000250|UniProtKB:Q8BLU0}. Secreted {ECO:0000250|UniProtKB:Q8BLU0}. Note=Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BLU0}. | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis. {ECO:0000250|UniProtKB:Q8BLU0}. | Rattus norvegicus (Rat) |
D3ZU57 | RIOX1_RAT | MDELPNGNGAAPLKRGRGRRRRQPQPRGASVLALPLRPRKVRRHRKSAASRVAALRARALLSEDSDSNVESVRGKRERPAELPEASRSAEPRPVPVRPRPASATLPRRVEGRAALSRNLGKPAPLPGSHVDDPERPWDSPLQQVLAELNGIPSSRRRAARLFEWLLAPLPPDHFYRRLWEREAVLVRRQDHSYYEGLFSTSDLDWMLRYEDVHFGQHLDAARYIDGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSPTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRDPSEELALTSSPNFSQEDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAVLPLAMQAAIEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVHGLPIRWEAGEPVNVGAQLTTETQVHMLQDGIARLVGEGGRLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLRSYPEFVRVGDLPCDSVEDQLSLATMLYDKGLLLTKTPLVLS | 1.14.11.27; 1.14.11.79 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9JJF3}; | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of osteoblast differentiation [GO:0045668] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506]; peptidyl-histidine dioxygenase activity [GO:0036139]; protein demethylase activity [GO:0140457] | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6W3}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6W3}. Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. {ECO:0000250|UniProtKB:Q9H6W3}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.27; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl-[protein] + O2 = CO2 + formaldehyde + L-lysyl-[protein] + succinate; Xref=Rhea:RHEA:60924, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60925; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L-histidyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:54256, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:13840, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29979, ChEBI:CHEBI:30031, ChEBI:CHEBI:138021; EC=1.14.11.79; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54257; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis. Participates in MYC-induced transcriptional activation (By similarity). {ECO:0000250|UniProtKB:Q9H6W3, ECO:0000250|UniProtKB:Q9JJF3}. | Rattus norvegicus (Rat) |
D3ZUA0 | MTD2L_RAT | MATRARGLSLLRGRLGRGPARAPGVAERAWRGFGSSSRRHEAVIISGTEMAKQIRRELQQGVESWLALGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELIVKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRHTPREQLKAHTQLAEIIIVAAGIPGLITADMVREGATVIDVGINYVQDPVTGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNITY | 1.5.1.15; 1.5.1.5; 3.5.4.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24733394}; | 10-formyltetrahydrofolate metabolic process [GO:0009256]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999] | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488] | PF00763;PF02882; | 3.40.50.10860;3.40.50.720; | Tetrahydrofolate dehydrogenase/cyclohydrolase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21163947}; Peripheral membrane protein {ECO:0000269|PubMed:21163947}; Matrix side {ECO:0000269|PubMed:21163947}. | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:21163947, ECO:0000269|PubMed:24733394}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.15; Evidence={ECO:0000269|PubMed:24733394}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000269|PubMed:24733394}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=147 uM for NAD(+) {ECO:0000269|PubMed:24733394}; KM=537 uM for NADP(+) {ECO:0000269|PubMed:24733394}; KM=40 uM for 5,10-methylenetetrahydrofolate (in presence of NAD(+)) {ECO:0000269|PubMed:24733394}; KM=42 uM for 5,10-methylenetetrahydrofolate (in presence of NADP(+)) {ECO:0000269|PubMed:24733394}; KM=130 uM for tetrahydropteroylpentaglutamate/H4PteGlu5 (in presence of NAD(+)) {ECO:0000269|PubMed:24733394}; KM=153 uM for tetrahydropteroylpentaglutamate/H4PteGlu5 (in presence of NADP(+)) {ECO:0000269|PubMed:24733394}; Note=Has similar catalytic efficiencies, at physiological concentrations, with either NAD(+) or NADP(+) as substrates for the dehydrogenation of (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate. {ECO:0000269|PubMed:24733394}; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000269|PubMed:24733394}. | null | null | FUNCTION: [Isoform 1]: Bifunctional mitochondrial folate-interconverting enzyme that has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. {ECO:0000269|PubMed:21163947, ECO:0000269|PubMed:24733394}.; FUNCTION: [Isoform 2]: Has no NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase activity. {ECO:0000269|PubMed:24733394}. | Rattus norvegicus (Rat) |
D3ZUE1 | GA2L2_RAT | MSQHVGHGRKPRTPGPPVRSIRPFKSSEQYLEVMKEDLAEWLRDLYGLDIDAANFLRVLETGLVLCRHANTVTEAALAFLAEAPERVQKIPMPQVGVFCNGAAQPGTFQARDNISNFIQWCRKEMGIQEVLMFETEDLVLRKNVKSVVLCLLELGRRAWRFGVAAPSLVYLEEEIEEELRRDLDLPSPDPPPPVPPARRPCHFHNLDQMVQSLVSHCTCPVQFSMVKISDGKYRVGDSNTLIFIRILRSHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPGPPVQHEVKVQDGPSQPQPLMTISRSQSPLPPVDWKTYTSSSRKLRPPTPSSSGPRSEFPARARTPREMAPFLRSQEKPTLSQRMSSPGPQLSSPCRGPDLQSTLSERRVNRSPGELPRGRTPTSWVPKEADSQGAHTKAPIPQRLQIPETTSKKTPARGPSPPPRSSSLASPHTIWLPDQGASPEISEPMSAQSSSPGKGLTKIPIRLSPARPPTPGRGSLGTEGGGSMQRGSLSSRALAGNLDRSTHGHHSVDVSKDHQKVIQISSGTEDPRSLGTQERKERYTSLPLGRTREPALYDNLKEELVANMKLLEVGAACTQGTRSQAIPRSGVYVPSLGGMWPEPRGPYDKVIQELVQGPPRLLKVDLKAWKVGSECLPRPIVNPGSPKEEQVSRERGTRRKARPSAQGTTVKTTSPARGQDCSTLPVSANLKAPTHSCSDPSSDKAKVCLGKGKRTLRKPQKVPSIYKLKLRPRIRPRRDHRPEKRPSRIPKPLVYPFLGPARTAPGSRLLKATLGGTGGDVNGVGKKEEEKKKETSISLESSIQPSESREPMQLDGTPLPPEEESWV | null | null | actin crosslink formation [GO:0051764]; microtubule bundle formation [GO:0001578]; negative regulation of microtubule depolymerization [GO:0007026]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; protein localization to microtubule plus-end [GO:1904825]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296]; regulation of microtubule polymerization or depolymerization [GO:0031110] | actin filament [GO:0005884]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; microtubule plus-end [GO:0035371]; plasma membrane [GO:0005886]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; cytoskeletal anchor activity [GO:0008093]; G-protein alpha-subunit binding [GO:0001965]; microtubule binding [GO:0008017] | PF00307;PF02187; | 1.10.418.10;3.30.920.20; | GAS2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23994616}. Cell membrane {ECO:0000269|PubMed:23994616}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8NHY3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8NHY3}. Note=Colocalizes with ADORA2A at neuronal processes (PubMed:23994616). Colocalizes with and tracks the tips of microtubule plus ends (By similarity). {ECO:0000250|UniProtKB:Q8NHY3, ECO:0000269|PubMed:23994616}. | null | null | null | null | null | FUNCTION: Involved in the cross-linking of microtubules and microfilaments (By similarity). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (By similarity). Enhances ADORA2-mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity). {ECO:0000250|UniProtKB:Q5SSG4, ECO:0000250|UniProtKB:Q8NHY3}. | Rattus norvegicus (Rat) |
D3ZUI5 | COBL_RAT | MKARAPPPPGKPAAQNVHSEQKLPHDATLGSQQSLVHLKEALHNSTLDITVVLPSGLEKQSVVSGSRAVMDLLVELCLQNHLNPSHHVLEIWSSETQQPLSFKPNTLIGSLNAHTVFLKEKVPEEKGKPGLTKAPEKSVRLVVNYLRTQKAVMRVSPEVPLQNILPVICAKCEVSPDHVVLLRDNIAGEELELSKSLNELGIKELYAWDNRREMLRKSSLGNDETDKEKKKFLGFFKVNKRSNSKAEHLGLSGADSDEDPSKSASGGDLNGCVTTPNSPSLHSRSLTLGPSLSLGNISGMSMKSDMKKRRAPPPPSPGLLGQDKVSEKASLSSQADLQKKKRRAPAPPPPQPPPPSPVVPNRKEDKEENRKSTVGMEENYETDTSSLTSSVNGVSNHSLQEAIIPDSGVDDIPVTFIGEVSDEPFDSGLFFSGSNNAAALNQGGIASQRSHLPPYQTEQSQPFIRTNRKEPDPSLPSQDYRKRNQPILANTSENENPVGIDPRVTSFVSKPSTDDPKAKDKDKMCGSGPSEKTQTGHRVNSLPVNPRVGEDENSNSALPPWSHHGQASGGSYGLKYGLTTYKIVPPKPEMRCYDRDVSLSTGAIKIDELGNLMSPHMNGSRTISKPSAVAETEAPPIGKVKEFWRRNSMEKYLNGPAECTVKKAPSTTITATSEKPQRDETKAGFTLTTPEQQPASQEYGAPPEEDRSRPHSAVSCPVKVPAPNPTDITFLKPQRRTSSQYVASAIAKKMGPPKVHADVVRPHKKTAEQGHEEAKLARPPPAWKDSAVPNLCSEAGQCEHGTNQGSVRLPSNPGGQLPADHPKVEVNSTYGKSATHNSPAAVHRNSYFLPGRSSQRDRVSVGQSCGFHEKQTISNQKMNSTSNPSQALDKAHPAPLLLTEARDSGRILVNGSAQTPGNCEPPHSQKESTLTSYIILQTEEKPSPLSADGQNSDDALPSSIFGPKKKFKPVVQRPLPKDISLHSALMEAIHTSGGRDKLRKTAEQASEGRPKKPSYVEAESERSALLAAIRGHSGTLSLRKVSSLASEELQSFRDAALMAPGVDKPQQEDRGLPPPPALPPPSTPASQVPSASIPVSRFSIGTLSNPVNARQALMDAIRSGTGAARLRKVPLLV | null | null | actin cytoskeleton organization [GO:0030036]; actin filament network formation [GO:0051639]; actin filament polymerization [GO:0030041]; collateral sprouting in absence of injury [GO:0048669]; digestive tract development [GO:0048565]; embryonic axis specification [GO:0000578]; floor plate development [GO:0033504]; liver development [GO:0001889]; neural tube closure [GO:0001843]; notochord development [GO:0030903]; positive regulation of dendrite development [GO:1900006]; positive regulation of ruffle assembly [GO:1900029]; somite specification [GO:0001757] | actin filament [GO:0005884]; axon [GO:0030424]; axonal growth cone [GO:0044295]; cell cortex [GO:0005938]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic growth cone [GO:0044294]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; terminal web [GO:1990357] | actin monomer binding [GO:0003785] | PF09469;PF02205; | null | null | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle. Cytoplasm. Cytoplasm, cytosol. Note=Recruited to the cell membrane via interaction with PACSIN1. Colocalizes with the actin cytoskeleton. Detected throughout the neuron cell body, as well as in axons and dendrites. | null | null | null | null | null | FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates dendrite branching in Purkinje cells (By similarity). Regulates neuron morphogenesis and increases branching of axons and dendrites. {ECO:0000250, ECO:0000269|PubMed:21725280, ECO:0000269|PubMed:23223303}. | Rattus norvegicus (Rat) |
D3ZUM2 | SARM1_RAT | MVLTLLFSAYKLCRFFIMSGPRPGADRLTVPGPDRSGGTSPWWAAGGRGSREVSPGVGTEVQGALERSLPELQQALSELKQASAAQAVGAGLAEVFQLVEEAWLLPAVGREVAQGLCDAIRLDGGLDLLLRLLQAPELETRVQAARLLEQILVAENRDRVARIGLGVILNLSKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCALHGGQTVQRCMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVEHSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQSLVLLLDSSRLEAQCIGAFYLCAEAAIKSLQGKTKVFSDIGAIQSLKRLVSYSTNGTTSTLAKRALRLLGEEVPRRILPCVASWKEAEVQTWLQQIGFSQYCENFRDQQVDGDLLLRLTDEELQTDLGMKSSITRKRFFRELTELKTFASYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRTRILSAAREMLHSPLPCTGGKPSGDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVMAARNFVLVLSAGALDKCMQDHECKDWVHKEIVTALSCSKNIVPIIDGFEWPEPQALPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRPSQDSSAGSDTSLEGATSMGLP | 3.2.2.-; 3.2.2.6 | null | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; NAD catabolic process [GO:0019677]; negative regulation of MyD88-independent toll-like receptor signaling pathway [GO:0034128]; nervous system development [GO:0007399]; nervous system process [GO:0050877]; protein localization to mitochondrion [GO:0070585]; regulation of dendrite morphogenesis [GO:0048814]; regulation of neuron apoptotic process [GO:0043523]; response to axon injury [GO:0048678]; response to glucose [GO:0009749]; signal transduction [GO:0007165] | axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling adaptor activity [GO:0035591] | PF07647;PF13676; | 1.25.10.10;3.40.50.10140;1.10.150.50; | SARM1 family | PTM: Phosphorylation at Ser-548 by JNK kinases (MAPK8, MAPK9 and /or MAPK10) enhance the NAD(+) hydrolase (NADase) activity (PubMed:32968873). Phosphorylation at Ser-548 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration (By similarity). Phosphorylation at Ser-548 increases in response to cerebral ischemia/reperfusion (I/R) injury (PubMed:32968873). {ECO:0000250|UniProtKB:Q6SZW1, ECO:0000269|PubMed:32968873}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6SZW1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion {ECO:0000250|UniProtKB:Q6SZW1}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q6PDS3}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; CATALYTIC ACTIVITY: Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:73672; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; | null | null | null | null | FUNCTION: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site. Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules. Can activate neuronal cell death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38. {ECO:0000250|UniProtKB:Q6PDS3, ECO:0000250|UniProtKB:Q6SZW1}. | Rattus norvegicus (Rat) |
D3ZUQ0 | RIPL1_RAT | MEEPLGSPPAALSALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRVERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLNHKDVGFSEEELQKHEGMSERERQVMKRLKEVVDKQRDEIRAKDRELVLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEEAEIPPQPDGEESISDAEKAALDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEIEEENRIPQPPPITHPRTSPQPESGIKRLFSFFSRDKRRLANTQRPTHIHESFGQWAITHRDDGYTEQGQEALQHL | null | null | cilium assembly [GO:0060271]; epithelial cell morphogenesis [GO:0003382]; nitric oxide mediated signal transduction [GO:0007263]; protein transport from ciliary membrane to plasma membrane [GO:1903445] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | dynein light intermediate chain binding [GO:0051959]; protein dimerization activity [GO:0046983]; small GTPase binding [GO:0031267] | PF09744;PF11461; | 1.20.58.1770;6.10.230.10; | RILPL family | PTM: S-nitrosylation is required for the interaction with GAPDH. {ECO:0000269|PubMed:19607794}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:30398148}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:30398148}. | null | null | null | null | null | FUNCTION: Plays a role in the regulation of cell shape and polarity (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus (PubMed:19607794). Competes with SIAH1 for binding GAPDH (PubMed:19607794). Does not regulate lysosomal morphology and distribution (By similarity). Binds to RAB10 following LRRK2-mediated RAB10 phosphorylation which leads to inhibition of ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q5EBL4, ECO:0000250|UniProtKB:Q9JJC6, ECO:0000269|PubMed:19607794}. | Rattus norvegicus (Rat) |
D3ZVK1 | MCM8_RAT | MSGAYRGRGFGRGRFQNWKRGRGGGNFSGRWRDRTDLSKAAGNHASEQASQPLLQQSTLDQFIPYKGWKLYFSEVYSNNSPLTEKIQAFEKFFTRHIDLYDKDEIERKGSILVDFKELTKDNEITNLIPDIENALRDAPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLCNGGGTMVNVPHIYARVYNYEPLTHLKNIRATCYGKYISIRGTVVRVSNIKPLCTKMAFQCAACGEIQSFPLPDGKYNLPTKCPVPACRGRSFTPLRSSPLTVTMDWQLIKIQELMSDAQREAGRIPRTIECELVHDLVDSCVPGDTVTVTGIVKVSNSEEGSRSKNDKCMFLLYIEANSVSNSKGQKAQTAEDGCKHGTLMEFSLKDLYAIQEIQAEENLLKLIVNSLCPVIFGHELVKAGLMLALFGGSQKYADDKNRIPIRGDPHVLIVGDPGLGKSQMLQAACNVAPRGVYVCGNTATSSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGVVCSLPARTSIIAAANPVGGHYNKARTVSENLKMGSALLSRFDLVFILLDTPNEQHDHLLSEHVIAIRAGKQRAVSSATVSRVLSQDSNTSVLEVVSEKPLSERLKVAPGEKTDPIPHQLLRKYIGYARQYVHPRLSTEAAQALQDFYLELRKQSQRVGSSPITTRQLESLIRLTEARARLELREEATKEDAEDIIEIMKHSMLGTYSDEFGNLDFERSQHGSGMSNRSTAKRFISALNSIAERTYNNIFQFHQLRQIAKELNIQVADFENFIGSLNDQGYLLKKGPKIYQLQTM | 3.6.4.12 | null | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; DNA duplex unwinding [GO:0032508]; double-strand break repair via homologous recombination [GO:0000724]; female gamete generation [GO:0007292]; male gamete generation [GO:0048232]; protein localization to chromatin [GO:0071168]; protein stabilization [GO:0050821]; recombinational interstrand cross-link repair [GO:0036298] | chromosome [GO:0005694]; MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; MutLbeta complex binding [GO:0032406]; MutSalpha complex binding [GO:0032407]; MutSbeta complex binding [GO:0032408]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116] | PF00493;PF17855;PF17207; | 2.20.28.10;2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9UJA3}; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC). Probably by regulating HR, plays a key role during gametogenesis. Stabilizes MCM9 protein. {ECO:0000250|UniProtKB:Q9CWV1, ECO:0000250|UniProtKB:Q9UJA3}. | Rattus norvegicus (Rat) |
D3ZVM4 | LIN41_RAT | MASFPETDFQICLLCKEMCGSPAPLSSSSSASSSSSQTSTSSAGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAPGGAGPAEALKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGGGPGGAGGHSNHRHHAHHPAQRAAAPAPQPPPGPAASPGSLLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAASAAQQLGLGPPFAGAPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTLGRHGGHSFAYLQDALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTIRGLLQPQEDDRVMFTPPDQALYLALKSFGFVSSGAFAPLTKAAGDGIKRALQGKVASFTVMGYDHNGEPRLSGGDLMSVVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLYNQHIENSPFKVVVKSGRSYVGIGLPVLSFGSEGDGEGKLCRPWGVSVDKEGYIIVADRSNNRIQVFKPCGSFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGSLWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFEANGSFLCKFGAQGSGFGQMDRPSGIAVTPEGLIVVVDFGNNRILIF | 2.3.2.27 | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to organic substance [GO:0071310]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; miRNA processing [GO:0035196]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; negative regulation of translation [GO:0017148]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; post-transcriptional regulation of gene expression [GO:0010608]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; regulation of miRNA-mediated gene silencing [GO:0060964]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of protein metabolic process [GO:0051246]; stem cell proliferation [GO:0072089] | P-body [GO:0000932] | miRNA binding [GO:0035198]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00630;PF01436;PF00643;PF00097; | 3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10; | TRIM/RBCC family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}. | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (By similarity). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity). {ECO:0000250|UniProtKB:Q1PSW8, ECO:0000250|UniProtKB:Q2Q1W2}. | Rattus norvegicus (Rat) |
D3ZVU1 | SPRTN_RAT | MDEDLVVALRLQEEWDVQAARRAAAREPLSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHKQPYYGYVKRATNRAPSAHDYWWADHQKTCGGTYIKIKEPENYAKKGRGKTKAGKQPTSAVENKDKLCRGEAQPLIPFSGKGYVLGDTSTCPSAGKLNTSHMVNDTKGLSGQDHSASGLKLDSNVEVKCEQNGLPNKKPHLVTPLPTASHQSVLSSYFPRVSVANQKAFRNVNGSPVKSGTIDGTKHSASAGAQRKVPPSRASLRNSSKVTAPASATVTSAAGTSAAISREESGSEDQFLNKRPRLEDRTALNNIKEQTQSGGDLEDSSRPTAISTPRSSGGQRRLVNCPVCQGVVLESQINEHLDRCLEGSKTNLRPRRV | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin binding [GO:0043130] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for subsequent acetylation and recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Acetylated following deubiquitination by VCPIP1, leading to recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Phosphorylation by CHEK1 promotes recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Catalyzes proteolytic cleavage of the HMCES DNA-protein cross-link following unfolding by the BRIP1/FANCJ helicase. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4. Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs. Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040}. | Rattus norvegicus (Rat) |
D3ZVU9 | NAT8L_RAT | MHCGPPDMVCETKIVATEDHEALPGAKKDALLAAAGAMWPPLPAAPGPAAAPPPAAGPQPHGGTGGAGPPEGRGVCIREFRAAEQEAARRIFYDGILERIPNTAFRGLRQHPRTQLLYALLAALCFAVTRSLLLTCLVPAGLLALRYYYSRKVILAYLECALHTDMADIEQYYMKPPGSCFWVAVLDGNVVGIVAARAHEEDNTVELLRMSVDSRFRGKGIAKALGRRVLEFAMLHNYSAVVLGTTAVKVAAHKLYESLGFRHMGASDHYVLPGMTLSLAERLFFQVRYHRYRLQLREE | 2.3.1.17 | null | acetate metabolic process [GO:0006083]; aspartate metabolic process [GO:0006531]; positive regulation of dopamine uptake involved in synaptic transmission [GO:0051586] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | aspartate N-acetyltransferase activity [GO:0017188] | PF00583; | 3.40.630.30; | Camello family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}. Microsome membrane {ECO:0000269|PubMed:18621030}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18621030}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3UGX3}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-aspartate = CoA + H(+) + N-acetyl-L-aspartate; Xref=Rhea:RHEA:14165, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29991, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.17; Evidence={ECO:0000269|PubMed:18621030}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166; Evidence={ECO:0000305|PubMed:18621030}; | null | null | null | null | FUNCTION: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from L-aspartate and acetyl-CoA (PubMed:18621030). Promotes dopamine uptake by regulating TNF-alpha expression (By similarity). Attenuates methamphetamine-induced inhibition of dopamine uptake (By similarity). {ECO:0000250|UniProtKB:Q3UGX3, ECO:0000250|UniProtKB:Q8N9F0, ECO:0000269|PubMed:18621030}. | Rattus norvegicus (Rat) |
D3ZVV1 | KHDC3_RAT | MATLKTFRTLVQLKHKLGKAYEIVGEPRLPKWFHVEYLEDPKKMYVEPTLVEIMFGKDGEHIPHVECTLHVLIHVNVWGPEKQAEILIFGPPNFQKDVAQMLSNVAHFCRMKLMEKEALEAGVERRLMAASKATTQPTPVKVRDAATQVAPVQVRDAAIQPAPVKVRDAATQVAPVQVHEVATQPVPVQVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATEPVPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVREAATQQTPVEVADDTQLVQLKAGEAFAQHTSGKVHQDVNGQSPIEVCEGATQRHSVDASEALSQKCPEDLEGGDTETSLDDSYVIIRPSRAVWEPFVML | null | null | actin filament organization [GO:0007015]; establishment of organelle localization [GO:0051656]; mitotic spindle assembly [GO:0090307]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of apoptotic process [GO:0043066]; positive regulation of dendrite development [GO:1900006]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of embryonic development [GO:0040019]; positive regulation of neurogenesis [GO:0050769]; regulation of protein localization [GO:0032880]; replication fork processing [GO:0031297] | apical cortex [GO:0045179]; cell cortex [GO:0005938]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; subcortical maternal complex [GO:0106333] | RNA binding [GO:0003723] | PF16005; | 3.30.1370.10; | KHDC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}. Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome {ECO:0000250|UniProtKB:Q587J8}. Note=Localized to centrosomes during interphase and mitosis (By similarity). Localizes to sites of DNA double-strand break repair (By similarity). {ECO:0000250|UniProtKB:Q587J8, ECO:0000250|UniProtKB:Q9CWU5}. | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Regulates homologous recombination-mediated DNA repair via recruitment of RAD51 to sites of DNA double-strand breaks, and sustainment of PARP1 activity, which in turn modulates downstream ATM activation (By similarity). Activation of ATM or ATR in response to DNA double-strand breaks may be cell-type specific (By similarity). Its role in DNA double-strand break repair is independent of its role in restarting stalled replication forks (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for maintenance of euploidy during cleavage-stage embryogenesis (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process (By similarity). Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function (By similarity). Promotes neural stem cell neurogenesis and neuronal differentiation in the hippocampus (By similarity). May regulate normal development of learning, memory and anxiety (By similarity). Capable of binding RNA (By similarity). {ECO:0000250|UniProtKB:Q9CWU5}. | Rattus norvegicus (Rat) |
D3ZW55 | ITPA_RAT | MAASLVGKKIVFVTGNAKKLEEVIQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAARQVQGPVLVEDTCLCFNALGGLPGPYIKWFLQKLKPEGLYQLLAGFEDKSAYALCTFALSTGDPSQPVLLFRGKTPGQIVMPRGSRDFGWDPCFQPDGYEQTYAEMPKAEKNTISHRFRALFKLQEYFGVTDGAGDH | 3.6.1.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148}; | chromosome organization [GO:0051276]; deoxyribonucleoside triphosphate catabolic process [GO:0009204]; ITP catabolic process [GO:0006193]; nucleoside triphosphate catabolic process [GO:0009143] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | dITP diphosphatase activity [GO:0035870]; identical protein binding [GO:0042802]; ITP diphosphatase activity [GO:0036220]; metal ion binding [GO:0046872]; nucleoside triphosphate diphosphatase activity [GO:0047429]; nucleotide binding [GO:0000166]; XTP diphosphatase activity [GO:0036222] | PF01725; | 3.90.950.10; | HAM1 NTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; | null | null | null | null | FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148}. | Rattus norvegicus (Rat) |
D3ZWK4 | LMBL1_RAT | MEGHSDMEIIRAVKGSATGEINVHLVARDSAGSHPHLPTTTFIIPTNAATLGLPSTALDVSYPREPVHVGAAERVAGSEPVTATILPQLSTGPGTNSTVRLLDWTGVSAPLAGSGMRFRINEYATQNMIEIERPRSPEQRHEGGTAGREADIQHPDVHKDPQEVIPQEPSVDAGSCKCQTCGPQQSIGLDVGSSGDRCPQPFQKRSVIVENSGCTVASELIKPMKKRKHKEYQSPSEESEPEAMKQGKGKDPDREPTPGTSENEEWSRSQLVSSEKKEGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEGVDPQHPSMYFVLTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTKAQAAPKHLFVSQSHSPPPVGFQVGMKLEAVDRMNPSLVCVASVTDVVASRFLVHFDDWDDTYDYWCDASSPYIHPVGWCQKQGKPLTPPQDYPDPDSFCWEKYLEETGTSAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKLHFDGWSHNYDFWIDADHPDIHPAGWCSKTGHPLEPPLRPRESSSASPGGCPPLSHRSPPHTKTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSETTARKKNQSNLSPRKKPRHQGRIGRPPKYRKMPDEDFQALPPSVVHQSLFMSTLPTHADRPLSVCWEQHCKLLPGVAGISASAVSKWTIEEVFGFVQTLTGSEDQARLFKEEMIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNNDDVFK | null | null | chromatin organization [GO:0006325]; hemopoiesis [GO:0030097]; heterochromatin formation [GO:0031507]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of mitotic nuclear division [GO:0007088] | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; condensed chromosome [GO:0000793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; methylated histone binding [GO:0035064]; nucleosome binding [GO:0031491]; SAM domain binding [GO:0032093]; zinc ion binding [GO:0008270] | PF02820;PF00536;PF01530; | 2.30.30.140;4.10.320.30;1.10.150.50; | null | PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Does not colocalize with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZYR1 | FCHO2_RAT | MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYNAKCVEQERLKKEGATPREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPVHPNNVHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPITSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPATLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC | null | null | clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; membrane invagination [GO:0010324]; protein localization to plasma membrane [GO:0072659]; synaptic vesicle endocytosis [GO:0048488] | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; presynaptic endocytic zone membrane [GO:0098835] | identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786] | PF00611;PF10291; | 1.20.1270.60; | FCHO family | PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZYW7 | FRDA_RAT | MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT | 1.16.3.1 | null | [2Fe-2S] cluster assembly [GO:0044571]; [4Fe-4S] cluster assembly [GO:0044572]; adult walking behavior [GO:0007628]; aerobic respiration [GO:0009060]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; embryo development ending in birth or egg hatching [GO:0009792]; heme biosynthetic process [GO:0006783]; intracellular iron ion homeostasis [GO:0006879]; iron import into the mitochondrion [GO:0048250]; iron-sulfur cluster assembly [GO:0016226]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of apoptotic process [GO:0043066]; negative regulation of lipid storage [GO:0010888]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of organ growth [GO:0046621]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; organ growth [GO:0035265]; oxidative phosphorylation [GO:0006119]; positive regulation of axon extension [GO:0045773]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of mitochondrial membrane permeability [GO:0035794]; proprioception [GO:0019230]; protein autoprocessing [GO:0016540]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to iron ion [GO:0010039]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410] | cytosol [GO:0005829]; L-cysteine desulfurase complex [GO:1990221]; mitochondrial iron-sulfur cluster assembly complex [GO:0099128]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; iron chaperone activity [GO:0034986]; metallochaperone activity [GO:0016530] | PF01491; | 3.30.920.10; | Frataxin family | PTM: [Frataxin mature form]: Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (frataxin(81-210)) which is the predominant form. The additional forms, frataxin(56-210) and frataxin(78-210), seem to be produced when the normal maturation process is impaired; their physiological relevance is unsure. {ECO:0000250|UniProtKB:Q16595}. | SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.; SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}. | CATALYTIC ACTIVITY: [Frataxin mature form]: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:Q16595}; | null | null | null | null | FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (By similarity). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation (PubMed:15247478). May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity). {ECO:0000250|UniProtKB:Q16595, ECO:0000250|UniProtKB:Q9H1K1, ECO:0000269|PubMed:15247478}.; FUNCTION: [Extramitochondrial frataxin]: Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival. {ECO:0000250|UniProtKB:Q16595}. | Rattus norvegicus (Rat) |
D3ZZC3 | KLH22_RAT | MAEEQDFAQLCKLSTQPSHSHCVNNTYRSTQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLNRLTQQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYSMEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLGPSPLRDTVASALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTILSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGKYIYAVAGRDYHNNLSAVERYDPATNSWEYVAPLKKEVYAHAGTTLQGKMYITCGRRGEDYLKETHCYDPGSNTWHTLADGPVRRAWHGMAALLDKLFVIGGSNNDAGYRRDVHQVACYSCTSRQWSSVCPLPAGHGEPGIAVLDNRIYVLGGRSHNRGSRTGYVHIYDMEKDCWEEGPQLNNSISGLAACVLTLPRSLLHEQPRGTPNRSQADADFASEVMSVSDWEEFDNSSED | null | null | cell division [GO:0051301]; cellular response to amino acid stimulus [GO:0071230]; cellular response to leucine [GO:0071233]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of autophagy [GO:0010507]; negative regulation of type I interferon production [GO:0032480]; positive regulation of cell growth [GO:0030307]; positive regulation of TORC1 signaling [GO:1904263]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein monoubiquitination [GO:0006513]; ubiquitin-dependent protein catabolic process [GO:0006511] | centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; polar microtubule [GO:0005827] | 14-3-3 protein binding [GO:0071889]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344;PF13415;PF13964; | 1.25.40.420;2.120.10.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}. Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome {ECO:0000250|UniProtKB:Q53GT1}. Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase. Localizes to the nucleus upon amino acid starvation. Relocalizes to the cytosol and associates with lysosomes when amino acids are available. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy. {ECO:0000250|UniProtKB:Q53GT1}. | Rattus norvegicus (Rat) |
D4A055 | CACB4_RAT | MSSSYAKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTTTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTSSSTPMTPLLGRNVGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGCSHDSRHRL | null | null | adult walking behavior [GO:0007628]; calcium ion transport [GO:0006816]; cAMP metabolic process [GO:0046058]; cellular response to leukemia inhibitory factor [GO:1990830]; chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion [GO:0014051]; gamma-aminobutyric acid signaling pathway [GO:0007214]; intracellular calcium ion homeostasis [GO:0006874]; muscle cell development [GO:0055001]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; nervous system process [GO:0050877]; neuromuscular junction development [GO:0007528]; neuronal action potential propagation [GO:0019227]; Peyer's patch development [GO:0048541]; positive regulation of protein localization to nucleolus [GO:1904751]; regulation of membrane potential [GO:0042391]; regulation of synaptic vesicle exocytosis [GO:2000300]; spleen development [GO:0048536]; synaptic transmission, glutamatergic [GO:0035249]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538] | glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; voltage-gated calcium channel complex [GO:0005891] | high voltage-gated calcium channel activity [GO:0008331]; protein kinase binding [GO:0019901]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626] | PF00625;PF12052; | 3.40.50.300;2.30.30.40; | Calcium channel beta subunit family | null | null | null | null | null | null | null | FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000250|UniProtKB:O00305}. | Rattus norvegicus (Rat) |
D4A1F2 | MICA2_RAT | MGENEDEKQAQASQVFENFVQATTCKGTLQAFNILTCLLDLDPLDHRNFYTQLKSKVNTWKAKALWHKLDKRGSHKEYKRGKACSNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDTFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVRVREPPKDQENRKIGWRAEFLPADHALSNFEFDVIIGADGHRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDSTHYFVMTAKKQSLLDKGVILNDYIDTEMLLCAENVNQDNLLSYAREAADFATNYQLPSLDFAINHNGQPDVAMFDFTSMYASENAALMRERQAHQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMVKSWDQGTPPLEVLAERESLYRLLPQTTPENINKNFEQYTLDPATRYPNLNVHCVRPHQVKHLYITKEMDRFPLERWGSVRRSASLSRRESDIRPNKLLTWCQQQTKGYQHVRVTDLTTSWRSGLALCAIIHSFRPELINFDSLNENDVVENNQLAFDVAKREFGILPVTTGKEMASTQEPDKLSMVMYLSKFYELFRGTPLRPMDSRRKNYGENADFGLGKTFFQNNYLNLTLPRKRTPRVDAQTEENDVNKRRRQGFNNLEELPAFSSRSLGSSQEYAKESGNQNKVKYMANQLLAKFEENTRNPSALKQDCPRVSGMGKPVLCSASRPPGTSHCPKLEESTPRLPPPLKRQFSSTVATGQVLRELNQVPASGECPGRPWRARAKSDLQLGGAENLATLPPTCQGALALSGVLRRLQQVEEKVLQKRAQNLANREFHTKNIKEKAAHLASMFGHGDLPQDKLLSKRVPHAHPPSPPSCLPSPDPAAAPSPPAADSVSPARKVLTVGKVSSGIGAAAEVLVNLYLNDHRPKTQATSPDLESLRKAEFPLSLGGRDTCYFCKKRVYVMERLSAEGHFFHRECFRCSVCAAILRVAAYAFDCDEGKFYCKLHFAHCKTSSKQRKRRAELNQQREEEGTWPEQEAARRDVPAESSCAVAAISTPEGSPPDEPISPKKSKSVPKPNSRPMEVEATSPRPSEWTSVRIGPGQDGQDVLAVRVLVTSEDSSSDTESDSGSIIGPCTEACEERPRLPESPPLSQPLTRHISLRETLTQPVSLLLHHKEPQAVPGLQRAYSLQSPSKYQNWRRKFQSNSTPMNQRALSPPKEPPPSSSSSSPSLPSSFSSASVPGHTTDDSSSPQVTYNLHSPQISRDDVSPTPIYLRRARAQGITKEIPLYLPHSPMLESTEHCLVSPDGEELRSPEEISASDGCQKALALGNSESTHKDSYPVSGKDPYLPNQMLALGAAGNTGDLSEESRMGQTGGAELSKERKLGLKKLVLTEEQKTMLLDWNDYTQEHKAGERLAQEKAENGRGNSLKPICSSTLSQAVKEKLLSQKKALGETRTPAAKAPREREVPPPKSPLRLIANAIFRSLLPSSEAGKKTSSKPETKTLPRGQPHAFTRSFSFRKLGSSKDGDQQSPGRHMAKKASAFFSLASPTSKAAQASDLSPPNPILRSRSLPNRPSKMFFATTSLPPSSKVEDVPTLLEKVSLQDAAQGPKKGASHISPLGLKDKSFESFLQECKERKDIGDFFNSPKEKGPPGNRVPSLEKLVQPVDSTSMGQVAHPSSTGQDAQAAVRTQAGKEGSSLVSSLVLVSGPGAPVTEDTSSPTSSSAEEDVETQLSSRLKEKIPRRRRKLEKQMAKQEELKRLHKAQAIQRQLEEVEERQRTSEIQGVRLEKVLRGETADSGTQDEAQLLQEWFKLVLEKNKLMRYESELLIMAQELELEDHQSRLEQKLRQKMLKDEGQKDENDLKEEQEIFEEMMQVIEQRNKLVDSLEEQRIKERTQDQHFENFVLSRGCQLSRT | 1.14.13.225 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; | actin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; heart development [GO:0007507]; heart looping [GO:0001947]; positive regulation of transcription by RNA polymerase II [GO:0045944]; sulfur oxidation [GO:0019417] | actin filament [GO:0005884]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; monooxygenase activity [GO:0004497]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709] | PF12130;PF00307;PF01494;PF00412; | 1.10.418.10;2.10.110.10;3.50.50.60; | Mical family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. Cytoplasm {ECO:0000250|UniProtKB:Q8BML1}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044, ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.225; Evidence={ECO:0000250|UniProtKB:O94851}; | null | null | null | null | FUNCTION: Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (By similarity). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By similarity). {ECO:0000250|UniProtKB:O94851, ECO:0000250|UniProtKB:Q8TDZ2}. | Rattus norvegicus (Rat) |
D4A1J4 | DHRS6_RAT | MGRLEGKVIVLTAAAQGIGRASALAFAREGAKVIATDINEAKLQELENYPGIQTRVLDVTKKRQIDQFASEIEKIDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVENRCVYSATKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARDDPKEALKAFLNRQKTGRFASAEEVALLCVYLASDESAYVTGTPVVIDGGWSL | 1.1.1.-; 1.1.1.104; 1.1.1.30 | null | epithelial cell differentiation [GO:0030855]; fatty acid beta-oxidation [GO:0006635]; heme metabolic process [GO:0042168]; intracellular sequestering of iron ion [GO:0006880]; siderophore biosynthetic process [GO:0019290] | cytoplasm [GO:0005737] | 3-hydroxybutyrate dehydrogenase activity [GO:0003858]; 4-oxoproline reductase activity [GO:0016617]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BUT1}. | CATALYTIC ACTIVITY: Reaction=cis-4-hydroxy-L-proline + NAD(+) = 4-oxo-L-proline + H(+) + NADH; Xref=Rhea:RHEA:13601, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63727, ChEBI:CHEBI:84813; EC=1.1.1.104; Evidence={ECO:0000269|PubMed:35150746}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13603; Evidence={ECO:0000269|PubMed:35150746}; CATALYTIC ACTIVITY: Reaction=(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH; Xref=Rhea:RHEA:20521, ChEBI:CHEBI:10983, ChEBI:CHEBI:13705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.30; Evidence={ECO:0000250|UniProtKB:Q9BUT1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=387 uM for 4-oxo-L-proline {ECO:0000269|PubMed:35150746}; KM=10232 uM for (R)-3-hydroxybutanoate {ECO:0000269|PubMed:35150746}; Vmax=28 umol/min/mg enzyme toward 4-oxo-L-proline {ECO:0000269|PubMed:35150746}; Vmax=0.04 umol/min/mg enzyme toward (R)-3-hydroxybutanoate {ECO:0000269|PubMed:35150746}; Note=kcat is 14 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.; | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:35150746}.; PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:Q8JZV9}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active from 5.5 to 9.0 with 4-oxo-L-proline. {ECO:0000269|PubMed:35150746}; | null | FUNCTION: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (PubMed:35150746). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (By similarity). {ECO:0000250|UniProtKB:Q8JZV9, ECO:0000250|UniProtKB:Q9BUT1, ECO:0000269|PubMed:35150746}. | Rattus norvegicus (Rat) |
D4A1R8 | CPNE1_RAT | MAHCVTLVQLSVSCDHLIDKDIGSKSDPLCVLLQDVGGAWAELCRTERVRNCSSPAFSKTLQIEYYFETVQKLRFGIYDIDNKTPELGDDDFLGGAECSLGQIVSSQTLTLPLMLKPGKPAGRGTITVSAQELKDSRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLAYRTEVVKNNLNPTWKRFSVSLQHFCGGDLNTPIQVRCSDYDSDGSHDLIGTFHTTLAQLQAVPAEFECIHPEKQQRKKSYKNSGTVCVKTCRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLTALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAQQRTASQYFVLLLLTDGAVTDVEATCKAVVEASKLPMSVIIVGVGGADFEVMEQLDADGGPLRTRSGEAAARDIVQFVPYRRFQNAPRETLAMTVLAEVPTQMVSYFKAQGWAPLKTLPAPAKGPAQAPQV | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | cellular response to calcium ion [GO:0071277]; negative regulation of gene expression [GO:0010629]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; neuron projection extension [GO:1990138]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; proteolysis [GO:0006508]; regulation of canonical NF-kappaB signal transduction [GO:0043122] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; NF-kappaB binding [GO:0051059]; phosphatidylserine binding [GO:0001786] | PF00168;PF07002; | 2.60.40.150;3.40.50.410; | Copine family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99829}. Cytoplasm {ECO:0000250|UniProtKB:Q99829}. Cell membrane {ECO:0000250|UniProtKB:Q99829}. Note=Translocates to the cell membrane in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q99829}. | null | null | null | null | null | FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner. Exhibits calcium-dependent phospholipid binding properties. Plays a role in neuronal progenitor cell differentiation; induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner. May recruit target proteins to the cell membrane in a calcium-dependent manner. May function in membrane trafficking. Involved in TNF-alpha-induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit. Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL. {ECO:0000250|UniProtKB:Q99829}. | Rattus norvegicus (Rat) |
D4A1W8 | MTP_RAT | MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKLQDSVGYRISSDVDVVLLWRNPDGDDDQLIQVTITAVNVENAGQQRGEKSIFKGKSTPKIVGKDNLEALRRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLTSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVTSKATSVTTYKIEDSFVTAVVAEETRAFALNFLQTVAGKIVSKQKLELKTTEAGPRMVPGKQVAGVIKAIDSKYKAIPIVGQVLQSVCKGCPSLAEHWQSIRKHLEPENLSNAEAVQSFLAFIQHLRTSRREEILQILKAEKKEVLPQLVDAVTSAQTPASLEAILDFLDFKSDSSIILQERFLYACGFASHPDEELLQALLSKFKGSFASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEAKKLILGGLEKPEKKEDTTMYLLALKNALLPEGIPLLLKYAEAGEGPVSHLATTVLQRYDASFITDEVKKTLNRIYHQNRKVHEKTVRTTAAAVILKNNPSYMDVKNILLSIGELPKEMNKYMLTIVQDILHFEMPASKMIRRVLKEMIVHNYDRFSKSGSSSAYTGYVERSPHAASTYSLDILYSGSGILRRSNLNIFQYIGKAELHGSQVVIEAQGLEGLIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPVSVVKGLILLIDHSQDIQLQSGLKANMDIQGGLAIDISGSMEFSLWYRESKTRVKNRVAVVITSDITVDSSFVKAGLESRAETEAGLEFISTVQFSQYPFLVCMQMDKAEAPLRQFETKYERLSTGRGYVSRRRKESLVPGCELPLHQENSEMCNVVFPPQPESGNSGGGWF | null | null | cholesterol homeostasis [GO:0042632]; circadian rhythm [GO:0007623]; establishment of localization in cell [GO:0051649]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; low-density lipoprotein particle remodeling [GO:0034374]; phospholipid transport [GO:0015914]; plasma lipoprotein particle assembly [GO:0034377]; protein secretion [GO:0009306]; response to calcium ion [GO:0051592]; triglyceride metabolic process [GO:0006641]; triglyceride transport [GO:0034197] | basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; microvillus membrane [GO:0031528]; receptor complex [GO:0043235]; vesicle [GO:0031982] | apolipoprotein binding [GO:0034185]; ceramide 1-phosphate transfer activity [GO:1902388]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine transfer activity [GO:0120019]; phosphatidylethanolamine transfer activity [GO:1904121]; phospholipid transfer activity [GO:0120014]; phospholipid transporter activity [GO:0005548]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; triglyceride transfer activity [GO:0140344] | PF19444;PF01347; | 1.25.10.20; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P55157}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P55157}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:16478722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000305|PubMed:16478722}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:15897609}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896; Evidence={ECO:0000305|PubMed:15897609}; CATALYTIC ACTIVITY: Reaction=a cholesterol ester(in) = a cholesterol ester(out); Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002; Evidence={ECO:0000269|PubMed:15897609}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008; Evidence={ECO:0000305|PubMed:15897609}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012; Evidence={ECO:0000305|PubMed:15897609}; | null | null | null | null | FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:15897609, PubMed:16478722). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (By similarity). May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins (By similarity). {ECO:0000250|UniProtKB:O08601, ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722}. | Rattus norvegicus (Rat) |
D4A1X2 | EXOSX_RAT | MAPPSPREHQSAPATGATKPDAEMVLPGFPDADSFVKFALGSVVAVTKASGGLPQVGDEYDFYRSFPAFQAFCETQGDRLLQCMSRVMQYHGCRSNIKDRSKVTELEDKFDLLVDTNDVILERVGILLDEASGVNKHQQPVLPAGLQVPKTIVSSWNRKAGEYGKKAKAETFRLLHAKNILRPQLRFREKIDNSNTPFLPKIFVKPNARKPLPQALSKERRERPQDRPEDLDVPPALADFIHQQRAQQVEQDVFAHPYQYELDHFTPPPSVLQRPQPQLYRPVEETPCHVVSSLDELVELNEKLLGCQEFAVDLEHHSYRSFLGLTCLMQISTRTEDFIVDTLELRSDMYILNESLTDPAIVKVFHGADSDIEWLQKDFGLYVVNMFDTHQAARLLNLARHSLDHLLRLYCGVESNKQYQLADWRIRPLPEEMLNYARDDTHYLLYIYDRMRLELWERGNDQPVQLQVVWQRSRDICLKKFVKPIFTDESYLELYRKQKKHLNSQQLTAFQLLFAWRDKTARREDESYGYVLPNHMMLKIAEELPKEPQGIIACCNPVPPLVRQQINEMHLLIQQAREMPLLKSETAAGVKKSGPLPSAERLENDLFGPHDCSHAPPDNYPVTSTDGTMPLQKQPSLFDEGKEETSVDARCLLATAVITLFSEPSTEEAGKTPLTVAQKKAQSIMESFENPFRMFLPSLENKAHISQAAKFDPSSKIYEISNRWKLASQVQKEPKEAAKKKVAEQTAAREETKEESTAAVLEQPIPVRQQAALENATKKRERATSDLRTIEQKQEKKRLKSSKKAKDPDPPGKDFSPYDYSQSDFGAFAGDSKSKPSSQFDPNKVAPSGKKCFGAKKFKQSVGNKSMSFPAGKSDRGFRHNWPKR | 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q01780}; | CUT catabolic process [GO:0071034]; DNA repair [GO:0006281]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; histone mRNA catabolic process [GO:0071044]; maturation of 5.8S rRNA [GO:0000460]; negative regulation of telomere maintenance via telomerase [GO:0032211]; nuclear mRNA surveillance [GO:0071028]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; nuclear polyadenylation-dependent CUT catabolic process [GO:0071039]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent snoRNA catabolic process [GO:0071036]; nuclear polyadenylation-dependent snRNA catabolic process [GO:0071037]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; positive regulation of mRNA cis splicing, via spliceosome [GO:1905746]; regulation of telomerase RNA localization to Cajal body [GO:1904872]; ribosomal small subunit biogenesis [GO:0042274]; RNA catabolic process [GO:0006401]; RNA processing [GO:0006396] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; euchromatin [GO:0000791]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small-subunit processome [GO:0032040] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA exonuclease activity [GO:0004532]; single-stranded RNA binding [GO:0003727] | PF01612;PF00570;PF08066; | 1.10.150.80;3.30.420.10; | Exosome component 10/RRP6 family | PTM: Sumoylated by USP36; sumoylation does not significantly affect EXOSC10 nucleolar localization and association with core exosome and USP36, but regulates the nucleolar RNA exosome activity in rRNA processing by promoting binding of EXOSC10 to pre-rRNAs. Effects of sumoylation on EXOSC10 levels vary between different studies. Sumoylation of EXOSC10 is required for the modulation of EXOSC10 effects on cellular protein translation and cell proliferation. Sumoylation is promoted by mild hypothermia. {ECO:0000250|UniProtKB:Q01780}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01780}. Nucleus {ECO:0000250|UniProtKB:Q01780}. Nucleus, nucleolus {ECO:0000269|PubMed:29118343}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q01780}. Note=Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence of a nucleolar RNA exosome complex form. {ECO:0000250|UniProtKB:Q01780}. | null | null | null | null | null | FUNCTION: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA (By similarity). Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination (By similarity). Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage (By similarity). Plays a role in oocyte development, maturation and survival (By similarity). Required for normal testis development and mitotic division of spermatogonia (By similarity). Plays a role in proper embryo development (By similarity). Required for global protein translation (By similarity). Required for cell proliferation (By similarity). {ECO:0000250|UniProtKB:P56960, ECO:0000250|UniProtKB:Q01780}. | Rattus norvegicus (Rat) |
D4A208 | SRGP2_RAT | MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDIIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRRQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLRHEGVFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLIACVTMDNLQERAVHIRKVLLVLPKPTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPNPRELEGPIYSRGGSMEDYCDSTHGETISAEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVMSEPPEEKVTARTGASCPSGGHVADIYLANINKQRKRPESGSIRKAFRSDSHGLGSSLTDSSSPGVGASCRPSSQPIMSQNLPKEGPDKCSISGHGSLNSISRHSSLKNRMDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELQELERQSSAKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSASPQSTDKSCTV | null | null | actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; excitatory synapse assembly [GO:1904861]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; filopodium assembly [GO:0046847]; inhibitory synapse assembly [GO:1904862]; lamellipodium assembly involved in ameboidal cell migration [GO:0003363]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron migration [GO:2001223]; neuron projection morphogenesis [GO:0048812]; positive regulation of GTPase activity [GO:0043547]; regulation of cell migration [GO:0030334]; signal transduction [GO:0007165]; substrate adhesion-dependent cell spreading [GO:0034446] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211] | GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267] | PF00611;PF00620;PF00018; | 1.20.1270.60;1.10.555.10;2.30.30.40; | null | PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000250|UniProtKB:O75044}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75044}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:O75044}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75044}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q91Z67}. Nucleus {ECO:0000269|PubMed:17710530, ECO:0000269|PubMed:27748913}. Cytoplasm, cytosol {ECO:0000269|PubMed:17710530, ECO:0000269|PubMed:27748913}. Note=Recruited to actin-rich phagosomes during phagocytosis (By similarity). Translocates from nucleus to cytoplasm during development (PubMed:17710530). {ECO:0000250|UniProtKB:Q91Z67, ECO:0000269|PubMed:17710530}. | null | null | null | null | null | FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses. Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation. Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions. In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. {ECO:0000250|UniProtKB:Q91Z67}. | Rattus norvegicus (Rat) |
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