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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F1M0Z1 | TRIO_RAT | MSGSSGGATAPAASSGPAAAASAAGSGCGGGAGEGAEEAAKDLADIAAFFRSGFRKNDEMKAMDVLPILKEKVAYLSGGRDKRGGPILTFPARSNHDRMRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDSIKPLLKILQESFPCCIHIALIIKPDNFWQKQRTNFGSSKFEFETNMVSLEGLTKVVDPSQLTPEFDGCLEYNHEEWIEIRVAFEDYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKVIKAPIEDLDLEGQKLLQRIQSSESFPKKNSGSGNADLQNLLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWITHNKGLFLNSYTEIGASHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIKQIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQDGKSLLDKLQRPLTPGSSDSLTASANYSKAVHHVLDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLDMSVSFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREEDWCGGADKLGPNSETDHVTPMISKHLEQKEAFLKACTLARRNADVFLKYLHRNSVSMPGMVTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQCQQYVVFERSAKQALEWIHDNGEFYLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVTAVDKRYRDFSLRMEKYRTSLEKALGISSDSNKSSKSLQLDIIPASIPGSEVKLRDAAHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNKELIIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLILEHAGSYFDEIQQRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVMLSVPKRANDAMHLSMLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGDPCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTVHLRGALKEPIHIPKTAPAARQKGRRDGEDLDSQGDGSSQPDTISIASRTSQNTLDSDKLSGGCELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTTDRSPAAEGLVPCGSLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQPHMMGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHAKKLAHKHKKSREVRKSADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPPPMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLSSSSPIDEMEERKCSLSLKRRHYVLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDMKGKDKIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVKHERRLHMYIVYCQNKPKSEHIVSEYIDTFFEDLKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASLDTSELEKAVEVMCIVPKRCNDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEENVESDPCKFALTSRTGDAVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEYQRNHSGGGGSGSGGSSGGGGGSGGSGASSGGSSSHGSGPSSCSSGPSSSRSRPSRIPQPVRHHPPMLVSSAASSQAEADKMSGMSAPSPSLPTPSNSLALEASLGQPSRLPLSGDSEGHERETEPIPKMKVMESPRKALGSTSGTSQDGNTKDARGNLGPLPLGKTRPGAVSPLNSPLSTTFPSPFGKEAFPPSSPLQKGGSFWSSIPASPASRPSSFTFPGDSDSLQRQTHRHAAPSKDTDRMSTCSSASEQSVQSTQSNGSESSSSSNISTMLVTHEYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGHTSAVIMENPDGTFKKSTSWHTALRLRKKSEKKDKDGKRDGKLENGYRKPREGLSNKLLNPNYIYDVPPEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYNISYSDVGEATLKIIGVSTEDDGVYTCIAVNDMGSASSSASLRVLGPGSDGIVVTWKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLFVSLLDTFETPTSYVLVLELADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLTDFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGSGKGMGVLDTSRLTSFIERRKHQNDVRPIRSIKNFLQSRLLPRV | 2.7.11.1 | null | axon guidance [GO:0007411]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of fat cell differentiation [GO:0045599]; neuron projection morphogenesis [GO:0048812]; phosphorylation [GO:0016310]; postsynaptic modulation of chemical synaptic transmission [GO:0099170] | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extrinsic component of membrane [GO:0019898]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]; presynaptic active zone [GO:0048786]; Schaffer collateral - CA1 synapse [GO:0098685] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13716;PF07679;PF00169;PF00069;PF00621;PF16609;PF00018;PF00435; | 1.20.58.60;3.40.525.10;1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Phosphorylated on serine residue(s). {ECO:0000250|UniProtKB:O75962}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0KL02}. Cell projection {ECO:0000250|UniProtKB:Q0KL02}. | 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: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth (By similarity). Plays a key role in the regulation of neurite outgrowth and lamellipodia formation (By similarity). In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (PubMed:26721934). May act as a regulator of adipogenesis (By similarity). {ECO:0000250|UniProtKB:O75962, ECO:0000250|UniProtKB:Q0KL02, ECO:0000269|PubMed:26721934}. | Rattus norvegicus (Rat) |
F1M386 | RPGF2_RAT | MKPLAAPANHGVLGQQEKQSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRSMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSSSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPAALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPEQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLSGQNLQPPVIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSANATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATSTLPKNPADRKPVKSETSPVAPRAGPQQKAQPQQPLAPPQPSHKVSQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRKQAEDTISNASSQLSSPPTSPQSSPRKGYALALSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVESNLGVGRMERRTLMEPDQYSLGSYAPVSESRGLYAAATVISSPSTEELSHDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDATGIWASGGHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSTEAESSSMVPVTTEEAKPVPMPAHIAVTPSTTKGLIARKEGRYREPPPTPPGYVGIPIADFPEGPCHPARKPPDYNVALQRSRMVARPTEAPAPGQTPPAATASRPGSKPQWHKPSDADPRLAPFQPQGFAGAEEDEDEQVSAV | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; blood vessel development [GO:0001568]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; cAMP-mediated signaling [GO:0019933]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of endothelial barrier [GO:0061028]; establishment of endothelial intestinal barrier [GO:0090557]; forebrain neuron development [GO:0021884]; G protein-coupled receptor signaling pathway [GO:0007186]; microvillus assembly [GO:0030033]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of melanin biosynthetic process [GO:0048022]; nerve growth factor signaling pathway [GO:0038180]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein binding [GO:0032092]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of vasculogenesis [GO:2001214]; protein localization to plasma membrane [GO:0072659]; Rap protein signal transduction [GO:0032486]; Ras protein signal transduction [GO:0007265]; regulation of cell junction assembly [GO:1901888]; regulation of synaptic plasticity [GO:0048167]; ventricular system development [GO:0021591] | apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; late endosome [GO:0005770]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | beta-1 adrenergic receptor binding [GO:0031697]; cAMP binding [GO:0030552]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; PDZ domain binding [GO:0030165]; phosphatidic acid binding [GO:0070300]; protein kinase binding [GO:0019901]; WW domain binding [GO:0050699] | PF00595;PF00788;PF00617;PF00618; | 2.30.42.10;2.60.120.10;1.10.840.10;1.20.870.10; | RAPGEF2 family | PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000269|PubMed:21382555}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:17724123}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:17724123}. | Rattus norvegicus (Rat) |
F1M391 | STING_RAT | MPYSNLHPSIPRPRSYRFKLAAFVLLVGSLMSLWMTGEPPSHTLHYLALHVASQQLGLLLKKLCCLAEELCHVQSRYQGSYWKAVRACVGSPICFMALILLSFYFYCSLENTSDLRLAWHLGILVLSKSLSMTLDLQSLAPAEVSAVCEEKNFNVAHGLAWSYYIGYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLEEILADVPESRNHCRLIVYQESEEGNSFSLSQEVLRHIRQEEKEEVTMSGPPTSVAPRPSLLSQEPRLLISGMEQPLPLRTDLI | null | null | activation of innate immune response [GO:0002218]; antiviral innate immune response [GO:0140374]; autophagosome assembly [GO:0000045]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to interferon-beta [GO:0035458]; cellular response to organic cyclic compound [GO:0071407]; cGAS/STING signaling pathway [GO:0140896]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; protein complex oligomerization [GO:0051259]; regulation of gene expression [GO:0010468]; regulation of inflammatory response [GO:0050727]; reticulophagy [GO:0061709] | autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; STING complex [GO:1990231] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; proton channel activity [GO:0015252]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; signaling adaptor activity [GO:0035591]; ubiquitin protein ligase binding [GO:0031625] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta. Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif. The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (By similarity). Phosphorylated on tyrosine residues upon MHC-II aggregation (By similarity). Dephosphorylation by PPP6C leads to inactivation and decreased production of IFN-beta (By similarity). Phosphorylation at Ser-358 is also required to activate IRF3 (By similarity). Phosphorylation at Ser-355 by MAP3K7/TAK1 facilitates its interaction with STEEP1, promoting STING1 translocation to COPII vesicles (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.; PTM: Ubiquitinated (By similarity). Ubiquitinated via 'Lys-63'-linked ubiquitin chains in response to double-stranded DNA treatment, leading to relocalization to autophagosomes and subsequent degradation; this process is dependent on SQSTM1 (By similarity). 'Lys-63'-linked ubiquitination mediated by TRIM56 at Lys-151 promotes homodimerization and recruitment of the antiviral kinase TBK1 and subsequent production of IFN-beta. 'Lys-48'-linked polyubiquitination at Lys-151 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation. 'Lys-11'-linked polyubiquitination at Lys-151 by RNF26 leads to stabilize STING1: it protects STING1 from RNF5-mediated 'Lys-48'-linked polyubiquitination (By similarity). 'Lys-33'-linked and 'Lys-48'-linked deubiquitinated by USP20; leading to its stabilization and promotion of innate antiviral response (By similarity). 'Lys-48'-linked deubiquitinated by USP44; leading to its stabilization and promotion of innate antiviral response (By similarity). Deubiquitinated by USP13; leading to inhibition of innate antiviral response (By similarity). 'Lys-63'-linked deubiquitinated by USP49; leading to inhibition of the subsequent recruitment of TBK1 to the signaling complex (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.; PTM: Sumoylated at Lys-338 by TRIM38 during the early phase of viral infection, promoting its stability by preventing its relocalization to autophagosomes and subsequent degradation. Desumoylated by SENP2 during the late phase of viral infection. {ECO:0000250|UniProtKB:Q3TBT3}.; PTM: Palmitoylation takes place in the Golgi apparatus and creates a platform for the recruitment of TBK1. {ECO:0000250|UniProtKB:Q3TBT3}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. Localizes in the lysosome membrane in a TMEM203-dependent manner. {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:26669264). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:26669264). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26669264). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:26669264}. | Rattus norvegicus (Rat) |
F1M3G7 | AKP13_RAT | MKLSPQQAPLYGDCVVTVLLAEEDKVEDDAIFYLIFSGSTLYHCTSTRKVSSDTLETIAPGHDCCETVKVLLCASKEGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLDRSGPPSGDVNSLDEKVALAFRHLKLPAEWNVLGTDHTLHDGGPRETLMHFAVRLGLLRLTWFLLQKPGGRGALSIHNKEGATPVSLALERGYHKLHQLLTEENAGEPDSWSSLSYEIPYGDYSVRHHRELDIYTLTSESESHCEPHGDSCTGHISKLMNIQQQLMKTNLKQMDNLMPLMVTTQDSSCVPCVPEPSDHQQLPFEETKSTVCCQGSPGRKDASPCDLSSVVEEENLICSHKKNKDTGRPGEGVEPASAVDSRSASHQDSCLQSIPDCGVKGREGLPSCGNRNEVTGTQYSGVATCQQPLSSESSVPQDVLVTEPDARQHSSGRELPDSSSTDAGAPEKAGELEHSLLTPDATTQNSKPQVGESAKERLENSDISSAEATAVQALREPKQKADVTNHVFAARAAGADAPAEASPAWSPEEIPTGKPGMETQERGCEGGITSDQSSQVLPAAAAATENKVLDGLELETLPACPCETASSLDLTVSGPRPDGMPKQNSESSAQHAQSLNSQAPLCSIAGAGTPSAESACPQSTETSSGGSVIEHGSGEASLPESTAAQPEPQGLCTAPCPEDPQADTVTSDTAAHNQKSVGSCHLCALDAKNQEKDLRQDTPSVNTLEDVPHLPSVVPQSEEKLEPDQVSPRGSSFSLASSPESESVTKDDVLSLVSSQKEKGTATPQLHRAPACSDGPDGRDLNDTDKVGDGAASPPTPSAVELQTSMGNTSPVGVGEQEGSSLTATLEVLSDSLLQSVDKAALVSDSLLPEEGGSIVVPESSTALGQGGKDKATKCPSVKEDVHSSEMSREDQRTPPPGQEISRLCEKPMSALCAGEKALQHSNSPDTPSACLQTETKHNKEVAPQSSPLMKGGAVQNLVPPKTSLSADSEQKTSSTEQSGSSLLPGGASEALRCSQPSLSVSVESIQFQGKTSACKVSRNAMEDVTVADAFLATAEPTKEDALHHVKDISDLLNQEKKTTPGLPEALLDKGVTDLQEVITPEIEPLDCKREKLEGTDLSCPTSKSKETPNNEETTQPPARDLPTETGLSAINDNGPQADMKHVTQASVPGEESNVTTVLGMVSTQAADGPPGADSIEETATRIVEAVIKQIKASNTLRTQVEIQNPPLSSSEIKEIENTGSESARVFLPGEPLQMENTQKETTGHCSVETEAPEKIILAVHRPEPAPEMPDTKTGGEVDLLSKRSAASEEEAIGNGAATPKMKQAPGTQVINRESWCAIEPCPEAASLLASKQSSECRSFIDVGLGTECATKEGVLQRESGSDSDLFHSPSDEMDSIIFSKPEEEQLLCDTTGSSSSTDDTASLDRHSSHGSDVSLPQTSKLNRSRNHQSSNGFFSHGVDPESREGESEPAGSGEMEEEEMDSITEVPANRSFLRNSMRSLSPFRRHSWGPGKNAASDAEMNQRSSMQVLGHVVRRPPIHRRSMSWCPSGVQYSAALNADFNIRSFSLEGLTGGGGVGNKPSSSLEISSANSSELRNPFSGEEQRSSLMSLSEEHLEPDQRQHHRMFDQQTCYRSKQQGFNYCTSAISSPLTKSISLMTISHPGLDNSRPFHSASANLTESITEENCNFLPPSPSKKSFEEKSGTKVSRTFSYIRNKMSSSKKSKKEKDKKTLNGHTFSPIPIVGPINCSQCMKPFTNKDAYTCASCGAFVHKGCRENLASCAKVKMKQPKGSLQAHDTSSLPTVIMRNKSSQPKERPRSAVLLAEEAIAAPMFTNRRSQQSVSLSKSVSIQNITGVGNDENMSNTWKFLSHSTDSLNKICKVNESTESLTDEGVGTDMNEGQLMGDFESDSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVSQFSGENAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYEKKVRLGEIYTKTDSKSIMRMKSGQMFAKEDLRRKKLVRDGSVFLKSATGRLKEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSLNRDEDEGIPSENEEEKRLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLPEDCSPTHSPRMLFRSNTEEALKGGPLMKSAISEVEILQGLVSGSLGGTLGQPISSPVEQEVMAGPISLPRRAETFGGFDCHQLNASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSIVHLHELLTMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEARELELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLKRDAEQLSQRQMEQDLCQVSNKHGRLMRVPSFLPNSDEFSLLSTPSITKSGSLDSELSVSPKRNSISRTQKDKGPFHILSSASQTKVPEGQSQAPSSTSTSTRLFGLSKPKEKKEKKKKSKGSRTQPGDGPAPEVPAEGEEIFC | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process [GO:0086023]; adrenergic receptor signaling pathway [GO:0071875]; bone development [GO:0060348]; cardiac muscle cell differentiation [GO:0055007]; cell growth involved in cardiac muscle cell development [GO:0061049]; G protein-coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; nuclear export [GO:0051168]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of glucocorticoid mediated signaling pathway [GO:1900169]; regulation of Rho protein signal transduction [GO:0035023]; regulation of sarcomere organization [GO:0060297] | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | guanyl-nucleotide exchange factor activity [GO:0005085]; MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; protein kinase A binding [GO:0051018]; small GTPase binding [GO:0031267] | PF17838;PF00621; | 3.30.60.20;1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12802}. Cytoplasm {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q12802}. Nucleus {ECO:0000250|UniProtKB:Q12802}. Membrane {ECO:0000250|UniProtKB:Q12802}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12802}. Note=Colocalizes with the actin cytoskeleton at the cell cortex. {ECO:0000250|UniProtKB:Q12802}. | null | null | null | null | null | FUNCTION: Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:17537920). May also activate other Rho family members. Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (By similarity). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (PubMed:20139090). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (By similarity). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (By similarity). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920). Required for normal adaptive cardiac hypertrophy in response to pressure overload (By similarity). Plays a role in osteogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q394, ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:23090968}. | Rattus norvegicus (Rat) |
F1M3J4 | MRP4_RAT | MLPVHTEVKPNPLQDANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKEVLRAKKDARKPSLTKAIVKCYWKSYLILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFFPSAIERVSEAVVSVRRIKNFLLLDELPERKAQEPSDGKAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDFQLLEDGDRLVIGDRGARLSGGQKARVNLATAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSPVPGTPTLRNRTFSEASIWSQQSSRPSLKDGVPDAQDAENTQAAQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNLMGQVFYVLQDWWLSHWANRQGALNDTKNANGNVTGTLDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECRKRPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHSDEELWKALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQQLGKGEAAALTETAKQVYFRRNYPDIAFSSPAVMSTSNGQPSALTIFETAL | 7.6.2.-; 7.6.2.2; 7.6.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O15439}; | bile acid and bile salt transport [GO:0015721]; bile acid signaling pathway [GO:0038183]; cAMP transport [GO:0070730]; cilium assembly [GO:0060271]; export across plasma membrane [GO:0140115]; leukotriene transport [GO:0071716]; positive regulation of smooth muscle cell proliferation [GO:0048661]; prostaglandin secretion [GO:0032310]; prostaglandin transport [GO:0015732]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to organonitrogen compound [GO:0010243]; response to xenobiotic stimulus [GO:0009410]; transmembrane transport [GO:0055085]; urate transport [GO:0015747] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; external side of apical plasma membrane [GO:0098591]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088] | ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; efflux transmembrane transporter activity [GO:0015562]; glutathione transmembrane transporter activity [GO:0034634]; guanine nucleotide transmembrane transporter activity [GO:0001409]; prostaglandin transmembrane transporter activity [GO:0015132]; purine nucleotide transmembrane transporter activity [GO:0015216]; urate transmembrane transporter activity [GO:0015143]; xenobiotic transmembrane transporter activity [GO:0042910] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | null | PTM: N-glycosylated; leading to substrate-selective effects on its transport activity. {ECO:0000250|UniProtKB:O15439}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12883481}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O15439}; Multi-pass membrane protein {ECO:0000255}. Note=Its localization to the basolateral or apical membranes is tissue-dependent. {ECO:0000250|UniProtKB:O15439}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene B4(in) = ADP + H(+) + leukotriene B4(out) + phosphate; Xref=Rhea:RHEA:66424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57461, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out); Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57746, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58165, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + prostaglandin E2(in) = ADP + H(+) + phosphate + prostaglandin E2(out); Xref=Rhea:RHEA:66388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66389; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + prostaglandin E1(in) = ADP + H(+) + phosphate + prostaglandin E1(out); Xref=Rhea:RHEA:66392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57397, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66393; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycodeoxycholate(in) + H2O = ADP + glutathione(out) + glycodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:82982, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66381; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + glutathione(in) + H2O = ADP + cholate(out) + glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:66396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66397; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycocholate(in) + H2O = ADP + glutathione(out) + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66401; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + taurocholate(in) = ADP + glutathione(out) + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:66404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66405; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycochenodeoxycholate(in) + H2O = ADP + glutathione(out) + glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66409; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + taurochenodeoxycholate(in) = ADP + glutathione(out) + H(+) + phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:66412, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66413; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycoursodeoxycholate(in) + H2O = ADP + glutathione(out) + glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66417; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + tauroursodeoxycholate(in) = ADP + glutathione(out) + H(+) + phosphate + tauroursodeoxycholate(out); Xref=Rhea:RHEA:66420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66421; Evidence={ECO:0000250|UniProtKB:O15439}; | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules. {ECO:0000250|UniProtKB:O15439}. | Rattus norvegicus (Rat) |
F1M3L7 | EPS8_RAT | MNGHMSNHSSGYGIYPSQMNGYGSSPPYSQMDREHCSRTSAKALYEQRKNYARDSVSSVSDVSQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVAHTCSYDSILALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPEALRMIAKADPGIPPPPRAPAPVPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKSKKSKRKGPGEGVLTLRAKPPPPDEFVDCFQKFKHGFNLLAKLKSHIQNPSASDLVHFLFTPLNMVVQATGGPELASSVLSPLLTKDTVDFLNYTVKAEERQLWMSLGETWMKVRAEWPKEQFIPPYVPRFRNGWEPPMLNFMGAPTEQDMYQLAESVANAAEQQRKQDSKRQSTEHSSMSDYPPADGYTFSNSMYHRGPHVDQGEAALALKSTPNRHVDRNYDPVKTQPKKYAKSKYDFVARNSSELSVMKDDVLEILDDRKQWWKVRNASGDSGFVPNNILDIMRTPESGVGRTDPPYTHTIQKQRTEYGPRSADTPSAPSPPPTPAPVPVPLPPSAPAPVPVPKVPANVTRQNSSSSESGGSIARDSQRYKQLPVDRRKSQMEEVQDELFQRLTIGRSAAQRKFHVPRQNVPVINITYDSSPEEVKTWLQSKGFNPVTVSSLGVLNGAQLFSLNKDELRSVCPEGARVFSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH | null | null | actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin polymerization-dependent cell motility [GO:0070358]; adult locomotory behavior [GO:0008344]; barbed-end actin filament capping [GO:0051016]; behavioral response to ethanol [GO:0048149]; cellular response to leukemia inhibitory factor [GO:1990830]; dendritic cell migration [GO:0036336]; exit from mitosis [GO:0010458]; positive regulation of ruffle assembly [GO:1900029]; Rac protein signal transduction [GO:0016601]; regulation of actin filament length [GO:0030832]; regulation of cell shape [GO:0008360]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; regulation of Rho protein signal transduction [GO:0035023]; Rho protein signal transduction [GO:0007266] | brush border [GO:0005903]; cell cortex [GO:0005938]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587]; stereocilium [GO:0032420]; stereocilium bundle [GO:0032421]; stereocilium tip [GO:0032426]; synapse [GO:0045202]; vesicle [GO:0031982] | actin binding [GO:0003779]; small GTPase binding [GO:0031267] | PF08416;PF18016;PF00018; | 2.30.29.30;2.30.30.40;1.10.150.50; | EPS8 family | PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation. Phosphorylated by several receptor tyrosine kinases (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Synapse, synaptosome. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cell projection, stereocilium {ECO:0000250, ECO:0000250|UniProtKB:Q08509}. Cell projection, growth cone. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells (By similarity). Localizes to the midzone of dividing cells. {ECO:0000250, ECO:0000250|UniProtKB:Q08509}. | null | null | null | null | null | FUNCTION: Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
F1M4A4 | KIF1A_RAT | MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHTSPEDINYASQKQVYRDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDTNTVPGGPKLTNALVGMSPSSSLSALSSRAASVSSLHERILFAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERERTPCAETPAEPVDWAFAQRELLEKQGIDMKQEMEQRLQELEDQYRREREEATYLLEQQRLDYESKLEALQKQMDSRYYPEVNEEEEEPEDEVQWTERECELALWAFRKWKWYQFTSLRDLLWGNAIFLKEANAISVELKKKVQFQFVLLTDTLYSPLPPDLLPPEAAKDRETRPFPRTIVAVEVQDQKNGATHYWTLEKLRQRLDLMREMYDRAAEVPSSVVEDCDNVVTGGDPFYDRFPWFRLVGRAFVYLSNLLYPVPLVHRVAIVSEKGEVKGFLRVAVQAISADEEAPDYGSGVRQSGTAKISFDDQHFEKFQSESCPVVGMSRSGTSQEELRIVEGQGQGADAGPSADEVNNNTCSAVPPEGLLDSPEKAALDGPLDTALDHLRLGSTFTFRVTVLQASSISAEYADIFCQFNFIHRHDEAFSTEPLKNTGRGPPLGFYHVQNIAVEVTKSFIEYIKSQPIVFEVFGHYQQHPFPPLCKDVLSPLRPSRRHFPRVMPLSKPVPATKLSTMTRPSPGPCHCKYDLLVYFEICELEANGDYIPAVVDHRGGMPCMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVGRIRNTPETDEALIDPNILSLNILSSGYVHPAQDDRQFLDSDIPRTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEMENCTQPAVITKDFCMVFYSRDAKLPASRSIRNLFGSGSLRATEGNRVTGVYELSLCHVADAGSPGMQRRRRRVLDTSVAYVRGEENLAGWRPRSDSLILDHQWELEKLSLLQEVEKTRHYLLLREKLETTQRPVPEVLSPASSEDSESRSSSGASSPLSAEGQPSPLEVPNERQRELAVKCLRLLMHTFNREYTHSHVCISASESKLSEMSVTLMRDPSMSPLGAATLTPSSTCPSLIEGRYGATDVRTPQPCSRPASPEPELLPELDSKKTPSPVRATETEKEPQRLLVPDIQEIRVSPIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRGILLQANSDKDMHDWLYAFNPLLAGTIRSKLSRRRSAQMRV | null | null | anterograde axonal transport [GO:0008089]; anterograde neuronal dense core vesicle transport [GO:1990048]; cytoskeleton-dependent intracellular transport [GO:0030705]; dense core granule cytoskeletal transport [GO:0099519]; interkinetic nuclear migration [GO:0022027]; microtubule-based movement [GO:0007018]; protein transport along microtubule [GO:0098840]; regulation of dendritic spine development [GO:0060998]; regulation of dendritic spine morphogenesis [GO:0061001]; retrograde neuronal dense core vesicle transport [GO:1990049]; vesicle-mediated transport [GO:0016192] | axon [GO:0030424]; axon cytoplasm [GO:1904115]; dendrite [GO:0030425]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; neuronal dense core vesicle membrane [GO:0099012]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]; synaptic vesicle [GO:0008021] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF12473;PF00498;PF12423;PF00225;PF16183;PF00169; | 2.60.200.20;6.10.250.2520;3.40.850.10;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12756}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q12756}. Cell projection, axon {ECO:0000250|UniProtKB:P33173}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P33173}. Synapse {ECO:0000250|UniProtKB:P33173}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165}; Peripheral membrane protein {ECO:0000305|PubMed:30021165}; Cytoplasmic side {ECO:0000305|PubMed:30021165}. Note=Within neuronal cells concentrated in the axon, with smaller amounts in the perinuclear and synaptic regions (By similarity). Expressed in distal regions of neurites. {ECO:0000250|UniProtKB:P33173, ECO:0000250|UniProtKB:Q12756}. | null | null | null | null | null | FUNCTION: Motor for anterograde axonal transport of synaptic vesicle precursors (Probable). Also required for neuronal dense core vesicles (DCVs) transport to the dendritic spines and axons (PubMed:29166604, PubMed:30021165). The interaction calcium-dependent with CALM1 increases vesicle motility and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites (PubMed:30021165). {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165, ECO:0000305}. | Rattus norvegicus (Rat) |
F1M5F3 | MCM9_RAT | MNSEQVTLVGQVFESYVSEYHKNDILLILKERDEDAHYPLVVNAMTLFETNMEIGDYFTVFPNEVLTVFDSALRRSALAVLQSLPEPEGLSMKQNLHARISGLPVCPELVREHIPKTKDVGHFLSVTGTVIRTSLVKVLEFERDYMCNKCKYVFTVKADFEQYYTFSRPSSCPSSDTCDSSKFTCLSDLSASPARCRDYQEIKIQEQVQRLSVGSIPRSMKVILEDDLVDSCKSGDDLTIYGVVMQRWKPFQRDMRCEVEIVLKANYVQVNNEQSSGMVMDEDARKEFEDFWEHYKSDPFAGRNEILASLCPQVFGMYLVKLAVAMVLAGGIQRTDAAGTRVRGESHLLLVGDPGTGKSQFLKYAAKITPRSVLTTGIGSTSAGLTVTAVKDSGEWNLEAGALVLADAGLCCIDEFNSLKEHDRTSIHEAMEQQTISVAKAGLVCKLNTRTTILAATNPKGQYDPQESVSVNIALGSPLLSRFDLILVLLDTRNEDWDRIISSFILENKGYPSKSENLWSMEKMKTYFCLIRNLHPTLSDVSNQVLLRYYQMQRQSDSRNAARTTIRLLESLIRLAEAHARLMFRSTVTLEDAITVVSVMESSMQGGALLGGVNALHTSFPESPRAQYRRQCELILEKLELQSLLQEELRRLERLQNESDQCQPHSPEVEAAPGSCRNDPRDRPGLRTPTQQEQSCSWSPAESSGGDSPTGPGLSRPTSCNHKAEDGGGRGDCLAWADPTASPEIAQESTIVSPGLKTMEEKEDLKISNNGAQGKGKHGLQKRSQLLKPGRLPASGATDTSLRSRGSESTRARQAAVVSEAGRDDDQESGPRRLPRLLKEGSQSVCTTRVRTLPPTVPFPLSISPPGPGKKTGTPKRKRQKSAQVEAPGPEGTETMSAPVVKLAKFTFKQKSKLTHSPEGQGPMPPSASKVAVDSSKIPRQRTRREAGVPAAGPGQSTSTSGDRCSEQLQGQTKALSRQPPESHRPREEKEQGPERRVIQSELELGSQAGHSHPACKKDRKEGASCSNKSKVHAGTMARLANFSFTSPPESKSESLPPERKESRDRSHNPPATTAPVLGQQRQSFQLQQPPERVNLSTLSLFTLSELDDEALDFDWDEEMRKKP | 3.6.4.12 | null | DNA damage response [GO:0006974]; DNA duplex unwinding [GO:0032508]; double-strand break repair via homologous recombination [GO:0000724]; female gamete generation [GO:0007292]; gamete generation [GO:0007276]; mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication [GO:0070716]; protein localization to chromatin [GO:0071168]; 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]; DNA helicase activity [GO:0003678]; enzyme binding [GO:0019899]; MutLbeta complex binding [GO:0032406]; MutSalpha complex binding [GO:0032407]; MutSbeta complex binding [GO:0032408]; protein-containing complex binding [GO:0044877]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116] | PF00493;PF17855;PF17207; | 2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NXL9}. Chromosome {ECO:0000250|UniProtKB:Q9NXL9}. Note=Colocalizes to nuclear foci with RPA1 following DNA damage. Localizes to double-stranded DNA breaks. Recruited to chromatin by MSH2. {ECO:0000250|UniProtKB:Q9NXL9}. | 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:Q9NXL9}; | 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 MRN complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand. In addition, recruits MLH1, a component of the MMR complex, to chromatin. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. Probably by regulating HR, plays a key role during gametogenesis. {ECO:0000250|UniProtKB:Q2KHI9, ECO:0000250|UniProtKB:Q9NXL9}. | Rattus norvegicus (Rat) |
F1M5M3 | TEX14_RAT | MSRAVHFPVPCPVLLGTLTDDSLEAQLHEYAKQGNYVKVKKILKKGVCVDAVNTLGQSALFVAALLGYVKLVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKVLTAGGDLRLHDEKGRNPQAWALAAGKDRSTQMVEFMQRCASHMKAVIQGFSYDLLKKIDSPQRLIGSPPWFGGLIQGSPNSSPNRQPKPGIISAQNIYSFGFGKFYLTSGMQLTYPGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNRSRVTVKELNLPTHPHCSRLRLADLLIAEQEHSSNLRHPSLLQLMAVCLSRDLEKIRLVYERITVGTLFSVLHERRSQFPVLHMEMIVHLLLQIADALIYLHSRGFIHRSLSSYAVHIVSAGEARLTNLEYMMESQDSGAHRDMTRVPLPAQLYNWAAPEVVLQKTATVKSDIYSFSMIIQEILTDNIPWNGLDGSLVKETIALGNYLEADVRLPEPYYDIVKSGIHAKQKNRTMNLQDIRYILKNDLKEFIGAQKTQTTESPRGQRYEPHPDINICLGLTSEYQKDPPDLDIKELKETGSQPHSPTDHSFLTEKTLAPQTLDSSLSAQEPDNPNVPSASRLAEEVRSPTPSEASLYSFEINEIYSGCLTLGTDKEEECPGTASSPEGDKANQVDELPSLEEELDKMERELHCFCEEDKSFSDVDTDLSFEDGDWQSDSLSSLSLPEPTREAKGKTSSWSKTDEYVSKCVLNLKISQVMMQQSAEWLRKLEQEVDELEWAQKELDNQCRSLWDASLRFANTKFLSAVGPPSLTYLPPVMQLSEPKQPENGGNWLTLARPPGNERDFQEGNFSKKSEKLSACDWNPFTQASEESRGYCSEPNNQPPTLCGPGKQNTGEQLPSTEEAKESLERNTNQNIRRMESVSSEVCDTKSRNNEDAGEARSKWRLAVKEMAEKAVSGQLLVPPWNLQSSFESKVENESTPLPRPPIRGPESTDWQYILEYQREKDELKGNMKFGKMENSDCDKNKHSSWTGLQRFTSIIYPFFRNHEQPEHNEASQASCDTXCGEKFYSTSSPIEDDFERIQSSFAQPQGYVEENFQIREIFGKNAEILTKPQFQAVQCAEDEQEETLEETPKELKEKNISLTDIQDLSSITYEQDGCFKETSCKTPKLKHAPTSASTPLSPESISSAASHYEDCLENTFHVKRGSTFCWNGQEAMRTLSTKFTTVRERAKSLESLLASSKTLPAKLTDPKRLCMFGGACSSNISTAFVTSTHSTKRKSLPGELAEATSQHHIDELPPPAQELLDEIEQLKQQQVSSMVSLENTAHDLNVTENDKKHLEEQETNSSKDSSFLSSREIQDLEDTERAHSSLDEDLERLLQLPEENMTLLDPTKGSTREKKTKDQDMVEQKRKKKEGIKPERRKSDSFLGTLEEDELKPCFWKRLGWSEPSRIIVLDQSDLSD | null | null | attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; cellular response to leukemia inhibitory factor [GO:1990830]; intercellular bridge organization [GO:0043063]; male meiotic nuclear division [GO:0007140]; mitotic sister chromatid separation [GO:0051306]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of cytokinesis [GO:0032466] | cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; kinetochore [GO:0000776]; midbody [GO:0030496] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901] | PF12796;PF07714; | 1.25.40.20;1.10.510.10; | Protein kinase superfamily | PTM: Phosphorylated on Thr residues by CDK1 during early phases of mitosis, promoting the interaction with PLK1 and recruitment to kinetochores. Phosphorylated on Ser-431 by PLK1 during late prometaphase promotes the rapid depletion from kinetochores and its subsequent degradation by the APC/C complex. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the intercellular bridges that connect male germ cell daughter cells after cell division. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
F1M5N7 | KI21B_RAT | MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDTVTSEEEQGIIPRAIAHLFRGIDERKRRAQEQGVTGPEFKVSAQFLELYNEEILDLFDSTRDPDARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCAQPDLVNETVTGLPDGTAPTGTEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARNPYSLGASPAGPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQTEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPTATVNGARPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIMQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGSSQNHLLLDALREKAEAHPELQALIYNVQHENGYASTDEEVSEFSEGSFSQSFTMKGSTSHDDFKFKGEPKLSAQMKAVSAECLGPPLDSSTKNITKSLASLVEIKEDGVGFSIRDPYYRDKVSRTVSLPTRGSTFPRQSRGATDTSPLTRRKSYDRGQPIRSTDIGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIITPIGGAKGARTAPLQCVSMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSSSYVKVWDIRDSAKCIRTLTSSGQVISGDACMATSTRAITSSQGEHQINQMALSPSGTMLYVASGNAVRIWELNRFQPIGKLTGHIGPVMCLTVTQTSNQHDLVVTGSKDHYVKMFQLGDCVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFVPGRPMLLSACRAGFIKVWNVDNFTPIGEIKGHDSPINAICTNSKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRATTLP | null | null | brain development [GO:0007420]; corpus callosum development [GO:0022038]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231] | cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF00400; | 3.40.850.10;2.130.10.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXL1}. Cytoplasmic vesicle {ECO:0000269|PubMed:25172774}. | null | null | null | null | null | FUNCTION: Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface. {ECO:0000250|UniProtKB:Q9QXL1}. | Rattus norvegicus (Rat) |
F1M625 | UBP46_RAT | MTVRNIASICNMGTNASALEKDIGPEQFPINEHYFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTCLADLFHSIATQKKKVGVIPPKKFISRLRKENDLFDNYMQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENSKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRE | 3.4.19.12 | null | adult feeding behavior [GO:0008343]; behavioral fear response [GO:0001662]; behavioral response to ethanol [GO:0048149]; proteolysis [GO:0006508]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; regulation of synaptic transmission, GABAergic [GO:0032228]; righting reflex [GO:0060013] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; synapse [GO:0045202] | cysteine-type deubiquitinase activity [GO:0004843]; deubiquitinase activity [GO:0101005]; metal ion binding [GO:0046872] | PF00443; | 3.90.70.10; | Peptidase C19 family, USP12/USP46 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62068}. Note=USP46/WDR48/WDR20 complex is predominantly cytoplasmic. {ECO:0000250|UniProtKB:P62068}. | 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:0000269|PubMed:22043315}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67 (By similarity). Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 (By similarity). {ECO:0000250|UniProtKB:P62068, ECO:0000250|UniProtKB:P62069}. | Rattus norvegicus (Rat) |
F1M649 | NLRC4_RAT | MNFIKENSQALIQRMGIVVIKQICDDLFALNVLNGEEVAIICSHRVEQDAARDIVHMILKKGSAACNLFLKSLENWNYPVYQDLTGHSLFHQNLEEDLDVLAQSLKDLYNSPVFKNFFPLGEDIDIIFNLQITFTEPVLWRKDHRHHRVEQMTLGSLLEALKSPCLIEGESGKGKSTLLQKIAMLWASGMCPALNQFKLVFFIRLSSARGGLFETLYDQLVNIPDSISKPTFRALLLKLHKKVLFLLDAYNEFHPQNCPEIEALVKENHRFKNMVIVTTTTECLRHIRHVGALTVEVGDMTEDSARVLIREVLINELAEGLLFQMQESRCLRNLMRTPLFVVITCAIQMGSEEFQAHTQTMLFQTFYDLLIQKNRRRHSGGTSGDFVRSLDYCGDLALEGVFSHKFDFELEDVCSMNEDVLVRTGLLCKYTAQRLRPTYKFFHKSFQEYTAGRRLSSLLKSREPEEVSKGNSYLKKMVSISDITSLYGNLLLYTCGSSTEATRAIMRHLAMVCEHGSLQGLSVTKRPLWRQESIQNLRNTTEQDVLKAINVNSFVECGINLFSESISKSELSQEFEAFFQGKSLYINSENIPDYLFDFFKYLPNCVSALDFVKLDFYGRATVSQDKTGENSSGVHTEGPSTYIPSRAVSLFFNWMQKFKTLEVTLRDISKLNKQDIKYLGKIFSSASNLKLYIKRCAAVAGRLSSVLRTCKNIHSLMVEASPLTTEDEQYITSVTDLQNLSIHDLHTQRLPGGLADSLGNLKNLLKLILDDIRLNEEDAKSLAEGLRNLKKMRLLHLTRLSDMGEGMDYIVKSLSEEPCDLQEMKLVDCCLTANSLKILAQNLHNLVKLSVLDMSENYLEKAGSEALQGLIGRLGVLEQLSALMLPWCWDAYISLPNLLKQLEGTPGLVKLGLKNWRLRDEEIRSFGEFLEMNPLRDLQQLDLAGHGVSSDGWLSFMDVFENLKQLVFFDFGTEEFLPDAALVRKLGQVLSKLTLLQEARLTGWELDDYDISVIKGTFKLVTA | null | null | activation of innate immune response [GO:0002218]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; detection of bacterium [GO:0016045]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of apoptotic process [GO:0043065]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of protein processing [GO:0010954]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; IPAF inflammasome complex [GO:0072557]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; caspase binding [GO:0089720]; endopeptidase activator activity [GO:0061133]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF00619;PF05729;PF17889; | 1.10.1900.50;1.10.533.10;3.40.50.300;3.80.10.10; | null | PTM: Phosphorylated at Ser-533 following infection of macrophages with S.typhimurium (Salmonella). Phosphorylation is essential for NLRC4 inflammasome function to promote caspase-1 activation and pyroptosis. PRKCD phosphorylates Ser-533 in vitro. {ECO:0000250|UniProtKB:Q3UP24}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3UP24}. | null | null | null | null | null | FUNCTION: Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. {ECO:0000250|UniProtKB:Q3UP24}. | Rattus norvegicus (Rat) |
F1M707 | NCF1_RAT | MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRKFTEIYEFHKMLKEMFPIEAGEIHTENRVIPHLPAPRWYDGQRAAESRQGTLTEYFNSLMGLPMKISRCPHLLNFFKVRPDDLKLPNDSQVKKPETYLTAKDGKNNVADITGPIILQTYRAIADYEKGSKTEMTVATGDVVDVVEKSESGWWFCQMKTKRGWVPASYLEPLDSPDEAEDPDPNYAGEPYVTIKAYAAVEEDEVSLSEGEAIEVIHKLLDGWWVVRKGDITGYFPSMYLQKAGEEITQAQRQIRSRGAPPRRSTIRNAQSIHQRSRKRLSQDTYRRNSVRFLQQRRRPARPGPQSPDSKDNPSTPRAKPQPAVPPRPSSDLILHRCTESTKRKLTSAV | null | null | cellular defense response [GO:0006968]; cellular response to cadmium ion [GO:0071276]; cellular response to glucose stimulus [GO:0071333]; cellular response to reactive oxygen species [GO:0034614]; cellular response to testosterone stimulus [GO:0071394]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; epithelial cell proliferation [GO:0050673]; hydrogen peroxide biosynthetic process [GO:0050665]; inflammatory response [GO:0006954]; leukocyte mediated cytotoxicity [GO:0001909]; leukotriene metabolic process [GO:0006691]; negative regulation of smooth muscle contraction [GO:0045986]; neutrophil-mediated killing of fungus [GO:0070947]; neutrophil-mediated killing of gram-positive bacterium [GO:0070946]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of JNK cascade [GO:0046330]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein targeting to membrane [GO:0006612]; reactive oxygen species biosynthetic process [GO:1903409]; regulation of respiratory burst involved in inflammatory response [GO:0060264]; respiratory burst [GO:0045730]; respiratory burst involved in defense response [GO:0002679]; response to bacterium [GO:0009617]; response to yeast [GO:0001878]; smooth muscle contraction [GO:0006939]; superoxide anion generation [GO:0042554] | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; NADPH oxidase complex [GO:0043020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; SH3 domain binding [GO:0017124]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF16621;PF08944;PF00787;PF00018; | 3.30.1520.10;2.30.30.40; | null | PTM: Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity. {ECO:0000250|UniProtKB:P14598}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14598}. Membrane {ECO:0000250|UniProtKB:P14598}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side {ECO:0000250|UniProtKB:P14598}. | null | null | null | null | null | FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P14598, ECO:0000250|UniProtKB:Q09014}. | Rattus norvegicus (Rat) |
F1M775 | DIAP1_RAT | MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDDQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMEEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIDNDDMRVQLNVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIEGLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITTQKQDLEAEVSKLTGEVAKLSKELEDAKKEMASLSAVAVAPSVSSSAAVPQAPPLPGTSGTVIPPPPPPPLPGGAVPPPPPPPLPAGTGIPPPPPLPGGACISSSPQLFGSTAIPPPPPLPGATAIPPPPPLPGDTAIPPPPPLPGXTAIPPPPPLPGATGVPPPPPPLPGSVGVPPPPPLPGGPGLPPPPPPFPGAPGIPPPPPGMGVPPPPPFGFGIPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSLAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCETDHPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAGCAVTSLLASELTKDDAVAASSAKVPKKSEGVTTILEEAKELVGRAS | null | null | actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; axon midline choice point recognition [GO:0016199]; brain development [GO:0007420]; cellular response to histamine [GO:0071420]; cytoskeleton organization [GO:0007010]; ephrin receptor signaling pathway [GO:0048013]; gene expression [GO:0010467]; multicellular organismal locomotion [GO:0071965]; negative regulation of neuron projection regeneration [GO:0070571]; neuron projection development [GO:0031175]; neuron projection retraction [GO:0106028]; positive regulation of cell migration [GO:0030335]; protein localization [GO:0008104]; protein localization to microtubule [GO:0035372]; regulation of cell shape [GO:0008360]; regulation of cytoskeleton organization [GO:0051493]; regulation of microtubule-based process [GO:0032886]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; sensory perception of sound [GO:0007605]; synaptic vesicle endocytosis [GO:0048488] | actin filament [GO:0005884]; brush border [GO:0005903]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; neuron projection [GO:0043005]; nucleus [GO:0005634]; presynapse [GO:0098793]; ruffle membrane [GO:0032587]; synapse [GO:0045202] | actin binding [GO:0003779]; identical protein binding [GO:0042802]; profilin binding [GO:0005522]; small GTPase binding [GO:0031267]; transmembrane transporter binding [GO:0044325] | PF06346;PF06367;PF06371;PF02181; | 1.20.1170.10;1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10; | Formin homology family, Diaphanous subfamily | PTM: Phosphorylation at Thr-761 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity). {ECO:0000250|UniProtKB:O60610}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08808}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O08808}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O08808}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O60610}. Cytoplasm {ECO:0000250|UniProtKB:O08808}. Nucleus {ECO:0000250|UniProtKB:O08808}. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells. {ECO:0000250|UniProtKB:O08808}. | null | null | null | null | null | FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane (By similarity). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (By similarity). {ECO:0000250|UniProtKB:O08808, ECO:0000250|UniProtKB:O60610}. | Rattus norvegicus (Rat) |
F1M7L9 | PKP2_RAT | MAIPGSLGECGYIRTVLGQQILGHLDSSSLALPSEARLRLAGSSGRGDPVARSQRIQEQVQQTLARRGRSSVVGGNLHRTSSVPEYVYKLHLVENDFVGRQSPAARDYDMLKVGLSGWRDGSTLKVPCTSIKPHREKKTWIEALREGLEHTTDHTDCPAHYVYSHYYFNSKKSNILVFQHIKDKSLQRNAIILLSPEHCTCQHVRLIPSSVLPSLFNQLQLSPELYFSNMGTLYMTSIKGTLCIQLLKGKLPAKHQANFVTMAERRVYTLLLSSTTSSETSFRRTGDTLPSVTSGQSRVHGLHFHHVICDCLSRNADLEMTLERAVNMLDADHVPLSKISAAATFIQHESFQKSEARKRVNQLQGIPKLLQLLKVQNEDVQRAVCGALRNLVFEDNDNKVTVVLGKVNITKREGGGQAAGYMKETWKLANKNPVFLGLLWNLSSSDKLKHLMITEALLTLTESVIIPFSGWPEGDYPKANGLLDFDIFYNVTGCLRNMSSAGPDGRKVMRRCDGLIDSLVHYVRGTIADYQPDDKATENCVCILHNLSYQLEAELPEKYSQSIYMQNRNIQTNSNKSIGCFGSRSRKVKEQYQDTPMPEERSSPRGIEWLWHSIVIRMYLSLIAKSSRNYTQEASLGALQNLTAGSGPIPTSVARMVVQKENGLQHTRKMLHVGDPSVKKTAVSLLRNLSRNLSLQNEIAKETLPDLVSIIPDTVPSTDLLIETTASACYTLNNLMQNSYQNARDLLNTGGLQKIMTISIGEGYAPNKASKAASVLLYSLWAHTELHNAYKKAQFKKTDFVNSRTAKASHSLKD | null | null | adherens junction maintenance [GO:0034334]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cardiac muscle cell action potential [GO:0086001]; cardiac muscle cell action potential involved in contraction [GO:0086002]; cell-cell adhesion [GO:0098609]; cell-cell signaling involved in cardiac conduction [GO:0086019]; desmosome assembly [GO:0002159]; desmosome organization [GO:0002934]; gap junction assembly [GO:0016264]; heart development [GO:0007507]; intermediate filament bundle assembly [GO:0045110]; lipid homeostasis [GO:0055088]; maintenance of animal organ identity [GO:0048496]; maintenance of protein localization at cell tip [GO:0099017]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cell adhesion [GO:0045785]; protein localization to plasma membrane [GO:0072659]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of cell-substrate adhesion [GO:0010810]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of substrate adhesion-dependent cell spreading [GO:1900024]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; ventricular cardiac muscle cell action potential [GO:0086005]; ventricular cardiac muscle tissue morphogenesis [GO:0055010] | adherens junction [GO:0005912]; cell junction [GO:0030054]; cell tip [GO:0051286]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; intermediate filament binding [GO:0019215]; molecular adaptor activity [GO:0060090]; protein kinase C binding [GO:0005080] | PF00514; | 1.25.10.10; | Beta-catenin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99959}. Cell junction, desmosome {ECO:0000269|PubMed:21617128}. Cell junction {ECO:0000269|PubMed:19661460, ECO:0000269|PubMed:26858265}. Cytoplasm {ECO:0000250|UniProtKB:Q99959}. Note=Colocalizes with CTNNA3 and SCN5A/Nav1.5 at intercalated disks in the heart. {ECO:0000269|PubMed:19661460}. | null | null | null | null | null | FUNCTION: Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (By similarity). Required to maintain gingival epithelial barrier function (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes, via ANK3 stabilization and modulation of SCN5A/Nav1.5 localization to cell-cell junctions (PubMed:19661460, PubMed:21617128). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (PubMed:21617128). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (PubMed:26858265). Required for mitochondrial function, nuclear envelope integrity and positive regulation of SIRT3 transcription via maintaining DES localization at its nuclear envelope and cell tip anchoring points, and thereby preserving regulation of the transcriptional program (By similarity). Maintenance of nuclear envelope integrity protects against DNA damage and transcriptional dysregulation of genes, especially those involved in the electron transport chain, thereby preserving mitochondrial function and protecting against superoxide radical anion generation (By similarity). May play a role in junctional plaques (By similarity). {ECO:0000250|UniProtKB:Q99959, ECO:0000250|UniProtKB:Q9CQ73, ECO:0000269|PubMed:19661460, ECO:0000269|PubMed:21617128, ECO:0000269|PubMed:26858265}. | Rattus norvegicus (Rat) |
F1M7Y5 | KPCI_RAT | MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQSSMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV | 2.7.11.13 | null | actin filament organization [GO:0007015]; cell migration [GO:0016477]; cell-cell junction organization [GO:0045216]; cellular response to insulin stimulus [GO:0032869]; establishment of apical/basal cell polarity [GO:0035089]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; eye photoreceptor cell development [GO:0042462]; Golgi vesicle budding [GO:0048194]; intracellular signal transduction [GO:0035556]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of neuron apoptotic process [GO:0043524]; phosphorylation [GO:0016310]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of glucose import [GO:0046326]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein localization to plasma membrane [GO:1903078]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; response to interleukin-1 [GO:0070555]; response to peptide hormone [GO:0043434] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; PAR polarity complex [GO:0120157]; Schaffer collateral - CA1 synapse [GO:0098685]; Schmidt-Lanterman incisure [GO:0043220] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; phospholipid binding [GO:0005543]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00564;PF00069;PF00433; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation at Thr-412 in the activation loop is not mandatory for activation (By similarity). Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334 (By similarity). Phosphorylation at Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus (PubMed:11891849). Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation (By similarity). Phosphorylated at Thr-564 during the initial phase of long term potentiation (PubMed:27498875). {ECO:0000250|UniProtKB:P41743, ECO:0000250|UniProtKB:Q62074, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:27498875}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}. Membrane {ECO:0000250|UniProtKB:P41743}. Endosome {ECO:0000250|UniProtKB:P41743}. Nucleus {ECO:0000269|PubMed:11891849}. Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. {ECO:0000250|UniProtKB:P41743}. | 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=2.7.11.13; 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=2.7.11.13; | null | null | null | null | FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity (By similarity). Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (PubMed:27498875). {ECO:0000250, ECO:0000269|PubMed:27498875}. | Rattus norvegicus (Rat) |
F1M8W4 | SOX5_RAT | MLTDPDLPQEFERMSSKRPASPYGETDGEVAMVTSRQKVEEEESERLPAFHLPLHVSFPNKPHSEEFQPVSLLTQEACGPRTPAAQHSTMEVDGNKVMSSLAPYNSSTSPQKAEEGGRQSGESVSSAALGTPERRKGSLADVVDTLKQRKMEELIKNEPEDTPSIEKLLSKDWKDKLLAMGSGNFGEIKGTPESLAEKERQLMGMINQLTSLREQLLAAHDEQKKLAASQIEKQRQQMELAKQQQEQIARQQQQLLQQQHKINLLQQQIQVQGQLPPLMIPVFPPDQRTLAAAAQQGFLLPPGFSYKAGCSDPYPVQLIPTTMAAAAAATPGLGPLQLQQFYAAQLAAMQVSPGGKLLGLPQGNLGAAVSPTSIHTDKSTNSPPPKSKDEVAQPLNLSAKPKTSDGKSPASPTSPHMPALRINSGAGPLKASVPAALASPSARVSTIGYLNDHDAVTKAIQEARQMKEQLRREQQALDGKVAVVNSIGISNCRTEKEKTTLESLTQQLAVKQNEEGKFSHGMMDFNMSGDSDGSAGVSESRIYRESRGRGSNEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFNVGQQAQIPIATAGVVYPGAIAMAGMPSPHLPSEHSSVSSSPEPGMPVIQSTYGVKGEEPHIKEEIQAEDINGEIYEEYEEEEEDPDVDYGSDSENHIAGQAN | null | null | asymmetric neuroblast division [GO:0055059]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate commitment [GO:0045165]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system neuron differentiation [GO:0021953]; chondrocyte differentiation [GO:0002062]; in utero embryonic development [GO:0001701]; negative regulation of DNA-templated transcription [GO:0045892]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cartilage development [GO:0061036]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of mesenchymal stem cell differentiation [GO:2000741]; regulation of timing of neuron differentiation [GO:0060164]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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]; transcription cis-regulatory region binding [GO:0000976] | PF00505; | 1.10.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35710}. | null | null | null | null | null | FUNCTION: Transcription factor involved in chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes, such as COL2A1 and AGC1 (By similarity). Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate (PubMed:26150426). Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX6, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts (By similarity). Binds to the proximal promoter region of the myelin protein MPZ gene (By similarity). {ECO:0000250|UniProtKB:P35710, ECO:0000269|PubMed:26150426}. | Rattus norvegicus (Rat) |
F1MA98 | TPR_RAT | MAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVNETRECQNLRLELEKLNNQVKVLTEKNKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVTVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCTLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQNKLENSLTELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLVSTPKRSSTSQTVSTPAPEPIIESTETIEAKAALKQLQEIFENYKKEKMDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSASNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLTELKKTLSSVQSEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKEVVQSPLNISLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLKEDLSKVRTEKESIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQKAMETSTQSSGDHQEQHISVQEMQELKDNLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTAQLQSELSRLRQELQDKTTKEEQLRQQMNEKDEKTWKAITVARSKIAHLSGVKDQLTKENEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPLLTVQQQTQATAFVQPTQQSHPQIEPANQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRAREEEEDSTIEAGDQVSDDTVEMPLPKKLKTVTPVGTEEEVMAEESTDGEAETQTYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDEDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESNQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETPAGDDGDEVFVETESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN | null | null | cell division [GO:0051301]; cellular response to heat [GO:0034605]; cellular response to interferon-alpha [GO:0035457]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mRNA export from nucleus [GO:0006406]; mRNA export from nucleus in response to heat stress [GO:0031990]; negative regulation of RNA export from nucleus [GO:0046832]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of translational initiation [GO:0045947]; nuclear pore organization [GO:0006999]; positive regulation of heterochromatin formation [GO:0031453]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein import into nucleus [GO:0042307]; protein export from nucleus [GO:0006611]; protein import into nucleus [GO:0006606]; regulation of mitotic sister chromatid separation [GO:0010965]; regulation of mitotic spindle assembly [GO:1901673]; regulation of protein localization [GO:0032880]; response to epidermal growth factor [GO:0070849]; RNA export from nucleus [GO:0006405]; RNA import into nucleus [GO:0006404] | cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; dynein complex binding [GO:0070840]; heat shock protein binding [GO:0031072]; mitogen-activated protein kinase binding [GO:0051019]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; structural constituent of nuclear pore [GO:0017056]; tubulin binding [GO:0015631] | PF07926; | 1.10.287.1490; | TPR family | PTM: Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). Plays a role in the regulation of nuclear protein export. {ECO:0000250, ECO:0000269|PubMed:11839768}. | Rattus norvegicus (Rat) |
F1MAB7 | DGKI_RAT | MDAAGRGCHLLPLPAARGPARAPAASSALSPAGLCSGTASASSAAAGAVAMNPSSSAGEERGATGGSSSSGSGAGSCCLGAEGGVDPRGAGAAAAAALEEPAAAGQKEKEEALEEKLRDLTFRKQVSYRKAISRTGLQHLAPAHPLGLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGTEQENKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQDLKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSVPDRLRIRVNKISLQDYEGLHYDKEKLREASIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDQETSFPRAISAQRLSPRWCFLDATSADRFYRIDRSQEHLHFVMEISHDEIFILDPDMVVSQQAGTPPGMPDLVVEQASGLSDWWNPALRKRMLSDSGMITPHYEDSDLKDFSHSRVLQSPVSSEDHAILQAVITGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGEIVKYILDHGPAELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETAV | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; excitatory postsynaptic potential [GO:0060079]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; neurotransmitter secretion [GO:0007269]; phosphatidic acid biosynthetic process [GO:0006654]; positive regulation of Ras protein signal transduction [GO:0046579]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; Ras protein signal transduction [GO:0007265]; regulation of long-term synaptic depression [GO:1900452]; regulation of synaptic transmission, glutamatergic [GO:0051966] | axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; extrinsic component of postsynaptic density membrane [GO:0099147]; extrinsic component of presynaptic active zone membrane [GO:0098891]; glutamatergic synapse [GO:0098978]; guanyl-nucleotide exchange factor complex [GO:0032045]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic membrane [GO:0097060]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; GTPase inhibitor activity [GO:0005095]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF12796;PF00130;PF00609;PF00781; | 2.60.200.40;3.30.60.20;1.25.40.20; | Eukaryotic diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:21119615}. Cell projection, dendrite {ECO:0000269|PubMed:21119615}. Presynapse {ECO:0000269|PubMed:21119615}. Postsynapse {ECO:0000269|PubMed:21119615}. Postsynaptic density {ECO:0000269|PubMed:21119615}. Synaptic cell membrane {ECO:0000269|PubMed:21119615}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:21119615}. Cytoplasm, cytosol {ECO:0000269|PubMed:15024004, ECO:0000269|PubMed:21119615}. Nucleus {ECO:0000250|UniProtKB:O75912}. Note=Excluded from inhibitory synapses (PubMed:21119615). Localization between cytoplasm and nucleus is regulated by protein kinase C (By similarity). Both in the detergent soluble and particulate fractions (PubMed:15024004). {ECO:0000250|UniProtKB:O75912, ECO:0000269|PubMed:15024004, ECO:0000269|PubMed:21119615}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15024004}. Note=Not detected in detergent soluble fraction. {ECO:0000269|PubMed:15024004}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:15024004}. Note=Not detected in detergent soluble fraction. {ECO:0000269|PubMed:15024004}. | 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:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000305|PubMed:15024004}; 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:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000305|PubMed:15024004}; CATALYTIC ACTIVITY: [Isoform 2]: 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:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000305|PubMed:15024004}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340; Evidence={ECO:0000305|PubMed:15024004}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340; Evidence={ECO:0000305|PubMed:15024004}; 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:0000269|PubMed:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000305|PubMed:15024004}; CATALYTIC ACTIVITY: [Isoform 2]: 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:0000269|PubMed:15024004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000305|PubMed:15024004}; | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:15024004}. | 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:15024004). 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 (Probable). Has probably no preference for any of the diacylglycerols in terms of the acyl chain composition, especially for the acyl chain at the sn-2 position (PubMed:15024004). By controlling the diacylglycerol/DAG-mediated activation of RASGRP3, negatively regulates the Rap1 signaling pathway. May play a role in presynaptic diacylglycerol/DAG signaling and control neurotransmitter release during metabotropic glutamate receptor-dependent long-term depression (By similarity). {ECO:0000250|UniProtKB:D3YWQ0, ECO:0000269|PubMed:15024004, ECO:0000305}.; FUNCTION: [Isoform 2]: Has a decreased affinity for ATP and a reduced diacylglycerol kinase activity. Has no preference for any of the diacylglycerols in terms of the acyl chain composition. {ECO:0000269|PubMed:15024004}.; FUNCTION: [Isoform 3]: Has no diacylglycerol kinase activity. {ECO:0000269|PubMed:15024004}. | Rattus norvegicus (Rat) |
F1MAD2 | INADL_RAT | MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRKGLLVFTDGSITNGNAHRPCSSITASESLPWTQRSGNEDFTSVIQQMAQGRHIEYIDIERPSTGGLGFSVVALRSQSLGLIDIFVKEVHPGSVADRDQRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQSRTSTSSADTTLPETVRWGHTEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGSTNVQGMTSEQVAQVLRNCGNSVRMLVARDPVGEIAVTPPTPASLPVALPVVATRTLGSDSSPFETYNVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSIIPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEQPSSREAVAEPPEVPELTGSLKPETNSRMEAEEIGERLDNLRKDTVQALEKPDVYPEDIPGCPENELKSRWENLLGPDYEVMVATLDTQIADDEELQKYSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRTVEPSLLEAEVDRSVDVSTEDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPMRSVIVIRSLVADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEEEKEEKEEHFIFHSNNNGDNSESPETVHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDMDSSSEAWEMHEFLSPRLERRGEEREMLVDEEYEIYQDRLRDMEAHPPPPHIREPTSASPRLDLQAGPQWLHADLSGGEILECHDTESMMTAYPQEMQDYSFSTTDMMKETFGLDSRPPMPSSEGNGQHGRFDDLEHLHSLVSHGLDLGMMTPSDLQGPGVLVDLPAVTQRREQEELPLYRLPSARVVTKPSSHVGMVSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTKALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPSVNNKGKTPPQNQDQNTQEKKAKRHGTAPPPMKLPPPYRAPSADTEESEEDSALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPDGPAAADGRMRVGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVNQMAVAPFPVPSHSPSPVEDLGGTEPVSSEEDSSVDAKPLPERESSKPEDLTQAVDDSMVAEQEKASESPDSAARQMKQPGYSAQVSSSSQEIPSAPAPLCQSTHADVTGSGNFQAPLSVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGVDLRSSSHEEAITALRQTPQKVRLVIYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIVKGGAADLDGRLIRGDQILSVNGEDVRQASQETVATILKCVQGLVQLEIGRLRAGSWASSRKTSQNSQGDQHSAHSSCRPSFAPVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGVSIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGDRIVSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEMMSAGSQLGSPTADRHPQDPEELLQRTAD | null | null | establishment of apical/basal cell polarity [GO:0035089]; microtubule organizing center organization [GO:0031023]; regulation of microtubule cytoskeleton organization [GO:0070507]; tight junction assembly [GO:0120192] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; subapical complex [GO:0035003]; tight junction [GO:0070160] | null | PF09045;PF00595; | 1.20.1440.360;2.30.42.10; | null | null | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (By similarity). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}. | null | null | null | null | null | FUNCTION: Scaffolding protein that facilitates the localization of proteins to the cell membrane (By similarity). Required for the correct formation of tight junctions and epithelial apico-basal polarity (By similarity). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}. | Rattus norvegicus (Rat) |
F1MH07 | MICA1_BOVIN | MASTISTNPAHAHFESFLQAQLCQDVLSSFQGLCGALGVEPGGGLSQYHKVKAQLNYWNAKSLWAKLDKRASQPVYQQGRACTGTKCLVVGAGPCGLRAAVELAMLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGSLDHISIRQLQLLLLKVALLLGVEIHWGITFTGLQPPPKKGSGWRAQLQPSPPAQLAKYEFDVLISAAGGKFVPEGFTVREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQSFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLHKDWPDTERLLGSANVVPEALQRFARAAADFATHGKLGKLEFARDAHGRPDVSAFDFTSMMRAESSARVQERHGTRLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGAGPLEVLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPSQVRDLYDMEAKEPVQRMSDETDSGKAATGAVGSQEELLRWCQEQTAGYPGVHVTDLSSSWADGLALCALVHRLRPALLEPSELQGMGALEATSWALKMAEHELGITPVLSAQAMVAGSDPLGLIAYLSHFHSAFKSVPHNPGSVSQGSPGTASAVLFLGKLQRTLQRTRTQENGEDAGGKKPRLEVKAETPSTEEPPVPKPDEPMTPPSQQQDASAEDLCALCGQHLYILERLCADGRFFHRSCFRCHICEATLWPGGYRQHPGDGYLYCLQHLPQTGHEEDSSDRGPESQDLPMSSENNTPSGPATPVDLHQGTSPVPNPIQPTRRLIRLSSPERQRLSSLHLTPDPEMEPPPKPPRSCSTLAHQALEASFKGWGMPVQSPQVLEAMEMGEEERSSSSEEETEEEEDVPLDSDMEHFLRNLAENSGTMNNYPTWRRTLLRRAKEEEMKRFCKAQAIQRRLNEIEAALRELEARGTELELALRSQSSSPEKQKALWVEQLLQLVQKKNSLVAEEAELMITVQELNLEEKQWQLDQELRTYMNREETLKTAADRQAEDQVLRKLLDVVNQRDALIRLQEERRLSELASEPGVQG | 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]; 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}. | Bos taurus (Bovine) |
F1MH24 | AAK1_BOVIN | MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINSVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKVITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPTKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKTQPPPSQPLPQSQPKQPQAPPTSQQPPSAPAQALPTQAQATPQHQQQLFLKQQQQQQTAPPAQQPAGTFYQQPQQQAQAPQFQAVHPAAQQPVIAQFPVVSQGSSQQQLIQNFYQQQQQQQQLATALHQQQLLTQQAALQQKTTAAAAPQPQAQPAAAASPAPAQEPAQIQAPVRQQPKVQTTPPPTIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKYPEKLGGSAESLIPGFQPTQGDAFAASSFSAGTAEKRKGGQTMDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL | 2.7.11.1 | null | endocytosis [GO:0006897]; positive regulation of Notch signaling pathway [GO:0045747]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of clathrin-dependent endocytosis [GO:2000369]; regulation of protein localization [GO:0032880] | cell leading edge [GO:0031252]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; terminal bouton [GO:0043195] | AP-2 adaptor complex binding [GO:0035612]; ATP binding [GO:0005524]; Notch binding [GO:0005112]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q2M2I8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11877461}; Peripheral membrane protein {ECO:0000269|PubMed:11877461}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P0C1X8}. Presynapse {ECO:0000250|UniProtKB:P0C1X8}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:P0C1X8}. | 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; Evidence={ECO:0000305}; 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; Evidence={ECO:0000250|UniProtKB:Q2M2I8}; | null | null | null | null | FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. {ECO:0000250|UniProtKB:Q2M2I8}. | Bos taurus (Bovine) |
F1MJR8 | TEX14_BOVIN | MSRAVHLPVPCPVQLGSLRNDSLEAQLHEYVKQGNYVKVKRILKKGIYVDAVNSLGQTALFIAALLGLTKLVDVLVDYGADPNHRCFDGSTPVHAAAFSGNQWILSKLLDAGGDLRLHDEKGRNPQTWALAAGKERSTVMVEFMQRCAAHMQAIIQGFSDLLKKIDSPQRLISGVPRFGGLMQGNPNGSPNRPPKAGVISAQNIYSFGFGKFYLTGGTQLAYLGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNGSRVTVKELHLSTHPHCSRLRMADLLIAEQEHSSKLRHPHVLQLMAVCLSPDLEKTRLVYERVTVGTLFSVLHERRAQFPVLHMEVIVHLLLQISDALRYLHSRGFIHRSLSSYAIHIVSTGEARLTNLEYMMESQDGGAHRGLTRVPLPTQLYNWAAPEVIIQKAATVKSDIYSFSVIVQEILTDNIPWDGLDGSVIKETIVLGNYLEADVRLPKPYYDIVKSGLQVKQKDRTMNLQDIRYIMKNDLKDFIGAQRTQPTESPRVQRYEFHPDVNVCLGLTSEHPKETPNLEIKELKETGSQFHSPRGHSSPTGKATPEPPVPDVSPVAQQTHRQDAASPACSVAEEARNPSPDQTSLCSFEINEIYSGCLDTADDPEEECPGTGSSLEGAIPNQTDELKSMEEELEKMEREVCCSCDEDESSSDADTELSCEDWEWQNDALCSPSRPEPARGAKGATNNRSMTEEYISKCVLNLKISQTLIHQNADLLRNVQQKIEKLEMIQKEQAERRSLWASSREFAGIHDSPSALGPPASSYLPPVVQRPGDQQLDPGGSGLTLARSPRTLPTLCGPGKQSRGEQFQPTHGAKASLERDRNQNTSSQGRPRESSPQSKTTQLSSALLTVPSHPQGSPTSSKPGQDSTRISMQSVSSEIYNAKSRNNKDDGEIHLKWKTEVKEMAAKAATGQLTVPPWHPRSGVALDSEAENEPDPLPQLPIRVSEHMDWQQAADYLKKSDEPGGNDKCGQTDSSDQRGRQSGPQRFTSIRHLPPREDEQPEHSEVFQANSDASVAVEKSYSGQSAQSTCSPESSEDTEDMTDEFLTPDHEYFYSSIAQENLALETSSPIDEDFEGIQHACARPQASGEEKFQMRKNLGKNSEILTKSQFQPIRSPEGEQDETLKEPPKEVKEKDISLTDIQDLSSISCEHDGSFKEVSCKTPKINHAPTSVSTPLSPGSLSSVASQYKDCLESIPFQDTKTGSTSCGTSQESTQTLSDKFTSVREKAKSLDSLLTSSEVLPARLTNLKRLPAFTGAGSSSIAKAPDTSRCATQRRSLPKELVEAISQHHIDELPPPSQELLDEIEHLKGQQVSSTALDENTASRPGSTENDQRHLEEQETHSNKEDSSMLWTKETQDLEEDTERAHSTLDEDLERWLQPPEDSTQLPDLPKGPAREASSKDQEVGEKKRKGEESTKPEKRKPESFLGTSEEEELKPCFWKRLGWSEPSRIIVLDQSDLSD | null | null | attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; intercellular bridge organization [GO:0043063]; male meiotic nuclear division [GO:0007140]; mitotic sister chromatid separation [GO:0051306]; mitotic spindle assembly checkpoint signaling [GO:0007094] | cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; kinetochore [GO:0000776]; midbody [GO:0030496] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672] | PF12796;PF07714; | 1.25.40.20;1.10.510.10; | Protein kinase superfamily | PTM: Phosphorylated on Thr residues by CDK1 during early phases of mitosis, promoting the interaction with PLK1 and recruitment to kinetochores. Phosphorylated on Ser-430 by PLK1 during late prometaphase promotes the rapid depletion from kinetochores and its subsequent degradation by the APC/C complex. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the intercellular bridges that connect male germ cell daughter cells after cell division. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
F1MLX5 | LGR4_BOVIN | MPGPLGLLCFLALGLRGSAEPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQLLDISMNNITQLPEDAFKNFPFLEELRLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSSLQSLRLDANHITSVPEDSFEGLTQLRHLWLDDNSLTEVPVHPLSNLPTLQALTLALNKISSIPDFAFTNLSSLVVLHLHNNKIKSLGQHCFDGLDNLETLDLNYNNLGEFPQAIKALPSLKELLFHSNSISVIPDGAFDGNPLLKTIHLYDNPLSFVGNSAFHNLSELHSLVIRGASMVQRFPNLTGTVRLESLTLTGTKISSISNNLCQEQKRLRTLDLSYNSIKDLPSFNGCHALEEISLQRNQIHQIKEDTFQGLTSLKILDLSRNLIHEIDDRAFAKLGSITNLDVSFNELTSFPTEGLNGLNQLKLVGNFKLKEALAAKDFVNLRSLSVPYAYQCCAFWGCDSYTHSNTEDNSLQDHSGSKDKGLSDVAGVTSSAENEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALFFNLLVILTTFASCTSVPSSKLFIGLISVSNLFMGAYTGILTFLDAVSWGRFAEFGIWWEIGSGCKIAGFLAVFSSESAIFLLMLAAVERSLSAKDMMKNGKSNHLRQFRIAALLAFLGAAVAGSFPLFHRGEYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAIIYTKLYCNLEKEDLSESSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAVSISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKEDWKLLKRHVSKKSGSASVSISSQAGCVEQDFYYDCGMYSHLQGNLTVCDCCEAFLLTKPVSCKHLIKSHSCPALTVGSCQRPDGYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVKD | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; circadian regulation of gene expression [GO:0032922]; digestive tract development [GO:0048565]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; hair follicle development [GO:0001942]; hormone-mediated signaling pathway [GO:0009755]; innate immune response [GO:0045087]; intestinal stem cell homeostasis [GO:0036335]; male genitalia development [GO:0030539]; metanephric glomerulus development [GO:0072224]; metanephric nephron tubule morphogenesis [GO:0072282]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of cytokine production [GO:0001818]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; osteoblast differentiation [GO:0001649]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF00560;PF13855;PF01462; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BXB1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BXB1}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however required additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and pro-inflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP. Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (By similarity). {ECO:0000250|UniProtKB:A2ARI4, ECO:0000250|UniProtKB:Q9BXB1}. | Bos taurus (Bovine) |
F1MMS9 | ITA3_BOVIN | MGPGPSRAAGVLRPLLGMLALMVAASNRAASAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLAVPDGYTNRTGAVYLCPLTAHKNDCERMDIKEKSNPNHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDARDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKDPEDQGNLYIGYTMQVGSAILHPTNITIVTGAPRHQHVGAVFLLSQEAGGDLRRRQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYIFMNQAGTSFPDHPSLLLHGPSRSAFGFSVASIGDVNQDGFQDIAVGAPFEGLGKVYIYHGSSRGLLRQPQQVIHGEQLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDRIVLLRARPVINILHKTLVAKPSILDPAFCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLHFARSQSAVFHGFFSMPEMRCQTLELLLMDNVRDKLRPITISMNYSLPLRLPDRPQLGLGSLDAYPVLNQAQALENHTEVQFQKECGQDNRCDSNLQMRAAFVSELGQRLSRLQYRRDLRKLLLSINVTNTPSRKRAGEDAHEALLTLEVPPTLLLSSVRPPGACQANETIVCELGNPFKRNQRMELLIAFEVIGVTLHTRELQAQLQLSTSSHQDDLRPMTLPLLVDYTLQASLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLAALGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWHCQPPGDLINPLNLTLSVPGDGPPSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSEIQLSCGSDHTHCVWLECPIPDAPVITNVTIQARVWNSTFIEDYRDFDRVRVASWATLFLRTGVPTINMENKTVRFSVDIDSDLVEELPAEIELWLVLVAVSAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTEDY | null | null | cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; positive regulation of protein localization to plasma membrane [GO:1903078] | anchoring junction [GO:0070161]; external side of plasma membrane [GO:0009897]; filopodium membrane [GO:0031527]; integrin complex [GO:0008305] | integrin binding [GO:0005178]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I membrane protein {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. {ECO:0000250|UniProtKB:P26006}. | null | null | null | null | null | FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. {ECO:0000250|UniProtKB:P26006}. | Bos taurus (Bovine) |
F1MNN4 | FBXW7_BOVIN | MNQELLSVGSKRRRTGGSLRGNPSSSQADEEQMNRVLEEEQQQPRHQEEEHAARNGEVVGAEPRPGDQNDPQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHRNSVTNSNSIVDLPIHQRSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPNKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked ubiquitination [GO:0070534]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; ubiquitin recycling [GO:0010992] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | phosphothreonine residue binding [GO:0050816]; ubiquitin binding [GO:0043130]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF12937;PF00400; | 1.20.1280.50;2.130.10.10; | null | PTM: Phosphorylation at Thr-204 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-204 and subsequent interaction with PIN1 (PubMed:25624101). Ubiquitination leads to its degradation (PubMed:25624101). {ECO:0000250|UniProtKB:Q969H0, ECO:0000269|PubMed:25624101}. | 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. 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), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, MLST8, RICTOR, and probably PSEN1. 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). 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}. | Bos taurus (Bovine) |
F1MSG6 | RPGF2_BOVIN | MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLCSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPAREAPLPFILLGGSEKGFGIFVDSVDSASKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVVQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKTFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPTDKKPVKSETSPVAPRAGLQPKAQPQPQPPQPPHKLNQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRRPAEDTISNTSSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSLPVSLPDERRQRPSVSIVETSLASGRLERRPAVEPDQYSLGSCAPLSESRGLYAAATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYPGDAAGLWASSSHMDQIMFPDHSAKYSRQSQSRESLDQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSLDADSSSMTAVTAEEAKPAAMAAHIAVTPSAAKGLIARKEGRYREPPPTPPGYVGIPITDFPEAHPHPARKPPDYTVALQRSRMLARPAEPPAPGSARPAPRPQWHRPGDGDPRAGPCAPPGLTAEEDEDEQVSAV | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; blood vessel development [GO:0001568]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; cAMP-mediated signaling [GO:0019933]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of endothelial barrier [GO:0061028]; forebrain neuron development [GO:0021884]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of melanin biosynthetic process [GO:0048022]; nerve growth factor signaling pathway [GO:0038180]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein binding [GO:0032092]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of vasculogenesis [GO:2001214]; Rap protein signal transduction [GO:0032486]; Ras protein signal transduction [GO:0007265]; regulation of cell junction assembly [GO:1901888]; ventricular system development [GO:0021591] | apical plasma membrane [GO:0016324]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; late endosome [GO:0005770]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | beta-1 adrenergic receptor binding [GO:0031697]; cAMP binding [GO:0030552]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; PDZ domain binding [GO:0030165]; WW domain binding [GO:0050699] | PF00595;PF00788;PF00617;PF00618; | 2.30.42.10;2.60.120.10;1.10.840.10;1.20.870.10; | RAPGEF2 family | PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions (By similarity). Binds to cAMP. {ECO:0000250, ECO:0000269|PubMed:23800469}. | Bos taurus (Bovine) |
F1MWM0 | ABCA4_BOVIN | MGFARQIKLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNVNPLYSKHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTAGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWRELRTLSQLMNTLRMHPERIAGRGIRIREVLKDDEMLTLFLVKNIGLSDSVVYLLVNSQVRPEQFARGVPDLMLKDIACSEALLERFLIFPQRRAAQTVRGSLCSLSQGTLQWMEDTLYANVDFFKLFHVFPRLLDSRSQGMNLRSWGRILSDMSPRIQEFIHRPSVQDLLWVTRPLVQTGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDERTTTFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPATRRILKNANSTFEELERVRKLVKVWEEVGPQIWYFFDKSTQMSMIRDTLENPTVKAFWNRQLGEEGITAEAVLNFLYNGPREGQADDVDNFNWRDIFNITDRALRLANQYLECLILDKFESYDDEFQLTQRALSLLEENRFWAGVVFPDMHPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEHGITRSQAQEEVPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNRVIWCTWFLDSFSIMSMSICLLTIFIMHGRILHYSNPFILFLFLLAFSIATIMQCFLLSTFFSRASLAAACSGVIYFTLYLPHILCFAWQDRITADMKMAVSLLSPVAFGFGTEYLARFEEQGVGLQWSNIGNSPMEGDEFSFLMSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPITEEMEDPEYPEGINDCFFERELPGLVPGVCVKNLVKIFEPYGRPAVDRLNITFYESQITAFLGHNGAGKTTTLSIMTGLLPPTSGTVLVGGKDIETNLDAIRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWDKAQLEMEAMLEDTGLHHKRNEEAQDLSGGVQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADILGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRRMKTIQSQGRGREATCSCASKGFSVRCPACAEAITPEQVLDGDVNELTDMVHHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDLDSGHLFAGGTQQKRENINLRHPCSGPSEKAGQTPQGSSSHPREPAAHPEGQPPPEREGHSRLNSGARLIVQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSLIIPPFGEYPALTLHPWMYGQQYTFFSMDQLDSEWLSALADVLVNKPGFGNRCLKEEWLPEFPCGNSSPWKTPSVSPDVTHLLQQQKWTADQPSPSCRCSTREKLTMLPECPEGAGGLPPPQRIQRSTEILQDLTDRNVSDFLVKTYPALIRSSLKSKFWVNEQRYGGISVGGKLPAPPFTGEALVGFLSDLGQLMNVSGGPMTREAAKEMPAFLKQLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLHKDKNPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFVSGVSPTTYWLTNFLWDIMNYTVSAALVVGIFIGFQKKAYTSSENLPALVALLMLYGWAVIPMMYPASFLFDIPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRINAMLRKLLIIFPHFCLGRGLIDLALSQAVTDVYARFGEEHSSNPFQWDLIGKNLAAMAVEGVVYFLLTLLIQYQFFFSRWTTEPAKEPITDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTAVTSGDATVAGKSILTNISDVHQSMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIERVTNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIMGIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIRSPKDDLLPDLGPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFRLLVSHKDSLLIEEYSVTQTTLDQVFVNFAKQQNETYDLPLHPRAAGASRQAKEVDKGNSAPQG | 7.6.2.1 | null | lipid transport [GO:0006869]; phospholipid transfer to membrane [GO:0006649]; phospholipid translocation [GO:0045332]; photoreceptor cell maintenance [GO:0045494]; retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; visual perception [GO:0007601] | endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; rod photoreceptor disc membrane [GO:0120202] | 11-cis retinal binding [GO:0005502]; ABC-type transporter activity [GO:0140359]; all-trans retinal binding [GO:0005503]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; ATPase-coupled transmembrane transporter activity [GO:0042626]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; N-retinylidene-phosphatidylethanolamine flippase activity [GO:0140347]; phosphatidylethanolamine flippase activity [GO:0090555]; phospholipid transporter activity [GO:0005548]; retinoid binding [GO:0005501]; retinol transmembrane transporter activity [GO:0034632] | PF12698;PF00005; | 3.40.50.300; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:11320094, ECO:0000269|PubMed:9092582, ECO:0000269|PubMed:9202155}.; PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal fragment and a 115-kDa C-terminal fragment that are linked through disulfide bonds. {ECO:0000269|PubMed:11320094, ECO:0000269|PubMed:9092582}.; PTM: Phosphorylation is independent of light exposure and modulates ATPase activity. {ECO:0000269|PubMed:21721517}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9092582, ECO:0000269|PubMed:9202155, ECO:0000269|PubMed:9288089}. Cytoplasmic vesicle {ECO:0000269|PubMed:21721517}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P78363}. Note=Localized to the rim and incisures of rod outer segments disks. {ECO:0000269|PubMed:9092582, ECO:0000269|PubMed:9288089}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + N-all-trans-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-retinylidenephosphatidylethanolamine(in) + phosphate; Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24707049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189; Evidence={ECO:0000305|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000305|PubMed:22735453}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) + phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167887, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24707049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193; Evidence={ECO:0000305|PubMed:24707049}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=278 uM for ATP (with a purified ABCA4) {ECO:0000269|PubMed:10075733}; KM=33 uM for ATP (with ABCA4 reconstituted into brain lipid membrane) {ECO:0000269|PubMed:10075733}; KM=725 uM for ATP (reconstituted into brain lipid membrane, plus 80 uM all-trans-retinal) {ECO:0000269|PubMed:10075733}; KM=18 uM for ATP (with amiodarone) {ECO:0000269|PubMed:10075733}; KM=400 uM for ATP (with all-trans-retinal) {ECO:0000269|PubMed:10075733}; KM=666 uM for ATP (with all-trans-retinal plus amiodarone) {ECO:0000269|PubMed:10075733}; KM=75 uM for ATP (with CHAPS-solubilized ABCA4) {ECO:0000269|PubMed:10767284}; KM=32 uM for ATP (with ABCA4 reconstituted into soybean phospholipid) {ECO:0000269|PubMed:10767284}; KM=20 uM for ATP (with ABCA4 reconstituted into brain polar lipid) {ECO:0000269|PubMed:10767284}; KM=25 uM for ATP (with ABCA4 reconstituted into ROS phospholipid) {ECO:0000269|PubMed:10767284}; KM=112 uM for ATP (with CHAPS-solubilized ABCA4 and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; KM=56 uM for ATP (with ABCA4 reconstituted into soybean phospholipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; KM=106 uM for ATP (with ABCA4 reconstituted into brain polar lipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; KM=75 uM for ATP (with ABCA4 reconstituted into ROS phospholipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; KM=0.02 mM for ATP (in the presence of 40 uM retinal) {ECO:0000269|PubMed:24707049}; Vmax=27 nmol/min/mg enzyme (for ATP hydrolysis and with a purified ABCA4) {ECO:0000269|PubMed:10075733}; Vmax=1.3 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into brain lipid membrane) {ECO:0000269|PubMed:10075733}; Vmax=29 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into brain lipid membrane, plus 80 uM all-trans-retinal) {ECO:0000269|PubMed:10075733}; Vmax=2 nmol/min/mg enzyme (for ATP hydrolysis and with amiodarone as substrate) {ECO:0000269|PubMed:10075733}; Vmax=20 nmol/min/mg enzyme (for ATP hydrolysis and with all-trans-retinal as substrate) {ECO:0000269|PubMed:10075733}; Vmax=50 nmol/min/mg enzyme (for ATP hydrolysis and with all-trans-retinal and amiodarone as substrates) {ECO:0000269|PubMed:10075733}; Vmax=190 nmol/min/mg enzyme (for ATP hydrolysis and with CHAPS-solubilized ABCA4) {ECO:0000269|PubMed:10767284}; Vmax=50 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into soybean phospholipid) {ECO:0000269|PubMed:10767284}; Vmax=29 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into brain polar lipid) {ECO:0000269|PubMed:10767284}; Vmax=202 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into ROS phospholipid) {ECO:0000269|PubMed:10767284}; Vmax=402 nmol/min/mg enzyme (for ATP hydrolysis and with CHAPS-solubilized ABCA4 and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; Vmax=110 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into soybean phospholipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; Vmax=171 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into brain polar lipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; Vmax=673 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4 reconstituted into ROS phospholipid and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284}; Vmax=35.5 pmol/min/ug enzyme toward all-trans-retinal (in liposome) {ECO:0000269|PubMed:22735453}; Vmax=4.9 nmol/min/mg enzyme towards all-trans-retinal (in rod outer segments) {ECO:0000269|PubMed:22735453}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:22735453}; | null | FUNCTION: Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid (PubMed:10075733, PubMed:10767284, PubMed:20552428, PubMed:22735453, PubMed:24707049). Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (PubMed:10767284). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (PubMed:15471866, PubMed:20552428, PubMed:22735453). {ECO:0000269|PubMed:10075733, ECO:0000269|PubMed:10767284, ECO:0000269|PubMed:15471866, ECO:0000269|PubMed:20552428, ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24707049}. | Bos taurus (Bovine) |
F1N206 | DLDH_BOVIN | MQSWSRVYCSLVKRGHFSRISHGLQGVSVVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALLNNSHFYHLAHGKDFASRGIEMSEVRLNLEKMMEQKSNAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGSTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDTRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P09622}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622}; | branched-chain amino acid catabolic process [GO:0009083]; gastrulation [GO:0007369]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proteolysis [GO:0006508]; regulation of membrane potential [GO:0042391]; sperm capacitation [GO:0048240] | acetyltransferase complex [GO:1902493]; acrosomal matrix [GO:0043159]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252] | branched-chain alpha-keto acid dehydrogenase activity [GO:0047101]; dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660]; pyruvate dehydrogenase (NAD+) activity [GO:0034604] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:36854377}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:O08749}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P09622}. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO:0000250|UniProtKB:P09622}; | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). {ECO:0000250|UniProtKB:O08749, ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4}. | Bos taurus (Bovine) |
F1N3B8 | OAS2_BOVIN | MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVFFGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLWSYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCGAEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNWLRSLRQNESPGPSWNVLPASLYITPGHLLDKFVKDFLQPNQTFQDQIKKALKIICSFLEENCFRHSTTKIQVIQGGSTVKGTALKTGSDASLVVFANSLKSYTSPKNERYNIIKEIHEQLEACRQEKDFEVKFEISKWKPPWVLSFTLKSKVLNESVDFDVLPAFNALGELKSGSTPSPRTYTELIHLYKPSDVFLEGEFSACFTKLQRNFVRSLPLKLKDLIRLLKHWYCGCEKKLKQKGSLPPKYALELLSIYAWEKGSGAQDFDMAEGFRTVLELVIQYQHLCVFWTVNYSFDDEILRNFLLGQIRRTRPVILDPADPTGDVGGGHRWCWHLLAKEATEWLSSLCFKDKSGCPIQPWNVPKKRVQTPGSCGAGIYSMVNEMHLLRSHRFLD | 2.7.7.84 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29728}; | defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; interleukin-27-mediated signaling pathway [GO:0070106]; negative regulation of viral genome replication [GO:0045071]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of lactation [GO:1903487]; response to virus [GO:0009615]; type I interferon-mediated signaling pathway [GO:0060337] | cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471] | 2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872] | PF01909;PF10421;PF18144; | 1.10.1410.20;3.30.460.10; | 2-5A synthase family | PTM: Myristoylation is not essential for its activity. {ECO:0000250|UniProtKB:P29728}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000250|UniProtKB:P29728}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. | CATALYTIC ACTIVITY: Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence={ECO:0000250|UniProtKB:P29728}; | null | null | null | null | FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000250|UniProtKB:P29728}. | Bos taurus (Bovine) |
F1N476 | ECE2_BOVIN | MSVALQELGGGGNMVEYKRATLRDEDAPETPVEGGASPDAVEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW | 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | brain development [GO:0007420]; cardioblast differentiation [GO:0010002]; heart development [GO:0007507]; peptide hormone processing [GO:0016486]; protein processing [GO:0016485] | cytoplasmic vesicle membrane [GO:0030659]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12054617}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12054617}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000250|UniProtKB:P0DPD6}; | null | null | null | null | FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing (By similarity). {ECO:0000250|UniProtKB:B2RQR8, ECO:0000250|UniProtKB:P0DPD6}. | Bos taurus (Bovine) |
F1N5C8 | ENPP6_BOVIN | MAGKLGVLLLALVLSLAQPASARRKLLVFLLDGFRADYISDEALESLPGFKEIVSRGVKVDYLTPDFPTLSYPNYYSLMTGRHCEVHQMTGNYMWDPDTNKSFDLGINRDSRLPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKSVPTDINFVNAVSGALDVFKSGQADLAAIYYERVDVEGHHYGPSSPQRKDAVKAVDTVMAYMTKWIQERDLQDDLNVIIFSDHGMTDISWTDKVIKLDNYINLRDLQQLKGRGPVVSLWPAPGKHSEIYNKVRRVEHMTVYAKEDIPSRFYYKKGKFVSPLTLVADEGWFITENRESLPFWMNSTVTRKPEGWQWGWHGYDNELRAMRGIFLAFGPDFKSDFRAAPIRVVDIYNLMCKVTGVTPLPNNGSWSRVMCMLKDPASSAPGAPPCACALVTVLLVLLAILA | 3.1.4.-; 3.1.4.38 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8BGN3}; | choline metabolic process [GO:0019695]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | glycerophosphocholine cholinephosphodiesterase activity [GO:0047390]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; metal ion binding [GO:0046872] | PF01663; | 3.30.1360.180;3.40.720.10; | Nucleotide pyrophosphatase/phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:19545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:17754, ChEBI:CHEBI:295975; EC=3.1.4.38; Evidence={ECO:0000269|PubMed:23161088}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19546; Evidence={ECO:0000305|PubMed:23161088}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:44720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168, ChEBI:CHEBI:64683, ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:23161088}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44721; Evidence={ECO:0000305|PubMed:23161088}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:36083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30909, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36084; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41127, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74966, ChEBI:CHEBI:75529, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41128; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41003, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:34071, ChEBI:CHEBI:74344, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41004; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:40999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:75536, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41000; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine-phosphocholine = H(+) + phosphocholine + sphing-4-enine; Xref=Rhea:RHEA:41095, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57756, ChEBI:CHEBI:58906, ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:23161088}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41096; Evidence={ECO:0000305|PubMed:23161088}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 1-(9Z,12Z-octadecadienoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:75561, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41116; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=glycero-2-phosphocholine + H2O = glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:61684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:144950, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61685; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2000 uM for lysophosphatidylcholine {ECO:0000269|PubMed:23161088}; KM=5000 uM for glycerophosphocholine {ECO:0000269|PubMed:23161088}; KM=35 uM for p-nitrophenylphosphocholine {ECO:0000269|PubMed:23161088}; KM=5 uM for lysosphingomyelin {ECO:0000269|PubMed:23161088}; | null | null | null | FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells (PubMed:23161088). Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids (By similarity). {ECO:0000250|UniProtKB:Q8BGN3, ECO:0000269|PubMed:23161088}. | Bos taurus (Bovine) |
F1N9Y5 | KSYK_CHICK | MASNMANPANHLPYFFGNITREEAEEYLMQGGMSDGLYLLRQSRNYLGGFALSLAYGRKVHHYTIERELSGTYAIAGGKSHASPAELINYHSEEADGLICLLRKSFNRPPGVEPKTGPFEDLKENLIREYVKQTWNLQGHALEQAIISQKPQLEKLIATTAHEKMPWFHGRISREESEHRILIGSRNNGKFLIRERDSNGSYALCLLNDGKVLHYRIDRDKTGKLSIPDGKRFDTLWQLVEHYSYKPDGLLRVLSIPCPRHGSESDNVVFDTRPLPGTPSKLQTPIGAPSDDQTPFNPYVLQRARGLIGAEKGDQREALPMDTEVYESPYADPDEIKPKNVTLDRKLLTLEEGELGSGNFGTVKKGFYKMKKGAKPVAVKILKNESNDPAIKDELLREANVMQQLDNPYIVRMIGICEAEAWMLVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEENNFVHRDLAARNVLLVTQHYAKISDFGLSKALSADENYYKAQSHGKWPVKWYAPECMNFYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGGEVAQMIERGERMECPEACPVEVYDLMKLCWTYNVDDRPGFVAVELRLRNYYYDISH | 2.7.10.2 | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; blood vessel morphogenesis [GO:0048514]; cell differentiation [GO:0030154]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to molecule of fungal origin [GO:0071226]; defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; leukocyte activation involved in immune response [GO:0002366]; leukocyte cell-cell adhesion [GO:0007159]; lymph vessel development [GO:0001945]; macrophage activation involved in immune response [GO:0002281]; neutrophil activation involved in immune response [GO:0002283]; neutrophil chemotaxis [GO:0030593]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of bone resorption [GO:0045780]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of mast cell degranulation [GO:0043306]; regulation of arachidonic acid secretion [GO:0090237]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of neutrophil degranulation [GO:0043313]; regulation of phagocytosis [GO:0050764]; regulation of platelet activation [GO:0010543]; regulation of platelet aggregation [GO:0090330]; regulation of superoxide anion generation [GO:0032928]; serotonin secretion by platelet [GO:0002554]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytosol [GO:0005829]; early phagosome [GO:0032009]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017; | 3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SYK/ZAP-70 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. Cytoplasm, cytosol {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include DEPTOR, VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. {ECO:0000269|PubMed:9697839}. | Gallus gallus (Chicken) |
F1NBL0 | MUC6_CHICK | CSTWGGGHFSTFDKYQYDFTGTCNYIFATVCDESSPDFNIQFRRGLDKKIARIIIELGPSVIIVEKDSISVRSVGVIKLPYASNGIQIAPYGRSVRLVAKLMEMELVVMWNNEDYLMVLTEKKYMGKTCGMCGNYDGYELNDFVSEGKLLDTYKFAALQKMDDPSEICLSEEISIPAIPHKKYAVICSQLLNLVSPTCSVPKDGFVTRCQLDMQDCSEPGQKNCTCSTLSEYSRQCAMSHQVVFNWRTENFCSVGKCSANQIYEECGSPCIKTCSNPEYSCSSHCTYGCFCPEGTVLDDISKNRTCVHLEQCPCTLNGETYAPGDTMKAACRTCKCTMGQWNCKELPCPGRCSLEGGSFVTTFDSRSYRFHGVCTYILMKSSSLPHNGTLMAIYEKSGYSHSETSLSAIIYLSTKDKIVISQNELLTDDDELKRLPYKSGDITIFKQSSMFIQMHTEFGLELVVQTSPVFQAYVKVSAQFQGRTLGLCGNYNGDTTDDFMTSMDITEGTASLFVDSWRAGNCLPAMERETDPCALSQLNKISAETHCSILTKKGTVFETCHAVVNPTPFYKRCVYQACNYEETFPYICSALGSYARTCSSMGLILENWRNSMDNCTITCTGNQTFSYNTQACERTCLSLSNPTLECHPTDIPIEGCNCPKGMYLNHKNECVRKSHCPCYLEDRKYILPDQSTMTGGITCYCVNGRLSCTGKLQNPAESCKAPKKYISCSDSLENKYGATCAPTCQMLATGIECIPTKCESGCVCADGLYENLDGRCVPPEECPCEYGGLSYGKGEQIQTECEICTCRKGKWKCVQKSRCSSTCNLYGEGHITTFDGQRFVFDGNCEYILAMDGCNVNRPLSSFKIVTENVICGKSGVTCSRSISIYLGNLTIILRDETYSISGKNLQVKYNVKKNALHLMFDIIIPGKYNMTLIWNKHMNFFIKISRETQETICGLCGNYNGNMKDDFETRSKYVASNELEFVNSWKENPLCGDVYFVVDPCSKNPYRKAWAEKTCSIINSQVFSACHNKVNRMPYYEACVRDSCGCDIGGDCECMCDAIAVYAMACLDKGICIDWRTPEFCPVYCEYYNSHRKTGSGGAYSYGSSVNCTWHYRPCNCPNQYYKYVNIEGCYNCSHDEYFDYEKEKCMPCAMQPTSVTLPTATQPTSPSTSSASTVLTETTNPPV | null | null | cholesterol homeostasis [GO:0042632]; intestinal cholesterol absorption [GO:0030299]; macrophage activation involved in immune response [GO:0002281]; negative regulation of cell growth [GO:0030308] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; supramolecular fiber [GO:0099512] | antigen binding [GO:0003823]; virion binding [GO:0046790] | PF08742;PF01826;PF00094; | 2.10.25.10; | null | PTM: N-glycosylated with N-acetylglucosamine (6.7%), N-acetylgalactosamine (0.6%), galactose (1.8%), mannose (4.6%), N-acetylneuraminic acid (1.0%) and sulfate-containing glycans (0.7%). {ECO:0000269|PubMed:21484392}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Ovomucin, the glycoprotein responsible for the gel properties of egg white, is composed for 2 subunits, alpha-ovomucin/MUC5B and beta-ovomucin/MUC6. {ECO:0000269|PubMed:5119791}. | Gallus gallus (Chicken) |
F1NCD6 | NLS1_CHICK | MAGGGGAERVRVGAAAAGLLPPSCRQPRRRESRERLSVCSKLCYAVGGAPYQTTGCALGFFLQIYLLDVAQLDPFYASIILFVGRAWDAITDPMVGFFISKTPWTRFGRLMPWIIFSTPFAVISYFLIWFVPDISTGQVMWYLIFYCIFQTLVTCFHVPYSALTMFISREQSERDSATAYRMTVEVLGTVLGTAIQGQIVGKAVTPCIENPPFLSETNFSVAIRNVNMTHYTGSLADTRNAYMVAAGVIGGLYILCAVILSVGVREKRESSELQSDEPVSFFRGLKLVMNHGAYIKLITGFLFTSLAFMLLEGNFALFCTYTLGFRNEFQNILLAIMLSATLTIPFWQWFLTRFGKKTAVYVGISSAVPFLITVVVLDSNLVVTYIVAVAAGISVAAAFLLPWSMLPDVIDDFKLQHPESRGHEAIFFSFYVFFTKFTSGVSLGISTLSLDFAGYQTRGCSQPSEVNITLKLLVSAVPVGLILLGLLLFKLYPIDEEKRRENKKALQDLREESNSSSESDSTELANIV | null | null | carbohydrate transport [GO:0008643]; fatty acid transport [GO:0015908]; lipid transport across blood-brain barrier [GO:1990379]; lysophospholipid translocation [GO:0140329] | endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | fatty acid transmembrane transporter activity [GO:0015245]; lysophospholipid:sodium symporter activity [GO:0051978] | PF13347; | 1.20.1250.20; | Major facilitator superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9DA75}; Multi-pass membrane protein {ECO:0000269|PubMed:34135507}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9DA75}; Multi-pass membrane protein {ECO:0000269|PubMed:34135507}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) = a 1-acyl-sn-glycero-3-phosphocholine(out) + Na(+)(out); Xref=Rhea:RHEA:44376, ChEBI:CHEBI:29101, ChEBI:CHEBI:58168; Evidence={ECO:0000250|UniProtKB:Q9DA75}; CATALYTIC ACTIVITY: Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine(in) + Na(+)(in) = 1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine(out) + Na(+)(out); Xref=Rhea:RHEA:43860, ChEBI:CHEBI:29101, ChEBI:CHEBI:73873; Evidence={ECO:0000250|UniProtKB:Q9DA75}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) + Na(+)(in) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) + Na(+)(out); Xref=Rhea:RHEA:43856, ChEBI:CHEBI:28610, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9DA75}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) = 1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + Na(+)(out); Xref=Rhea:RHEA:43864, ChEBI:CHEBI:29101, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:Q9DA75}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(in) + Na(+)(in) = a 1-acyl-sn-glycero-3-phosphoethanolamine(out) + Na(+)(out); Xref=Rhea:RHEA:43868, ChEBI:CHEBI:29101, ChEBI:CHEBI:64381; Evidence={ECO:0000250|UniProtKB:Q9DA75}; | null | null | null | null | FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function (By similarity). Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain (By similarity). Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain (By similarity). Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons (By similarity). Does not transport docosahexaenoic acid in unesterified fatty acid (By similarity). {ECO:0000250|UniProtKB:Q9DA75}. | Gallus gallus (Chicken) |
F1ND48 | FBH1_CHICK | MHLTADDCEALSRSTEGLSSLTQPLNQRRSRGDVNRGLQPTHRTRTQPGAQGRQKNIMDYFKVSQRQQAVAGRTKDISIKEEVLDPFFAEDDESSISSVMETSGDSSSFLENEYMGNSRKRPLSSTAPGRLQIENDLWGEPEKKAVVVHPEHSQIKQELDDEIEIEPVPDSHYGLLGTRNWEVPQGSIEDLPDEVLRSIFAFLPVTDLYQSLSLVCRRWRIIVGDPWFIPWKKLYHQYLVKEDMALRRVEQVLQDFAITGQHKECILGLIRCVSTIPTSRNVDPSAVLQCLKGHHLFSRAEVCITNKLPHLQSKTGPEYMWAIITAMVLFSDGVRDIQRLMACLQRPCSSLSIVDVTETLYCIATLLYAMREKNINITNRIHYNIFYCLYLMENASVTAPQVVEEETPSSRCRQDFWSSSLSEVKLTHEQQRILNHKIERGQIVKIMAFAGTGKTSTLVKYAEKFADLSFLYVTFNKAVAERGRLVFPRNVTCKTFHSLAFGSVGKLYKEKGKLNFSKLSAYSVSFLIQNREGQSIFIRGKTVSQTLENFFASSDEEICEEHTPVWFKNTHGERKLVTPEEKRINVEEAKEIWRNMKKLDGDVERKYKITCDGYLKLWQLSKPQLSGYDAIFVDEAQDCTPAIVDIVLSQTCGVILVGDPHQQIYSFRGAVNTLYTVPHTHIYYLTQSFRFGPEIAYVGATILDVCKGIRNKTLVGGNQEGDVRGSMEGKITMLSRSNFTVFEDAAKLAGRERQIKIHIIGGLVRFGLSKIYDIWKLSQPADEREKANLVINDSFIKRWEENEGFIGLKDYATRVDDKELEMKIRIVEKFKERIPELVQKIESSHVLQEAMADYLIGTVHQAKGLEFDTVLIADDFVDVPCARDNNQRRPQFIIGMCPEDEWNLLYVAVTRAKKCLLMSQSLEHLLALAGEHFLRVELMGEAVKTGVACSTQQCTQTLQSGIRLVVKKLPLIHSNGSRDMGGYLCYSCVQKRFGSMTPLAFLPALQEEPIVL | 5.6.2.4 | null | DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; protein ubiquitination [GO:0016567]; replication fork processing [GO:0031297] | chromatin [GO:0000785]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; double-stranded DNA binding [GO:0003690]; isomerase activity [GO:0016853]; single-stranded DNA binding [GO:0003697] | PF12937;PF00580;PF13361; | 1.20.1280.50;3.40.50.300; | Helicase family, UvrD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFZ0}. Chromosome {ECO:0000250|UniProtKB:Q8NFZ0}. Note=Accumulates at sites of DNA damage or replication stress. Localizes to the nucleoplasm in absence of DNA damage. {ECO:0000250|UniProtKB:Q8NFZ0}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; 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=5.6.2.4; Evidence={ECO:0000250|UniProtKB:Q8NFZ0}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q8NFZ0}. | null | null | FUNCTION: 3'-5' DNA helicase and substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks (By similarity). Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:17283053). Also promotes cell death and DNA double-strand breakage in response to replication stress: promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress. {ECO:0000250|UniProtKB:Q8NFZ0, ECO:0000269|PubMed:17283053}. | Gallus gallus (Chicken) |
F1NHE9 | KCJ12_CHICK | MTAGRVNPYSIVSSEEDGLRLTTMPGINGFGNGKIHTRRKCRNRFVKKNGQCNVEFTNMDDKPQRYIADMFTTCVDIRWRYMLLLFSLAFLVSWLLFGLIFWLIALIHGDLENPGGDDTFKPCVLQVNGFVAAFLFSIETQTTIGYGFRCVTEECPLAVFMVVVQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVAMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRITEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEINEDSPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVLFEEKNQYKVDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSTNSFCYENELAFMSRDEDEEDDDSRGLDDLSPDNRHEFDRLQATIALDQRSYRRESEI | null | null | potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; protein homotetramerization [GO:0051289]; regulation of monoatomic ion transmembrane transport [GO:0034765] | membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242] | PF01007;PF17655;PF08466; | 1.10.287.70;2.60.40.1400; | Inward rectifier-type potassium channel family | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification is probably due to the blockage of outward current by cytoplasmic polyamines and/or magnesium ions. {ECO:0000269|PubMed:20019282, ECO:0000269|PubMed:21874019}. | Gallus gallus (Chicken) |
F1NJ67 | PCFT_CHICK | MAAPSDPPTAATPPAPPPPARRCLLAPSVEPLLFLATLALGLQVPLATQYLWDRLGAERGYVGPNASSPHGCGNGSGAVDPLREEVEALVAHWNLCINLGGFFVGLFSVTLFGPWSDSVGRRPVLVLPAVGMAVQAAVYLLVMYLRLHVAYLLLGRIISGLLGDYNLILAGCFASVADSSNQRTRTFRVAILEACLGVAGMVASVGGGQWRKAEGYINPFWLVLAASLAAALYAALCLQETVKQRRAAKLLTLQHYKAVYKLYTAPEDLSSRRKLALYSLAFFLLVTVHFGTKDLYVLYELGSPLCWASDLIGYGSAASYLAYLSSLGGLRLLQLCLEDTWVAEIGLISNIAGLVVISLATTTPLMFTGYGIMFLSMAATPVIRAKLSKLVGETEQGALFASVACVEGLCSLVATGVFNSLYPSTLHFMRGFPFLFGAILLLIPAAIMGWIEIQDSNLQYSHFSDASSSPADG | null | null | folate import across plasma membrane [GO:1904447]; transmembrane transport [GO:0055085] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endosome [GO:0005768]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886] | folic acid binding [GO:0005542]; folic acid:proton symporter activity [GO:0140211]; methotrexate transmembrane transporter activity [GO:0015350]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, SLC46A family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000269|PubMed:34040256}. Apical cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000269|PubMed:34040256}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q6PEM8}. Note=Localizes to the apical membrane of intestinal cells in iron-deficient cells, while it resides in the cytoplasm in iron-replete cells (By similarity). Localizes to the basolateral membrane of choroid plexus (By similarity). {ECO:0000250|UniProtKB:Q6PEM8}. | CATALYTIC ACTIVITY: Reaction=folate(in) + H(+)(in) = folate(out) + H(+)(out); Xref=Rhea:RHEA:70159, ChEBI:CHEBI:15378, ChEBI:CHEBI:62501; Evidence={ECO:0000305|PubMed:34040256}; CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate(in) + H(+)(in) = (6S)-5-methyl-5,6,7,8-tetrahydrofolate(out) + H(+)(out); Xref=Rhea:RHEA:70167, ChEBI:CHEBI:15378, ChEBI:CHEBI:18608; Evidence={ECO:0000250|UniProtKB:Q6PEM8}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + methotrexate(in) = H(+)(out) + methotrexate(out); Xref=Rhea:RHEA:70163, ChEBI:CHEBI:15378, ChEBI:CHEBI:50681; Evidence={ECO:0000250|UniProtKB:Q96NT5}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + pemetrexed(in) = H(+)(out) + pemetrexed(out); Xref=Rhea:RHEA:70171, ChEBI:CHEBI:15378, ChEBI:CHEBI:63724; Evidence={ECO:0000250|UniProtKB:Q96NT5}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for folic acid {ECO:0000269|PubMed:34040256}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-5.5. {ECO:0000269|PubMed:34040256}; | null | FUNCTION: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force (PubMed:34040256). Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus (PubMed:34040256). Functions at acidic pH via alternate outward- and inward-open conformation states (PubMed:34040256). Protonation of residues in the outward open state primes the protein for transport (PubMed:34040256). Binding of folate promotes breaking of salt bridge network and subsequent closure of the extracellular gate, leading to the inward-open state and release of protons and folate (PubMed:34040256). Also able to transport antifolate drugs, such as methotrexate and pemetrexed (PubMed:34040256). Also acts as a lower-affinity, pH-independent heme carrier protein and constitutes the main importer of heme in the intestine (By similarity). Imports heme in the retina and retinal pigment epithelium, in neurons of the hippocampus, in hepatocytes and in the renal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q96NT5, ECO:0000269|PubMed:34040256}. | Gallus gallus (Chicken) |
F1NPQ2 | MINP1_CHICK | MAPRRAACLLPLLVAVASAGLGGYFGTKSRYEEVNPHLAEDPLSLGPHAAASRLPAACAPLQLRAVLRHGTRYPTAGQIRRLAELHGRLRRAAAPSCPAAAALAAWPMWYEESLDRLAPRGRRDMEHLARRLAARFPALFAARRRLALASSSKHRCLQSGAAFRRGLGPSLSLGADETEIEVNDALMRFFDHCDKFVAFVEDNDTAMYQVNAFKEGPEMRKVLEKVASALCLPASELNADLVQVAFLTCSYELAIKNVTSPWCSLFSEEDAKVLEYLNDLKQYWKRGYGYDINSRSSCILFQDIFQQLDKAVDESRSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQANNYIRQAHRKFRSGRIVPYAANLVFVLYHCEQKTSKEEYQVQMLLNEKPMLFHHSNETISTYADLKSYYKDILQNCHFEEVCELPKVNGTVADEL | 3.1.3.62; 3.1.3.80 | null | intracellular monoatomic cation homeostasis [GO:0030003] | endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | 3-phytase activity [GO:0016158]; 4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]; bisphosphoglycerate 3-phosphatase activity [GO:0034417]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol hexakisphosphate 2-phosphatase activity [GO:0052826]; inositol pentakisphosphate phosphatase activity [GO:0052827]; inositol phosphate phosphatase activity [GO:0052745]; inositol trisphosphate phosphatase activity [GO:0046030]; inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity [GO:0030351]; inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity [GO:0030352]; inositol-hexakisphosphate phosphatase activity [GO:0004446] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family, MINPP1 subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:16759730, ECO:0000269|PubMed:9472008}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:9472008}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:20960, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58747; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20961; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,3,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77111, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58747, ChEBI:CHEBI:195534; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77112; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,3-trisphosphate + phosphate; Xref=Rhea:RHEA:77123, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195534, ChEBI:CHEBI:195536; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77124; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol 2,3-bisphosphate + phosphate; Xref=Rhea:RHEA:77127, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195536, ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77128; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77139, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77140; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77147, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:203600; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77148; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for inositol hexakisphosphate {ECO:0000269|PubMed:16759730}; Vmax=715 nmol/min/mg enzyme with inositol hexakisphosphate as substrate {ECO:0000269|PubMed:16759730}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-7.5. {ECO:0000269|PubMed:16759730}; | null | FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal chelators which control many aspects of cell physiology (PubMed:16759730). Has a weak in vitro activity towards 1D-myo-inositol 1,4,5-trisphosphate which is unlikely to be physiologically relevant. By regulating intracellular inositol polyphosphates pools, which act as metal chelators, it may control the availability of intracellular calcium and iron, which are important for proper neuronal development and homeostasis. May have a dual substrate specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering glycolytic bypass and is a regulator of systemic oxygen homeostasis as the major allosteric effector of hemoglobin (By similarity). {ECO:0000250|UniProtKB:Q9UNW1, ECO:0000269|PubMed:16759730}. | Gallus gallus (Chicken) |
F1NQJ3 | PMS2_CHICK | MEEAAPCSEPAKTIKRIDRESVHRICSGQVVLSLGTAVKELVENSLDAGATNIDVRLKDHGAELIEVSDNGGGVEEENFEGLTLKHYTSKIQDFSDLIHVETFGFRGEALSSLCALSDVTISTCHKSAKVGTRLVFDHNGKITQKAPYPRQQGTTVSIQQLFHTLPVRHKEFQRNIKKEYAKMVQILQAYCIISKGVRINCTNQVGQGKKSPVVSTTGGPNLKENIGAVFGKKQLQSLIPFVQLPPNEAVCEEYGLKSTDLPEKLYSITGFISRCDHGVGRSTTDRQFFFINQRPCDPAKVVKLVNEVYHLYNKHQYPFIVLNICVDSECVDINVTPDKRQILLQEEKLLLAILKTSLIEMFGSDVNKLNVNQNLLDIVGNVKAPPGDAEKPWVEMSHHSETENPSSEGKRVMTLSRLRESFSLHQTESYFQSPKKVKQRHSSSKQLSLDTILSTVRTQKAVLSEDSESCHEMKSKMPVPRKYLRKVDDIDSGFCSTSESDAGYNTPEAGSCVISESVNNPIEEEFCSSEEQHQNEYLKTVGHSEKSLECDIQVLGTEHKLNRVNDCNNQTNLPQEATNSLPRVRRFKNEADDFKAGIHPKVENTRNYMPCVDVLVEVKKKTVPLEFSMKALAERVRKIVQQQQKCTETQNYRRFRAKISPGENKVAEDELRKEISKEMFAKMEIIGQFNLGFIIAKLNSDLFIIDQHATDEKYNFEMLQQHTVLQGQKLIAPQNLNLTAVNETVLIENLEIFRKNGFDFVINENAPVTQRVKLISLPTSKNWTFGPQDIDELIFMLSDCPGVMCRPSRVRQMFASRACRKSVMIGTALNVQEMKKLVTHMGEIEHPWNCPHGRPTMRHIASLDLIASE | 3.1.-.- | null | mismatch repair [GO:0006298]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; somatic hypermutation of immunoglobulin genes [GO:0016446]; somatic recombination of immunoglobulin gene segments [GO:0016447] | cytosol [GO:0005829]; MutLalpha complex [GO:0032389]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; endonuclease activity [GO:0004519]; MutSalpha complex binding [GO:0032407]; single base insertion or deletion binding [GO:0032138]; single-stranded DNA binding [GO:0003697] | PF01119;PF13589;PF08676; | 3.30.230.10;3.30.565.10;3.30.1540.20;3.30.1370.100; | DNA mismatch repair MutL/HexB family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54278}. | 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; Evidence={ECO:0000250|UniProtKB:P54278}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P54278}; | null | null | null | null | FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Involved in B cell growth by positively regulating B cell proliferation and controlling replication efficiency. Controls cell cycle to prevent re-replication and defects in DNA damage-induced G2 checkpoint. Doesn't seem to counteract or control the immunoglobulin gene conversion (Ig GC) and to contribute to guanine/uracil mismatch repair. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (By similarity). {ECO:0000250|UniProtKB:P54278, ECO:0000269|PubMed:23314153}. | Gallus gallus (Chicken) |
F1NSM7 | OC116_CHICK | MRATLFCLCLCLLGTVLPTPVSLPARARGNCPGQHQILLKGCNTKHGFYIFQYIYSHLMQKNQTQVKKEEGDHQGTIHGHWLGKVDGEAPGQGAGSSHVPEDKDSPKTHSHITPASKGEGRALRPGIGDSNSVYPTSTSVEGSGDMGSILLGEIINGEDGLPQSTHPGGPHGDGDGGNGVLVDGAVTAGRERASGSEGAGSEGGSHAPVPDQGQAGTMGTGDSAITSVTDSAITSVTKKEDVHVDTEGIDEFAYIPDVDAVTITRGQDGETHISPEDEVKIFIGRANIQVGENDSSVGSAGATSEANVIPTVVTVRPQGHPEESATMATLHHGDSVTSRPVGHPSVGNSGDGATEIHSGQELEAPSPWESTGGDATVTMAVGVQSGKGRSGQRALGKHSLPATMTTRGGRGTASSGLTTGDCSTAASTPSRKGSHVVSAGQGESGEVGTAGPERQRARVQQEVAPARGVVGGMVVPEGHRARVQQEVAPARGVVGGMVVPEGHRARTQPEVASAPSTVGKAAPERHRNRAQQEVAPVPSMVVETVAPERHRARVRPESARLGQAARPEVAPAPSTGGRIVAPGGHRARVWPGAAPAPGVVGVARPAPSKAYNGDKRVAIGKSTDVPRDPWVWGSAHPQAQHTRGSTVAGGFAHLHRGQRLGGLTEMEHSRQVEQVRHADRLRLHERAVYGLSGVGGPLQPPAVHTDPWSADSSQSSEGRWGSHSDSHEEDGEVRGYPYGRQSL | null | null | biomineral tissue development [GO:0031214]; shell calcification [GO:0031215] | extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | extracellular matrix protein binding [GO:1990430] | null | null | Osteoregulin family | PTM: Asn-62 is fully glycosylated, whereas only less than 10% of Asn-293 seem to be glycosylated. {ECO:0000269|PubMed:12225802}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10551857}. Note=Synthesized and secreted by the granular epithelial cells of the uterus and incorporated into the eggshell matrix. {ECO:0000269|PubMed:10551857}. | null | null | null | null | null | FUNCTION: Major component of the eggshell matrix. May play an important role in the regulation of calcite growth during eggshell calcification. May also regulate the mineralization process in developing and growing bones. {ECO:0000269|PubMed:12225802, ECO:0000303|PubMed:10551857, ECO:0000303|PubMed:20665709}. | Gallus gallus (Chicken) |
F1NUK7 | FLRT3_CHICK | MITVPWSVFLIWTKIGLLLDMAPYSVAAKPCPSVCRCDVGFIYCNDRDLTSIPTGIPEDATNLFLQNNQINNAGIPSELKNLRRVERIFLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSQIPYLEELHLDDNSVSAVSIEDGAFRDNIYLRLLFLSRNHLSTIPWGLPKTIEELRLDDNRISTISELSLQDLTNLKRLVLDGNLLNNHGLGDKVFMNLVNLTELSLVRNSLTAAPVNLPGTNLRKLYLQENHINHVPPNAFSYLRQLYRLDMSNNNLSNLPQGVFDDLDNITQLFLRNNPWHCGCKMKWVRDWLQSLPLKVNVRGLMCQAPEKVRGMAIKDLNAELFDCKDDMSTIQITTAVPNTLYPAQGHWPVSVTKQPDIKTPNLNKNYRTTASPVRKIITIFVKSVSTETIHISWKVALPMTALRLSWLKMGHSPAFGSITETIVTGDRSDYLLTALEPESPYRVCMVPMETSNIYLSDETPECIETETAPLKMYNPTTTLNREQEKEPYKNSSVPLAAIIGGAVALVALALLALVCWYVHRNGALFSRHCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFQMIPITNDQVSKEEFVIHTIFPPNGMNLYKNSHSESSSNRSYRDSGIPDSDHSHS | null | null | axon guidance [GO:0007411]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; embryonic morphogenesis [GO:0048598]; fibroblast growth factor receptor signaling pathway [GO:0008543]; head development [GO:0060322]; heart development [GO:0007507]; neuron projection development [GO:0031175]; neuron projection extension [GO:1990138]; positive regulation of synapse assembly [GO:0051965]; proepicardium cell migration involved in pericardium morphogenesis [GO:0003345]; response to axon injury [GO:0048678]; synapse assembly [GO:0007416]; synaptic membrane adhesion [GO:0099560] | axon terminus [GO:0043679]; axonal growth cone [GO:0044295]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synaptic membrane [GO:0097060] | chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104]; protein homodimerization activity [GO:0042803] | PF13855; | 3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BGT1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1}. | null | null | null | null | null | FUNCTION: Modulates the structure and function of the apical ectodermal ridge (AER) that controls embryonic limb development (PubMed:21575622). Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development. Plays a role in cell-cell adhesion via its interaction with latrophilins that are expressed at the surface of adjacent cells. Mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC-5 family members. Plays a role in the regulation of the density of glutamaergic synapses. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning (By similarity). {ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:21575622}. | Gallus gallus (Chicken) |
F1NV61 | CASP7_CHICK | MSGDQHADRSSGEKSNGDQDDTVDAKPDRSSRLSLFAKKKKNGEEEQPKSSLSNQYRIVTPTFQYNMNYKKVGKCIIINNKNFEDKTGMGTRNGTDKDAGDLSKSFRSLGFDVYTYNDRSCEDMQTLLKQAAEENHSDAACFACILLSHGEEGLIYGTDGPMAIKHLTTLFRGDKCKTLIGKPKLFFIQACRGSEFDEGIQTDSGPANDTLETDANPRYKIPVEADFLFAYSTVPGYYSWRNPGRGSWFVQSLCSVLNEHGKQLEIMQILTRVNYVVATNFESQSDDPRFSEKKQIPCVVSMLTKELYF | 3.4.22.60 | null | defense response to bacterium [GO:0042742]; execution phase of apoptosis [GO:0097194]; lymphocyte apoptotic process [GO:0070227]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of plasma membrane repair [GO:1905686]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | aspartic-type endopeptidase activity [GO:0004190]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; RNA binding [GO:0003723] | PF00656; | 3.40.50.1460; | Peptidase C14A family | PTM: Cleavage by different proteases, such as granzyme B (GZMB), caspase-1 (CASP1), caspase-8 (CASP8) or caspase-9 (CASP9) generate the two active subunits. Its involvement in different programmed cell death processes is probably specified by the protease that activates CASP7 (By similarity). Cleaved and activated by initiator caspases (CASP8 and/or CASP9), leading to execution phase of apoptosis (By similarity). Cleavage and maturation by GZMB regulates granzyme-mediated programmed cell death (By similarity). Cleaved and activated by CASP1 in response to bacterial infection (By similarity). {ECO:0000250|UniProtKB:P55210, ECO:0000250|UniProtKB:P97864}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55210}. Nucleus {ECO:0000250|UniProtKB:P55210}. Secreted, extracellular space {ECO:0000250|UniProtKB:P97864}. Note=Following cleavage and activation by CASP1 or granzyme B (GZMB), secreted into the extracellular milieu by passing through the gasdermin-D (GSDMD) pores or perforin (PRF1) pore, respectively. {ECO:0000250|UniProtKB:P97864}. | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60; Evidence={ECO:0000250|UniProtKB:P97864}; | null | null | null | null | FUNCTION: Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins (PubMed:14583630). Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (By similarity). Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (By similarity). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8 and/or CASP9), mediates execution of apoptosis by catalyzing cleavage of proteins (PubMed:14583630). Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins (By similarity). Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair (By similarity). {ECO:0000250|UniProtKB:P97864, ECO:0000269|PubMed:14583630}. | Gallus gallus (Chicken) |
F1NWE3 | PTPRS_CHICK | MRILPSPGMPALLSLVSLLSVLLMGCVAESPPVFIKKPVDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIEFDESAGAVLRIQPLRTPRDENIYECVAQNPHGEVTVHAKLTVLREDQLPPGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSTSNGRIKQLRSGGLQIESSEETDQGKYECVASNSAGVRYSSPANLYVRELREVRRVAPRFSILPVSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPKAPGTPVVTETTATSITITWDSGNPDPVSYYVIEYKSKSQDGPYQIKEDITTTRYSIGGLSPNSEYEIWVSAVNSIGQGPPSESVVTRTGEQAPASAPRNVQGRMLSSTTMIIQWEEPVEPNGQIRGYRVYYTMEPDQPVSNWQKHNVDDSLLTTVGSLLEDETYTVRVLAFTSVGDGPLSDPIQVKTQQGVPGQPMNFRAEAKTETSIVLSWSPPRQEIIVKYELLFKEGDHGREVPRNFEPTTSFTVEGLKPNTEYVFRLAARSALGLGAFTPEVRERTLQSILPKNFKVKMVTKTSVLLSWEFPENYNSPTPYKIQYNGLNVDVDGRTTKKLITNLKPHTFYNFVLMNRGNSMGGLQQNVAAWTAANMLSRKPEVTHKPDADGNVVVILPDVKSSVAVQAYYIVVVPLRKSRGGQFLNPLGSPEEMDLEELIQDIARLRRRSLRHSRQLDFPKPYIAARFRSLPNHFVLGDMKHYDNFENRALEPGQRYVIFILAVLQEPEATFAASPFSDPIQLDNPDPQPIIDGEEGLIWVIGPVLAVVFIICIVIAILLYKNKRKDSEPRTKCLLNNAEITPHHPKDPVEMRRINFQTPDSGLSSPLSDPEFDFESMLSHPPIPVSELAEHTEHLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILLPIEGIVGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEEKSRIKCDQYWPGRGTDTYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVACGNTEVPARNLYTYIQKLAQIEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGSFDHYAT | 3.1.3.48 | null | negative regulation of axon extension [GO:0030517]; negative regulation of axon regeneration [GO:0048681]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of dendritic spine development [GO:0061000]; peptidyl-tyrosine dephosphorylation [GO:0035335]; synaptic membrane adhesion [GO:0099560] | axon [GO:0030424]; growth cone [GO:0030426]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; receptor complex [GO:0043235]; synaptic vesicle membrane [GO:0030672] | heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF07679;PF13927;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | PTM: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17178832, ECO:0000305|PubMed:17967490}; Single-pass type I membrane protein {ECO:0000305|PubMed:17967490}. Cell projection, axon {ECO:0000269|PubMed:7600997}. Perikaryon {ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q64605}. Postsynaptic density {ECO:0000250|UniProtKB:Q64605}. Cell projection, neuron projection {ECO:0000250|UniProtKB:B0V2N1}. Cell projection, growth cone {ECO:0000250|UniProtKB:B0V2N1}. Note=Detected along neurites and at axon growth cones. {ECO:0000269|PubMed:7600997}. | 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:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans (PubMed:11865065, PubMed:17178832). Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth (By similarity). Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection (PubMed:17967490). Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase (PubMed:17967490). Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (PubMed:17967490). Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta (By similarity). {ECO:0000250|UniProtKB:B0V2N1, ECO:0000269|PubMed:11865065, ECO:0000269|PubMed:17178832, ECO:0000269|PubMed:17967490}. | Gallus gallus (Chicken) |
F1NY98 | DSCAM_CHICK | MWMLAVALLHSISHGILTENFLSHHAFPSLLLSLHFSHPSVFSEDLHASLYFVNASLQEVVFASTTGTLVPCPAAGIPPVTLRWYLATGEEIYDVPGIRHVHPNGTLQIFPFPPSSFNNLIHDNTYYCTAENPSGKIRSQDVHIKAVLREPYTVRVEDQKAMRGNVAVFKCIIPSSVEAYITVVSWEKDTVSLVSGPRFLITSTGALYILDVQNEDGLYNYRCITRHRYTGETRQSNSARLFVSDPANSAPSILDGFDHRKAMAGQRVELPCKASGHPTPKYRWLKDNIPWEPDSRFRQTVTGLLIENTRPSDSGNYVCEVWNNYGTAEMIGRLYVKQPLKATISPRKVKSSVGSQVSLSCSVTGTEDQELSWYRNGEIINPGNNVRITGINRENLIMDGMAKSDGGAYQCFVRKDKMSAQDYVQVILEDGTPKIISAFSEKVVSPGEPVSLMCNVKGTPLPTITWTLDEDPIVKDGSHRISQIITSEGNVVSYLNISNTQVRDGGVYRCTANNSAGVVLYQARINVRGPASIRPMKNITAIAGRDTYIHCRVIGYPYYSIKWYKNSNLLPFNHRQVAFENNGTLKLSDVQKEVDEGEYTCNVLVQPQLSTSQSVHVTVKVPPFIQPFEFPRFSIGQRVFIPCVVVSGDLPITITWQKDGRPIPASLGVTIDNIDFTSSLRISNLSLMHNGNYTCIARNDAAAVEHQSQLIVRVPPRFVVQPSDQDGIYGKAVILNCSAEGYPVPTIVWKYSKGAGVPQFQPIALNGRIQLLTNGSLLIKHVLEEDSGYYLCKVSNDVGADVSKSMYLTVKIPAMITSYPNTTLATQGQKKEMSCTAHGEKPIIVRWEKEDRIINPEMSRYLVSTKEVGDEVISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQEPPDPPEIEIREVRARSIALRWTMGFDGNSPITGYDIECKNKSDSWDSVQRTKDVSPQLNQATIIDLHPSSTYNIRMYAKNRIGKSEASNELTITTDEAAPDGPPQDVQLEPISSQSIRVTWKAPKKHLQNGIIRGYQIGYREYSAGGNFQFNIISIDTTGDSEVYTLNNLKKFTQYGMVVQACNRAGIGPSSQEIITTTLEDVPSCPPGNVQATATSPETISISWSTLAKETLNGILQGFRVIYWANLLDGELGEIRNVTTTQPSLELDGLEKYTNYSIQVLAFTRAGDGVRSEQIFTRTKEDVPGPPAGVKAAASSASTVFVSWLPPLKLNGIIRKYTVFCSHPYPTVISEFEASPDSFSYRIPNLSRNRQYSVWVVAVTAAGRGNSSEIITVEPLAKAPARILTFSGTVTTPWMKDIVLPCKAVGDPAPTVKWMKDSNGTPSLVMIDGRRSIFSNGSFVIRTVKAEDSGYYSCVASNNWGSDEIILNLQVQVPPDQPRLTVSKTTSSSITLSWIPGDNGGSSIRGYILQYSEDNSEQWGSFPISPSERSYRLETLKCGTWYKFTLTAQNGVGPGRISEIIEAKTLGKEPQFSKEQELFASINTTRVRLNLIGWNDGGCPITSFTLEYRPFGTTVWTTAQRTSLSKSYILYDLQEATWYELQMRVCNSAGCAEKQAKFATLNYDGSTIPPLIKSVVQSEEGLATNEGLKMLVTISCILVGVLLLFVMLLIVRRRRREQRLKRLRDAKSLAEMLMSKNTRTSDTLNKQQQTLRMHIDIPRAQLLIEERDTMETIDDRSTVLLTDADFGETSKQKSLTVTHTVHYQSVSQATGPLVDVSDARPGTNPTTRRSAKTGPTARNRYASQWTLNRPHPTISAHTLTTDWRLPTPRPAGSVDKESDSYSVSPSQDTDRARSSMVSTESASSTYEELARAYEHAKMEEQLRHAKFTITECFISDTSSEQLTAGTNDYTDSLTSSTPSESGICRFTASPPKPQDGGRVMNMAVPKAHRPGDLVHLPPYLRMDFLLNRGAQGASRDLGLGQACLEPQKSRTLKRPTVLEPIPMEASSTREAQSWQPGAVATLPQREGAELGQAAKMSSSQESLLDSRGHLKGNNPYAKSYTLV | null | null | axon guidance [GO:0007411]; camera-type eye photoreceptor cell differentiation [GO:0060219]; dendrite morphogenesis [GO:0048813]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; locomotory behavior [GO:0007626]; negative regulation of cell adhesion [GO:0007162]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of phosphorylation [GO:0042327]; post-embryonic retina morphogenesis in camera-type eye [GO:0060060]; retina layer formation [GO:0010842]; synapse assembly [GO:0007416] | dendrite [GO:0030425]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202] | cell-cell adhesion mediator activity [GO:0098632]; netrin receptor binding [GO:1990890]; protein tyrosine kinase binding [GO:1990782] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERC8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, axon {ECO:0000250|UniProtKB:Q9ERC8}. Synapse {ECO:0000269|PubMed:18216854}. Note=Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. {ECO:0000250|UniProtKB:Q9ERC8}. | null | null | null | null | null | FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (PubMed:18216854). {ECO:0000250|UniProtKB:O60469, ECO:0000250|UniProtKB:Q8VHZ8, ECO:0000269|PubMed:18216854}. | Gallus gallus (Chicken) |
F1P963 | 8ODP_CANLF | MGTSRLYTLVLVLQPERVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELREESGLTVDTLHKVGQIMFEFVGEPELMDVHIFCTDSVQGTPVESDEMRPQWFQLDQIPFTDMWPDDSYWFPLLLQKKKFHGYFRFQGPNTILDYTLREVDKL | 3.6.1.-; 3.6.1.56 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q7ZWC3}; Note=Binds 2 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q7ZWC3}; | DNA protection [GO:0042262]; purine nucleoside catabolic process [GO:0006152] | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; nuclear membrane [GO:0031965] | 2-hydroxy-ATP hydrolase activity [GO:0106377]; 2-hydroxy-dATP hydrolase activity [GO:0106378]; 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; dATP diphosphatase activity [GO:0008828]; metal ion binding [GO:0046872]; N6-methyl-(d)ATP hydrolase activity [GO:0106431]; O6-methyl-dGTP hydrolase activity [GO:0106433]; RNA binding [GO:0003723] | PF00293; | 3.90.79.10; | Nudix hydrolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}. | CATALYTIC ACTIVITY: Reaction=2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+); Xref=Rhea:RHEA:31583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63212, ChEBI:CHEBI:77897; EC=3.6.1.56; Evidence={ECO:0000250|UniProtKB:P36639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31584; Evidence={ECO:0000250|UniProtKB:P36639}; CATALYTIC ACTIVITY: Reaction=2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+); Xref=Rhea:RHEA:67392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:71395, ChEBI:CHEBI:172878; Evidence={ECO:0000250|UniProtKB:P36639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67393; Evidence={ECO:0000250|UniProtKB:P36639}; CATALYTIC ACTIVITY: Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+); Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; Evidence={ECO:0000269|PubMed:29281266, ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:32144205}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31576; Evidence={ECO:0000305|PubMed:29281266}; CATALYTIC ACTIVITY: Reaction=8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+); Xref=Rhea:RHEA:65396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:71361, ChEBI:CHEBI:172871; Evidence={ECO:0000250|UniProtKB:P36639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65397; Evidence={ECO:0000250|UniProtKB:P36639}; CATALYTIC ACTIVITY: Reaction=H2O + O(6)-methyl-dGTP = diphosphate + H(+) + O(6)-methyl-dGMP; Xref=Rhea:RHEA:67600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:169974, ChEBI:CHEBI:169975; Evidence={ECO:0000269|PubMed:30304478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67601; Evidence={ECO:0000305|PubMed:30304478}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-methyl-dATP = diphosphate + H(+) + N(6)-methyl-dAMP; Xref=Rhea:RHEA:67604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:169976, ChEBI:CHEBI:172872; Evidence={ECO:0000269|PubMed:32144205}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67605; Evidence={ECO:0000305|PubMed:32144205}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-methyl-ATP = diphosphate + H(+) + N(6)-methyl-AMP; Xref=Rhea:RHEA:67608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:144842, ChEBI:CHEBI:172873; Evidence={ECO:0000250|UniProtKB:P36639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67609; Evidence={ECO:0000250|UniProtKB:P36639}; | null | null | null | null | FUNCTION: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool (PubMed:29281266, PubMed:30304478, PubMed:32144205). Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (By similarity). Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP (PubMed:29281266, PubMed:30304478, PubMed:32144205). Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A (PubMed:29281266, PubMed:30304478, PubMed:32144205). Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA (PubMed:30304478, PubMed:32144205). Through this antimutagenic activity protects cells from oxidative stress (PubMed:29281266, PubMed:30304478, PubMed:32144205). {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:29281266, ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:32144205}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PAA9 | CADH1_CANLF | MGPRYGGAPALLLPLLLLLQVSSGLCQEPEPCRPGFGADSYTFTVPRRHLERGRVLGRVSFEGCTGLPRTAYVSDDTRFKVGTDGVITVKRPLQLHKPEISFLVHAWDSSRRKLSTRVRLKAATHHHHHHHDAPSKTQTEVLTFPSSQHGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNRDKEIKVFYSITGQGADAPPVGVFIIERETGWLKVTEPLDREQIAKYILYSHAVSSNGNAVEDPMEIVITVTDQNDNKPEFTQAVFQGSVTEGALPGTSVMQVTATDADDDVNTYNAAIAYSILTQDPLLPSSMMFTINKDTGVISVLTTGLDREGVPMYTLVVQAADLQGEGLTTTATAVITVTDINDNPPIFNPTTYQGRVPENKANVEIAVLKVTDADVPDTPAWRAVYTILNNNNDQFVVTTDPVTNDGILKTTKGLDFEDKQQYVLYVTVVNVTPFEVILSTSTATVTVDVEDVNEAPIFIPCPKVVSIPEDFGVGQEITSYTAEDPDTYMEQRITYRIWRDAAGWLEVNPESGAIFTRAELDREDFEHVKNSTYEALIIAIDNGSPVATGTGTLLLVLSDVNDNGPIPEPRNMDFCQKNPQPHVINIIDPDLPPNTSPFTAELTHGASVNWTIEYNDPARESLILKPKKTLELGDYKINLKLTDNQNKDQVTTLDVFVCDCEGVVNSCKRTAPYAEAGLQVPAILGILGGILALLILILLLLLFVRRRRVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLLSVPQYRPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; regulation of gene expression [GO:0010468]; synapse assembly [GO:0007416] | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; catenin complex [GO:0016342]; cell-cell junction [GO:0005911]; endosome [GO:0005768]; flotillin complex [GO:0016600]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By similarity). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (By similarity). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (By similarity). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (By similarity). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (By similarity). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:P12830}.; PTM: N-glycosylation at Asn-639 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12830}.; PTM: Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-757 (By similarity). {ECO:0000250}.; PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Thr-287 and Thr-511 are O-mannosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3. {ECO:0000250|UniProtKB:P09803}. | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P12830}. Cell membrane {ECO:0000250|UniProtKB:P12830}; Single-pass type I membrane protein {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000250|UniProtKB:P09803}. Cell junction {ECO:0000250|UniProtKB:Q90Z37}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250|UniProtKB:P12830}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000250|UniProtKB:P12830}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PBJ0 | RPGF2_CANLF | MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQAQPPPPQPQPQHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHEERRQRHSVSIVETNLGVGRMERRTMMEPDQYSLGSYAPMAESRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSVTSVTTEETKPVPMPAHVAVTSSTAKGLIVRKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARPTDTAAPSPIQQPHGHPASGRPVNKPQWHKPNECDPRLAPYQSQGFSTEEDEDEQVSAV | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; blood vessel development [GO:0001568]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; cAMP-mediated signaling [GO:0019933]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of endothelial barrier [GO:0061028]; forebrain neuron development [GO:0021884]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of melanin biosynthetic process [GO:0048022]; nerve growth factor signaling pathway [GO:0038180]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein binding [GO:0032092]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of vasculogenesis [GO:2001214]; Rap protein signal transduction [GO:0032486]; Ras protein signal transduction [GO:0007265]; regulation of cell junction assembly [GO:1901888]; ventricular system development [GO:0021591] | apical plasma membrane [GO:0016324]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; late endosome [GO:0005770]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | beta-1 adrenergic receptor binding [GO:0031697]; cAMP binding [GO:0030552]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; PDZ domain binding [GO:0030165]; WW domain binding [GO:0050699] | PF00595;PF00788;PF00617;PF00618; | 2.30.42.10;2.60.120.10;1.10.840.10;1.20.870.10; | RAPGEF2 family | PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:10873669}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane (By similarity). Colocalized with CTNNB1 and TJP1 at cell-cell contacts. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PJP5 | STT3A_CANLF | MTKLGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSIYWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDTGKHIKEHDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT | 2.4.99.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P46977}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B9KDD4}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279] | oligosaccharyltransferase III complex [GO:0035000] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; metal ion binding [GO:0046872] | PF02516;PF21436; | 3.40.50.12610; | STT3 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12887896}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P46978}. | CATALYTIC ACTIVITY: Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529, Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805, ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497, ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18; Evidence={ECO:0000250|UniProtKB:P39007}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P46977}. | null | null | FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (PubMed:12887896). {ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:P46977, ECO:0000269|PubMed:12887896}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PLN3 | FTO_CANLF | MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREAGSVPEDLHKEVQEAFLTLHKHGCFFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGASTKYDEAGIAAACQTFLKLNDYLQIETIQALEELACKEKSNIDAVPVCIGPDFPRVGMGSFDGQDELDIKNRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVERSAVAVYSYSCEGPEEESEDDPQLEGRDPDTWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGLPPRFSSTHRVAECSTGTLDYILQRCQLALQNVRDEADNGDVSLKSFEPVVLKQGEEIHNEVEFEWLRQYWFQGNRYRKCTDWWCQPMTQLEGLWKKMEGVTNAVLHEVRREGVPVEQRNEILTAILALLTTRQNLRREWHARCQSRIARTLPVDQKPECRPYWEKDDPSMPLPFDLTDIVSELRGEFGTLPWSA | 1.14.11.-; 1.14.11.53 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9C0B1}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9C0B1}; | DNA dealkylation involved in DNA repair [GO:0006307]; oxidative single-stranded DNA demethylation [GO:0035552]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of multicellular organism growth [GO:0040014]; RNA repair [GO:0042245] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607] | broad specificity oxidative DNA demethylase activity [GO:0035516]; ferrous iron binding [GO:0008198]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; transferase activity [GO:0016740] | PF12934;PF12933; | 2.60.120.590;1.20.58.1470; | Fto family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C0B1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9C0B1}. Cytoplasm {ECO:0000250|UniProtKB:Q9C0B1}. Note=Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'-O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)-methyladenine from tRNAs and internal m6A in mRNAs. In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)-methyladenine from tRNAs. {ECO:0000250|UniProtKB:Q9C0B1}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57896, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; Evidence={ECO:0000250|UniProtKB:Q9C0B1}; 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:Q9C0B1}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyladenosine in U6 snRNA + O2 = adenosine in U6 snRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57900, Rhea:RHEA-COMP:13573, Rhea:RHEA-COMP:13574, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; Evidence={ECO:0000250|UniProtKB:Q9C0B1}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in U6 snRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in U6 snRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57904, Rhea:RHEA-COMP:15030, Rhea:RHEA-COMP:15031, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; Evidence={ECO:0000250|UniProtKB:Q9C0B1}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(1)-methyladenosine in tRNA + O2 = an adenosine in tRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:54576, Rhea:RHEA-COMP:10242, Rhea:RHEA-COMP:12312, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; Evidence={ECO:0000250|UniProtKB:Q9C0B1}; | null | null | null | null | FUNCTION: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA. Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping. Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Ability to repair alkylated DNA and RNA is however unsure in vivo. Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation. Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells. Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs. Plays an oncogenic role in a number of acute myeloid leukemias by enhancing leukemic oncogene-mediated cell transformation: acts by mediating m6A demethylation of target transcripts such as MYC, CEBPA, ASB2 and RARA, leading to promote their expression. {ECO:0000250|UniProtKB:Q8BGW1, ECO:0000250|UniProtKB:Q9C0B1}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PRN2 | MYO1D_CANLF | MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKALNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFKVVADAMKVIGFKPEETQTVYKILAAILHLGNLKFMVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTIHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDEMFLEALNSKLGKHGHFSSRKLCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLLYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIEHCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLIRIVLFLQKVWRGTLARMRYKRTKAALTIIRYYRHYKVKSYIQEVARRFHGVKTMKDHGKHVKWPTPPKVLRRFEEALQAIFNRWRASQLIKSLPASDLPQVRAKVAAMEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPEPDFTKNRSGFILSVPGN | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; early endosome to recycling endosome transport [GO:0061502]; endocytosis [GO:0006897]; protein transport [GO:0015031]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; axon [GO:0030424]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome [GO:0005768]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; myosin complex [GO:0016459]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; protein domain specific binding [GO:0019904] | PF00063;PF06017; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63357}. Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63357}. Early endosome {ECO:0000269|PubMed:11208135}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11208135}. Note=Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane (PubMed:11208135). Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles (By similarity). {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}. | null | null | null | null | null | FUNCTION: Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (PubMed:11208135). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PTE3 | RAB13_CANLF | MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDSFNNTYISTIGIDFKIRTVDVEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQAIKLAREHGIRFFETSAKSSTNVDEAFSSLARDILLKSGGRRSGNSHKAPGTDLKPCDKKNTSKCSLG | null | null | bicellular tight junction assembly [GO:0070830]; cellular response to insulin stimulus [GO:0032869]; cortical actin cytoskeleton organization [GO:0030866]; endocytic recycling [GO:0032456]; endothelial cell chemotaxis [GO:0035767]; establishment of Sertoli cell barrier [GO:0097368]; Golgi vesicle fusion to target membrane [GO:0048210]; neuron projection development [GO:0031175]; protein kinase A signaling [GO:0010737]; protein localization to cell leading edge [GO:1902463]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; regulation of exocytosis [GO:0017157]; trans-Golgi network to recycling endosome transport [GO:0044795]; vesicle docking involved in exocytosis [GO:0006904] | bicellular tight junction [GO:0005923]; cytoplasmic vesicle [GO:0031410]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; insulin-responsive compartment [GO:0032593]; lamellipodium [GO:0030027]; lateral plasma membrane [GO:0016328]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle [GO:0008021]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-46 and Lys-58; impairing the recruitment of guanosine diphosphate (GDP) dissociation inhibitor 1/GDI1. {ECO:0000250|UniProtKB:P51153}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18094055}; Lipid-anchor {ECO:0000269|PubMed:18094055}; Cytoplasmic side {ECO:0000269|PubMed:18094055}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome membrane {ECO:0000269|PubMed:18094055}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells. {ECO:0000250|UniProtKB:P51153, ECO:0000250|UniProtKB:Q9DD03}. | null | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis. {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:18779367}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1PZQ5 | CCD66_CANLF | MGSKNKIAKCPIRTKQTGYILKSTQNTCIRSGKLLQKKRMGSETSLAKGEKSSMIFSPTKDLCKQYVDKDCLYVQKEISPATPTIQKTRNTINTSVVAKQKHCKKHITAENTKSGLVCLTQDQLQQILMTVNQGNKSISAIENGKEETSQDSLHLNNTSNQPKDENIMGFQKNEALSSVLDENKSTLNKNQETSKQYEQKIAIENVWKPADIFSTLGERERDRSLLEAKKAQWKKELDEQVALKKKEKEASEKWNNPWKKFESDKIVWEKFQTLGQSKTSLSSSNILSQSPSQITVVQADDYPLCRASQILEETVPLERPLSTVKQEQQRKWIEDLNKQIEDDRQRKIEEKITSSKGEEHDRWAMHFDSLKNYPASQSQLSSRSIHNQPEYFCVSPDTQELSDISNVYTPTTGSQVEPSEEEHIAKPVRDMAMANSQKTNFLRSMTALLDPAQIEERDRRRQKQLEHQKAITAQVEEKRRKKQLEEQQRKKEEQEEERRLAREREEMQKQYEEDILKQKQKEEIMTLKTNELFQTMQRAQELAQRLKQEQRIRELAQKGHDTSGLIKNLGGYGLDDVSGKMNTCINSTTSPKKDTAVQTDDLNTGMFTIAESCCGSIIEREILNCSSPEIPAEFNDQFKKDKQELINQDKAANLEKENSWYNDQYEFARTEKKHMKKCPKRPDWNINKPLKRYIPASEKYPKQLQKQREEKKVRRQMELLNLVERNNPGHLSQNRGTSPVLPSPQEAEARFRWHLIRKEEPLKSDSFSKKKKNRSQSPLELVKNRTQQTQTLKNRENLILGDSQTETSPGASEPSHFIPYVRTNEIYHLDPDAPLSRPLTQDLQYQNPHDCDQEQWQLFESDVRDPLLNPNLVKNRDRQQAILKGLSELRQGLLQKQRELETNLMPLAANQEENFNSSF | null | null | cilium assembly [GO:0060271]; microtubule bundle formation [GO:0001578]; regulation of protein localization to cilium [GO:1903564]; retina homeostasis [GO:0001895] | centriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803] | PF15236; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:A2RUB6}. Cell projection, cilium {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A2RUB6}. Photoreceptor inner segment {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the centrosomes and the spindle microtubules during mitosis (By similarity). Enriched in the inner segment of the photoreceptor (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000269|PubMed:19777273}. | null | null | null | null | null | FUNCTION: Microtubule-binding protein required for ciliogenesis. May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites (By similarity). Plays a role in retina morphogenesis and/or homeostasis (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000269|PubMed:19777273}. | Canis lupus familiaris (Dog) (Canis familiaris) |
F1Q4R9 | MEOX1_DANRE | MEQSASSCMRSPHTGGALWGCVRSPHSGGSGAGIQPYQQAPFALHQKHDFLAYTDFSSSCLVPAPHAYPREDRLYPETHSGYQRTEWQFSPCEPRGRGQEPCQGAAEAVGAEMDSAGGDRLAGAVTGCLEGDYSPQSVPAVDTEKKSSKRKREVTDIQDSSFKADSNCKARKERTAFTKEQLRELEAEFTHHNYLTRLRRYEIAVNLDLTERQVKVWFQNRRMKWKRVKGGQPASPHDLEADELDSAASPSSE | null | null | developmental pigmentation [GO:0048066]; hematopoietic stem cell differentiation [GO:0060218]; hemopoiesis [GO:0030097]; muscle cell development [GO:0055001]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sclerotome development [GO:0061056]; skeletal system development [GO:0001501]; somite development [GO:0061053] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; 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] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P32442}. Cytoplasm {ECO:0000250|UniProtKB:P32442}. Note=Localizes predominantly in the nucleus. {ECO:0000250|UniProtKB:P32442}. | null | null | null | null | null | FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints. Binds specifically to the promoter of target genes and regulates their expression. Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome. Acts by mediating specification of endothelial cells of the endotome within the nascent somite, notably by repressing expression of cxcl12b. {ECO:0000269|PubMed:25119043}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1Q506 | SNXAA_DANRE | MDNTSFEKREFISVWVRDPQVHKEDFWHTYISYEICLHTNSMCFRKKTSCVRRRYSEFVWLRHKLQDNALLIELPKLPPWNPFFNLNNEFHITQRMQGLQQFLEAVLQTPLLLSDSRLHLFLQSQLSIAKMDACAQGHTHYTVAQAIQRCGGEARFPVEEQHQEDSKTCCDSDCDSTTSSGLGCSIEPATLVEQDLSHNERFAHEFQATNPEAELCSSLSSSPHGHSVI | null | null | cilium assembly [GO:0060271]; heart looping [GO:0001947]; intracellular protein transport [GO:0006886]; Kupffer's vesicle development [GO:0070121]; left/right axis specification [GO:0070986]; protein localization to centrosome [GO:0071539]; protein localization to cilium [GO:0061512]; vesicle organization [GO:0016050] | centrosome [GO:0005813]; endosome [GO:0005768]; endosome membrane [GO:0010008] | phosphatidylinositol phosphate binding [GO:1901981] | PF00787; | 3.30.1520.10; | Sorting nexin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. {ECO:0000269|PubMed:21844891}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1Q749 | DKC1_DANRE | MADTESKKEKKRKSKKISDEEVGDIQESGDFLIKPESKVASLDTSQWPLLLKNFDKLNIRTAHYTPLPHGSNPLKRGIHDYVRSGFINLDKPANPSSHEVVAWIKRILRVEKTGHSGTLDPKVTGCLIVCVERATRLVKSQQSAGKEYVGIVRLHNALENEHQLARALECLTGALFQRPPLIAAVKRQLRVRTIYESKLIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVLGEKDNLVTMHDVLDAQWQFDHNKDETYLRRVIFPLEKLLISHKRIVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQDIVVITTKGEAICTAVALMTTAVISTCDHGVVAKIKRVIMERDTYPRKWGLGPKASQKKMMIQKGLLDKHGKPNNSTPSDWKEGYVDYSTTKVKKGGEASAKRKRDESGSEGEAAAAAQDTSKTEEESKKEKKKKKKEKKQKLAEEAAAEAPAEEETEVTESAKKKKKKKKAKETEADSD | 5.4.99.- | null | box H/ACA RNA 3'-end processing [GO:0000495]; definitive hemopoiesis [GO:0060216]; mRNA pseudouridine synthesis [GO:1990481]; rRNA processing [GO:0006364]; rRNA pseudouridine synthesis [GO:0031118]; snRNA pseudouridine synthesis [GO:0031120] | box H/ACA snoRNP complex [GO:0031429]; Cajal body [GO:0015030] | pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723] | PF08068;PF01472;PF16198;PF01509; | 3.30.2350.10;2.30.130.10; | Pseudouridine synthase TruB family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O60832}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P40615}. | CATALYTIC ACTIVITY: Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:O60832}; | null | null | null | null | FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed:32554502). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (By similarity). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity). Required for ribosome biogenesis and telomere maintenance (By similarity). {ECO:0000250|UniProtKB:O60832, ECO:0000269|PubMed:32554502}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1Q7H8 | ZD20A_DANRE | MAPSHAVRCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTIPNVNEQVIYLVVFHAFFFMFMWSYWKTISSKPTNPSKEFCLPKAEKELYEKEERPEAQQDILKRVARELPIYTFTGSGAIRYCDRCQLIKPDRCHHCSTCDKCVLKMDHHCPWVNNCVGFSNYKFFVLFLAYSMLYCVYIAATVLQYFIKFWTNQLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNITQVFGDQKKYWCLPIFSSLGDGYTFPTRLVTVDVEHGNIEHQTIKCTVDGQTNARPLSESQNHLLCNDEGQKDSSMAAIEVCQPVCVTLENES | 2.3.1.-; 2.3.1.225 | null | protein palmitoylation [GO:0018345]; protein targeting to membrane [GO:0006612]; synaptic vesicle maturation [GO:0016188] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; protein-cysteine S-myristoyltransferase activity [GO:0019705]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; protein-cysteine S-stearoyltransferase activity [GO:0140439] | PF01529; | null | DHHC palmitoyltransferase family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; Evidence={ECO:0000250|UniProtKB:Q5W0Z9}; | null | null | null | null | FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains. {ECO:0000250|UniProtKB:Q5W0Z9}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1Q8K0 | RAD54_DANRE | MRRSLAPSQVAKRKQGPDSDDEEDWEPDMEPQCKRDCREKYISPYRKPLTPLTNRPFCADGNEHEAFIRKILSKPFKIPIPNYTGVLGLRALGLRRAGVRKALHDPFEDGALVLYEPPVISAHDLIKADKEKLPVHVVVDPVLSKVLRPHQREGVKFLWDCVTGRRIENSYGCIMADEMGLGKTLQCITLIWTLLKQSPDCKPEIDKVIVVSPSSLVRNWYNEVGKWLGGRVQPVAIDGGSKDEIDSKLVNFISQQGMRIPTPILIISYETFRLHAEVLHKGKVGLVICDEGHRLKNSDNQTYLALNSMNAQRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAQEFKKRFEIPILKGRDADASDKDRAAGEQKLQELISIVNRCLIRRTSDILSKYLPVKIEQVVCCNLTPLQKELYKLFLKQAKPVESLQTGKISVSSLSSITSLKKLCNHPALIYEKCLTGEEGFDGALDLFPQNYSTKAVEPQLSGKMLVLDYILAMTRTTTSDKVVLVSNYTQTLDLFEKLCRNRRYLYVRLDGTMSIKKRAKIVERFNNPSSPEFIFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSTGTIEEKILQRQAHKKALSSCVVDEEQDVERHFSLGELRELFSLNEKTLSDTHDRFRCRRCVNGRQVRPPPDDSDCTCDLSNWHHCADKRGLRDPVLQASWDAAVSFVFHQRSHEDQRGVV | 3.6.4.12 | null | double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; transcription-coupled nucleotide-excision repair [GO:0006283] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787] | PF00271;PF00176; | 3.40.50.300;1.20.120.850;3.40.50.10810; | null | PTM: Phosphorylated. Phosphorylations at Ser-566 and Ser-567 allow efficient removal of RAD51 filaments from DNA. {ECO:0000269|PubMed:30961891}. | null | 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:P32863}; | null | null | null | null | FUNCTION: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks (PubMed:30961891). Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By similarity). {ECO:0000250|UniProtKB:P32863, ECO:0000269|PubMed:30961891}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1Q8X5 | FERM2_DANRE | MALDGIRMPDGCYADGTWELKMHVTDLNRDVSLRVTGEIHIGGVMLKLVEKLDVKKDWSDHALWWEKKKTWLLKTHWTLDKYGIQADARLLFTPQHKLLRLQLPNMKHMRVKVNFSDRVFKAVSDICKTFNIRHPEELSLLRKPRDPKKKKKKLEDAEEETLELEGPLLTPGSGSIYSSPGLYSKTMTPTYDSRDGSPLSPTSAWFGDSPLSEGNPSILAVSQPITSPDILVKMYKPQSLLDKAKINQGWLDSSRSLMEQDVKENEVLLLRFKYHSFFDLNPKYDAIRVNQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMSSDNHMNNSEKEVDEVDAALSDLEITLEGGKTSNTLGDITSIPELADYVKVFKPKKLTLKGYKQYWCTFKDITISCYKSREEAHGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVADGMNEIWLRCDTEKQYAQWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHMNPDPQIIEPITTDINPECLVSPRYLKKYKNKQPGFVRDLISARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFLAKFQGGKKDELIGITYNRLIRMDAGTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEPSLAFICAEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV | null | null | angiogenesis [GO:0001525]; cardiac muscle tissue morphogenesis [GO:0055008]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; cytoskeleton organization [GO:0007010]; integrin-mediated signaling pathway [GO:0007229]; regulation of cell shape [GO:0008360]; Wnt signaling pathway [GO:0016055] | cell cortex [GO:0005938]; cell surface [GO:0009986]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; I band [GO:0031674]; intercalated disc [GO:0014704]; lamellipodium membrane [GO:0031258]; nucleus [GO:0005634]; stress fiber [GO:0001725] | integrin binding [GO:0005178]; lipid binding [GO:0008289] | PF00373;PF18124;PF00169; | 2.30.29.30; | Kindlin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with integrins at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling (By similarity). Required for normal embryonic development, including normal heart morphogenesis and normal angiogenesis. {ECO:0000250, ECO:0000269|PubMed:18174465, ECO:0000269|PubMed:21378273}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QB30 | AMFR_DANRE | MPLLFLERFPWPSLQTYTALSALLLAGTVLSAYSTVRDSEFSSALSEGPQNEELKLENLGNVATGVLLHLITDSLFVWVMVNTACCILMLIGKVIQCIVFGPLRVSEKQHLKDKFWNFIFYKFIFIFGVLNVQRVEEVVLWCLWFSMLIFLHLMVQLCKDRFEYLSFSPTTPMSSHVRVLALLVSVLSCCGGLAVLCALAGHIHGMHTVAFMAAECLLVTVRTGHVIIRYSIHLWDLNHEGTWENKSSYIYYTDFIMELAILSLDLMHHIHMLLFGNIWLSMASLVIFMQLRHLFHEVQRRIRRHKNYLRVIDNMESRFAVATPEELAANNDDCAICWDSMTTARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNIHEGRREREEGQREPLEDNMAAAGAADARAHINQHNHFFHFDGSRIASWLPSFSVEVMHTTNILGIAQANNSQLNGMAHQIQEMFPQVPYHLILQDLQLTRSVEVTTDNILEGRIQVPFPTQSTDRTPIQMNAASEDGAGASSGSEVAAPEAEDFEVRGSRFSKSADERQRMLMQRKEELLLRARRRYLHKKPEDGDAYSVLGADNDDSVPSIEDEDSDSVTLRRRRLAAAAERRILRQEPSPF | 2.3.2.36 | null | endoplasmic reticulum unfolded protein response [GO:0030968]; positive regulation of plant-type hypersensitive response [GO:0034052]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; response to endoplasmic reticulum stress [GO:0034976]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151] | metal ion binding [GO:0046872]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630] | PF02845;PF18442;PF13639; | 1.10.8.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25064675}; Multi-pass membrane protein {ECO:0000255}. Note=Palmitoylation promotes localization to the peripheral endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9UKV5}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; Evidence={ECO:0000269|PubMed:25064675}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:25064675}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins (PubMed:25064675). May participate in the final step of endoplasmic reticulum-associated degradation (ERAD) (PubMed:25064675). Required for proper lipid homeostasis (PubMed:37119330). {ECO:0000269|PubMed:25064675, ECO:0000269|PubMed:37119330}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QBY1 | NIPLB_DANRE | MNGDMPHVPITTLAGIASLTDLLNQLPLPSPLPATTTKSLLYNGRIAEEVSCLLSRRDDALVSQLAHSLNQVSTEHIELKDNLGSDDPEGDVPLLLQTVLSRNPNVFREKSLMQQPMIPSYKMPQNSMHGSPASNYQQTTITPSPPSRYVQTQAGSGSRYMPQQNSPVPSPYAPQSPAGYMQYSHPPSYPQHQPIQQVSVSSPIVPSGMRNIHDNKVSGQVSGNSNHNARHCSSDEYINIVQRLGNDEGDPAMRNTSFPVRSACSPAGSEGTPKVGPRPPLILQSPPPYTSPSDTAPDLLLDSPERKKKQKRLLKEEGGKGAMYGIVSSPSKDSTKLTIKLSRVKSSETEQSAEPVVPVVDHGSDAENEVSCNSLSYHRNPQERLSAGQCLSGEQSAYQQVPVLQNIGALAAKQPGVVSGTPYDEAELDALAEIERIERESAIERERCSKEVQDKDKPLKKRKQDSYPQEPGAAGTAGASGTPGVGGGCNAGNKLVPQEACAASNGSSRPALMVSIDLQQAGRVEGPVDSCPVPATEAQRWTEDGSESTGVLRLKSKTDGEVQRTVDGRPEVIKQRVETTPQKTAVDGRPETPINKHENRREISNKVSSEKRSDLSKHRHDGKAEKIRAEGKGHETSRKHEGRSELSRDCKEERHREKDSDSSKGRRSDTSKSSRVEHNRDKEQEQEKVGDKGLEKGREKELEKGRDKERVKDQEKDQEKGRDKEVEKGRYKERVKDRVKEQEKVRDKEQVKGRDKKRSKDLEKCREKDQDKELEKDREKNQDKELEKGREKDQDKELEKGREKDRDKEMEKAREKDQDKELEKGREKDQDKELEKGQEKDRDKVREKDRDKVRDKDRDKVREKDRDKVREKDRDKLREKDREKIRERDRDKGREKDRDKEQVKTREKDQEKERLKDRDKEREKVRDKGRDRDRDQEKKRNKELTEDKQAPEQRSRPNSPRVKQEPRNGEESKIKPERSVHKNSNNKDEKRGGENKNQLDGHKPQSIDSKTADFPNYLLGGKSSALKNFVIPKLKRDKEGNVMQEVRIELFSEPRVKLEKLDLVEDLNKGAKPVVVLKKLSIDEVQKMISNSRSSKSSRSSHGRFRETDSRLPLCERVKMNKRRRSSTNEKPKYAEVSSDDDSSSSVEIAPKRSKKDRDKTWEYEEKDRRGSGDHRRSFDSRRSSGGRHRERSPEDSDEDSPPPSLSDLARKLKKKEKQKKRKAYEPKLTVDEMMDSSTFKRFTTSVDNILDNLEDVDLTSLDDDEIPQELLLGKHQLSELSSESAKIKAMGIMHKITHDKMVKVQSILEKNIQDGAKLSTLMNHDNDRDDEERLWRDLIMERVTKSADACLTALNIMTSARMPKAVYIEDVIERVVQYTKFHLQNTLYPQYDPVYRVDHHGGGTLSSKAKRAKCSTHKQRVTVMLYNKVCDIISNLSELLEIQLLTDTTILQISSLGITPFFVENVSELQLCAIKLVTAVFSRYEKHRQLILEEIFTSLARLPTSKRNLRNYRLNSSDVDGEPMYIQMVTALVLQLIQCVVNLPSDKDSDEENDRKVDHDVLITNSYETAMRTAQNFLSVFLKKCGSKQGEDDYRPLFENFVQDLLSTVNKPDWPAAELLLSLLGRLLVHQFSNKQTEMALRVASLDYLGTVAARLRKDAVTSKMDQRSINRILGENSGSDEIQQLQKALLNYLDENVETDPFLLFARKFYLAQWYRDTSTETEKAMKSQRDDDSSDGPHHAKDVETTSEILQKAEARKKFLRSVIKTTASKFSSLRVNSDTVDYEDSCLIVRYLASMRPFAQSFDIYLTQILRVLGESAIAVRTKAMKCLSEVVAVDPSILARLDMQRGVHGRLMDNSTSVREAAVELLGRFVLSRPQLTEQYYDMLIERILDTGISVRKRVIKILRDICLEQPTFNKVTEMCVKMIRRVNDEEGIKKLVNETFQKLWFTPTPNHDKEAMTRKILNITDVVAACRDSGYDWFEQLLQNLLKSEEDASYKPARKACAQLVDSLVEHILKYEESLADCENKGLTSNRLVACITTLYLFSKIRPHLMVKHAMTMQPYLTTKCNTQSDFMVICNVAKILELVVPLMDHPSESFLTTIEEDLMKLIIKYGMTVVQHCVSCLGAVVNRVTHNYKFVWSCFNRYYGALSKLKMQHQEDPNSTVLVSNKPALLRSLFTVGALCRHFDFDQEEFKGSNKVVIKDKVLELLLYFTKNDDEEVQTKAIIGLGFLFIQDPGLMFVTEVKNLYNTLLADRKTSVNLKIQVLKNLQTYLQEEDSRMQEADREWNKLSKKEDLKEMGDISSGMSSSIMQLYLKQVLEAFFHTQSSVRHYALNVIALTLNQGLIHPVQCVPYLIAMGTDSEPTMRNKADQQLVEIDKKYTGFIHMKAVAGMKMSYQVQQAIVGSKDTVIRGFRLDESSTALCSHLYTMVRGNRQHRRAFLISLLNLFDDNTKSDVNMLLYIADNLASFPYQTQEEPMFIMHHVDITLSVSGSNLLQSFKESLLKEPRKVEVVKKKKKKKKKKKQKQKRGKKYGSEEEDESSRSSSSSSSSSSSSSDSDSSEEEVIHRRKKPRRTTANSDSDSDLDVEDVDKVMLRLPDNPEPLLDFANASQGILLLLMLKQHLKNLYGFSDSKIQKYSPTESAKIYDKAVNRKANVHFNPRQTLDYLTNSLSNSDLSNDVKRRVVRQYLDFKVLMEHLDPDEEEEEGEASASSHARNKAINALLGGSSPKNNAAESYDDDSEVEEKTPGSSRRSRRTGDSAEASGHRNETVEATDVIALCCPKYKDRPQIARVIQKTSKGYSIHWMAGSYSGTWAEAKKRDGRKLVPWVDTIKESDIIYKKIALTSAHKLSNKVVQTLRSLYAAKEGSSS | null | null | brain development [GO:0007420]; central nervous system development [GO:0007417]; developmental growth [GO:0048589]; digestive tract development [GO:0048565]; embryonic pectoral fin morphogenesis [GO:0035118]; embryonic viscerocranium morphogenesis [GO:0048703]; establishment of mitotic sister chromatid cohesion [GO:0034087]; establishment of protein localization to chromatin [GO:0071169]; heart development [GO:0007507]; heart jogging [GO:0003146]; heart morphogenesis [GO:0003007]; mitotic cohesin loading [GO:0061780]; mitotic sister chromatid cohesion [GO:0007064]; neuron cellular homeostasis [GO:0070050]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of gene expression [GO:0010468]; regulation of hemopoiesis [GO:1903706]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414] | Scc2-Scc4 cohesin loading complex [GO:0090694] | chromatin binding [GO:0003682]; chromatin loop anchoring activity [GO:0140587] | PF12765;PF12830; | 1.25.10.10; | SCC2/Nipped-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6KCD5}. | null | null | null | null | null | FUNCTION: May play a structural role in chromatin. Involved in sister chromatid cohesion, possibly by facilitating the cohesin complex loading (PubMed:22039349). Transcription factor, which may promote cortical neuron migration during brain development by regulating the transcription of crucial genes in this process (By similarity). {ECO:0000250|UniProtKB:Q6KCD5, ECO:0000269|PubMed:22039349}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QC45 | XRP2_DANRE | MGCFFSKKSRRKSPKKDAALPTGDESATGNDLAETNNTALGSNSNQEAPKQYSWDKREKVDPKDFMLTGLKNETVGRLPGKLNGQQFVIQDCENCNIFVLDHSATITIDDCVNCRIVLGPVKGSVFFRDCKDIKCVVACQQFRTRDCKKMDVFLCCATQPIIESSTGMKFGCFQYYYPELAFHFKDAGLSIFNNNWSNIHDFTPVSGETNWSLLPEDAVVLDHVPLPDPESEFKSVRIATEAGRSIVPLTKGSRRTESEESCLFVFFAGDYTTANARKLIDEATAKGFVLIQTKEVSMRPEDVSRVFQNNAESLTEWITKGPVVALELNGDGVVEACRSFANEVFNGTQLFVSESKNTSSRDVDNFFNFADMQMGL | null | null | determination of heart left/right asymmetry [GO:0061371]; heart looping [GO:0001947]; photoreceptor cell development [GO:0042461]; photoreceptor cell maintenance [GO:0045494]; photoreceptor cell outer segment organization [GO:0035845]; post-Golgi vesicle-mediated transport [GO:0006892]; pronephros development [GO:0048793]; protein transport [GO:0015031]; retina development in camera-type eye [GO:0060041]; retina layer formation [GO:0010842] | cilium [GO:0005929]; periciliary membrane compartment [GO:1990075] | GTP binding [GO:0005525]; GTPase activator activity [GO:0005096] | PF07986; | 2.160.20.70;3.30.70.141; | TBCC family | PTM: Myristoylated on Gly-2; which may be required for membrane targeting. {ECO:0000250|UniProtKB:O75695}.; PTM: Palmitoylated on Cys-3; which may be required for plasma membrane targeting. {ECO:0000250|UniProtKB:O75695}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26034134}; Lipid-anchor {ECO:0000250|UniProtKB:O75695}; Cytoplasmic side {ECO:0000250|UniProtKB:O75695}. Cell projection, cilium {ECO:0000250|UniProtKB:O75695}. | null | null | null | null | null | FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane (By similarity). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization (By similarity). In the retina, required for maintenance of rod and cone photoreceptor cells (PubMed:26034134). May have a role in normal retinal localization of the transducins GNB1 and GNAT1, and the rhodopsin kinase GRK1 (PubMed:26034134). {ECO:0000250|UniProtKB:O75695, ECO:0000269|PubMed:26034134}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QCP6 | TAZ_DANRE | MPLEVTWPFPQCPRLGWRISSRVVMGMVGSYSYLWTKYFNSLMVHNQDVLLNLVDERPQDTPLITVCNHQSCMDDPHIWGVLKFRQLWNLNKMRWTPTASDICFTREFHSSFFSRGKCVPVVRGDGVYQKGMDFLLERLNQGEWIHIFPEGRVNMSGEFMRIKWGIGRLIAECSLHPIILPMWHIGMNDVLPNETPYIPRVGQRITVLVGKPFTVRHLVNALRAENTNPTEMRKTVTDYIQDEFRSLKAQAEALHHRLQNHT | 2.3.1.- | null | cardiolipin acyl-chain remodeling [GO:0035965]; cardiolipin metabolic process [GO:0032048]; heart development [GO:0007507]; heart looping [GO:0001947]; inner mitochondrial membrane organization [GO:0007007]; mitophagy [GO:0000423]; positive regulation of heart contraction [GO:0045823] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184] | PF01553; | null | Taffazin family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16635}; Intermembrane side {ECO:0000250|UniProtKB:Q16635}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16635}; Intermembrane side {ECO:0000250|UniProtKB:Q16635}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1-acyl-sn-glycero-3-phosphate = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:67748, ChEBI:CHEBI:57970, ChEBI:CHEBI:58608, ChEBI:CHEBI:64716, ChEBI:CHEBI:64840; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750; Evidence={ECO:0000250|UniProtKB:Q16635}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:67752, ChEBI:CHEBI:72840, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754; Evidence={ECO:0000250|UniProtKB:Q16635}; CATALYTIC ACTIVITY: Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + a cardiolipin; Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:62237, ChEBI:CHEBI:64743; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733; Evidence={ECO:0000250|UniProtKB:Q16635}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:68988, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990; Evidence={ECO:0000250|UniProtKB:Q16635}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:43816, ChEBI:CHEBI:28610, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:74669; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817; Evidence={ECO:0000250|UniProtKB:Q16635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818; Evidence={ECO:0000250|UniProtKB:Q16635}; | null | PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q16635}. | null | null | FUNCTION: Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function (By similarity). Its role in cellular physiology is to improve mitochondrial performance (By similarity). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (By similarity). Catalyzes the transacylation between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor. CoA-independent, it can reshuffle molecular species within a single phospholipid class. Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy (By similarity). Required to ensure progression of spermatocytes through meiosis (By similarity). {ECO:0000250|UniProtKB:Q06510, ECO:0000250|UniProtKB:Q16635, ECO:0000250|UniProtKB:Q91WF0, ECO:0000250|UniProtKB:Q9V6G5}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QCV2 | HDA10_DANRE | MASGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLAQSETNPKRPRLDATNGGPKESSEPASESNPKKTAQDIVWPEPLKRMPASVRTVVVPPPGVELTLPKNCQHSGDISESTAKEVQRIRDKHFHDLTDQNILRSLGNIISVLDRMMRSDEVCNGCVVVSDLSVSVQCALQHALTEPAERVLVVYVGDGELPVKTNDGKVFLVQICTKETEDKCVNRLSLCLREGESLTAGFMQALLGLILPVAYEFNPALVLGIVGETAAKTGLMTVWGHMTCLIQGLARGRTLTLLQGYDKDLLELTVSALSGASISPLGPLRALKPEDVEMMEKQRQRLQERWGLLRCTVSES | 3.5.1.48; 3.5.1.62 | null | homologous recombination [GO:0035825]; macroautophagy [GO:0016236]; negative regulation of transcription by RNA polymerase II [GO:0000122]; polyamine deacetylation [GO:0106047]; regulation of tubulin deacetylation [GO:0090043]; spermidine deacetylation [GO:0106048]; swimming behavior [GO:0036269] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | acetylputrescine deacetylase activity [GO:0047609]; acetylspermidine deacetylase activity [GO:0047611]; deacetylase activity [GO:0019213]; zinc ion binding [GO:0008270] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}. Nucleus {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from the nucleoli. {ECO:0000250|UniProtKB:Q969S8}. | CATALYTIC ACTIVITY: Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine; Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48; Evidence={ECO:0000269|PubMed:28516954}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetylputrescine = acetate + putrescine; Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62; Evidence={ECO:0000269|PubMed:28516954}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetylcadaverine = acetate + cadaverine; Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58384, ChEBI:CHEBI:134408; Evidence={ECO:0000269|PubMed:28516954}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 uM for acetylcadaverine {ECO:0000269|PubMed:28516954}; KM=160 uM for acetylputrescine {ECO:0000269|PubMed:28516954}; KM=130 uM for N(8)-acetylspermidine {ECO:0000269|PubMed:28516954}; KM=180 uM for N(1),N(8)-diacetylspermidine {ECO:0000269|PubMed:28516954}; | null | null | null | FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Has a very weak lysine deacetylase, if any (PubMed:28516954). {ECO:0000269|PubMed:28516954}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QDF8 | FXJ1A_DANRE | MLSMSSMDPWPEGSVGLEEEVVTAAAQAERLDTSTPLQCNTSLDSDNLDDSLTSLQWLQEFSILNASTGQHTSPSSHSHLMGSDAPSSPLAGDPASIGMPLTPGKPTAASFCRVPMFSALPSLVAHGHCPDEVDYKSNPHIKPPYSYATLICMAMQASKKTKITLSCIYKWITDNFCYFRHADPTWQNSIRHNLSLNKCFIKVPRQKDEPGKGGFWKIDPQYAERLLNGAYKKRRLPPVQINPALQHRLRMNAQATGVISRNLSVSPESQQLLKDFEEATSADQNWDPRLAEATMLSCWISGKGTNKRKQPYNHRTGKTPRRSSSPLLVMDEQEDLSSLRGNFDWDALLDSALNGELSLNEGSPLSPTPQDEELMIRGTHISPQEAPVENHVLMETQRSGDEDFDEETFLATAFLQSPWSEVDESNRSDFLGSSTVSIDQLFDLSFGGDLSSKIETLL | null | null | cerebrospinal fluid circulation [GO:0090660]; cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; heart jogging [GO:0003146]; heart looping [GO:0001947]; Kupffer's vesicle development [GO:0070121]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296]; regulation of transcription by RNA polymerase II [GO:0006357]; response to wounding [GO:0009611] | extracellular region [GO:0005576]; nucleus [GO:0005634] | 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] | PF00250; | 1.10.10.10; | FOXJ1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. | null | null | null | null | null | FUNCTION: Key transcription factor required for motile ciliogenesis. Activates genes essential for motile cilia formation and function. Its activity is sufficient for ectopic development of cilia that resemble motile cilia. {ECO:0000269|PubMed:19011629, ECO:0000269|PubMed:19011630, ECO:0000269|PubMed:20937855}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QEB7 | WDR11_DANRE | MASTMIPYTVNIKLAARTLTGTLNLQNKTAVDWGWQGLIAQGCHSSILIIDPNTAQTIQVLERHKANVVKVKWSRENYHHSLSSPYSLRLASADAAGKIIVWDVVSGMAHCEIQEHSKPIQDMDWLWAQDASRDLLLAVHPPNYIVLWNGDTGTKLWKKSYAENILSFSFDPFEPSNLALLTSEGIVFITDFSHSKPPGSGGKKVYIASPHSSPAHSKPAAAQPTGAKKALNKVKVLITNEKPTAEAVTLNDCLQLSYLPSKRNHMLLLYPREILILDLELSQTVGVVAIERSGVPFIQVIPCAQRDALYCLHENGCITLRVCRSTTPSPNETVTDPEQNSQELVYDLRSQCDAIRVTKTVRPYRVVICPVNENKAVLVVSDGRVMLWELKAHASKSSSNLSSGLPPLYSAVNFCGTPLRQNQKCIPDLSLNSMIGHSLIPGVDSPRPLADQKEVHLKFLLTGLLSGLPLPPFSLRMCPPLTTKNINHYQPLLAVGTSNGSVLVYNLTSGLLHKELSVHSCEVRGIEWISLTSFLSFATSVPNNLGLVRNELQHVDLRTGRCFAFRGERGNDEPAIEMIKVSHLKQYLVVVFRDKPLELWDVRTGTLLREMAKNFPTVTALEWSPSHNLKSLKKKQLAAREAMARQTTLADAEQSSVESSVISLLQDAESKSESSQGISAREHFVFTDTDGQVYHITVEGNTVKDGARIPPDGSMGSIACIAWKGDTLVLGDVDGNLNFWDLKARLSRGVPTHRGWVKKIRFAPGKGNQKLLVMYTDGAEVWDTKEVQMVSSIRVGRNVNYRILDIDWCTSDKVVLASDDGCVRVLEMAMKSASYRMDEQDLTDPVWCPYLLLPRAALTLKAFLLLQPWMDTFTMDITQVDYKEKDEIKGLIQEQLNSLSNDIKSVLQDPNLSLLQRCLLVSRLFGDESDLQFWTVASHYIQAFAQSAQSNESVPEGQAAASHLDICHDILCESSFFQGFQLERVRLQEVKRSSYEHTKKCADQLLLLGQTDRAVQLLLETSADNSSYYCDSLKACLVTTITSSGPSQSTIKLVATNMIANGKLAEGVQLLCLIDKAADACRYLQTYGEWTRAAWLAKVRLNAAEGSDVLKRWAEHLCSPQVNQKSKAMLVLLSLGCFQKVGEMLHSMRYFDRAALFIEACLKYGVMETNDDINKLVGAAFVDYAKLLRSIGLKQGAVHWASRAGEAGKQLLEDLSQTEGTGTESSPADDTDNSLVNIE | null | null | cilium assembly [GO:0060271]; head development [GO:0060322]; heart development [GO:0007507]; intracellular protein transport [GO:0006886]; multicellular organism growth [GO:0035264]; neural crest cell migration [GO:0001755]; regulation of smoothened signaling pathway [GO:0008589]; vesicle tethering to Golgi [GO:0099041] | axoneme [GO:0005930]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802] | null | null | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9BZH6}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZH6}. Nucleus {ECO:0000250|UniProtKB:Q9BZH6}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29263200}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9BZH6}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9BZH6}. Note=Shuttles from the cilium to the nucleus in response to Hh signaling. Might be shuttling between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9BZH6}. | null | null | null | null | null | FUNCTION: Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis (PubMed:29263200). Regulates the proteolytic processing of gli3 and cooperates with the transcription factor emx1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production. WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles. {ECO:0000250|UniProtKB:Q9BZH6, ECO:0000269|PubMed:29263200}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QG30 | NSMA5_DANRE | MSLRESPFPNGFLEGLHAVGWGLIFPCFWFLDRLIAVCISTTLERMWRLEQECYLHPLKVVFGSILFFILFVISTPFALLGFILWAPLQAIRRPFSYHKQEQSIPMENRNARWEEMGKISFGFLTANVCLLPDGIARFNNLGHTQKRALIIGKSIVQGVTRPHIRIFVDSPSSCGTVTPSSSLIPQPNASSYGSVDASGELPDAIEVNEITPKPNCNQNSNHQKHPPRSLRTLLRDADIPMEVSALFPPSVDIVCLQEVFDKRAARKLTQALGPLYGHVLYDVGVYACHPAGSCSSFKFFNSGLFLASRFPIMEAEYRCFPNGRGEDALAAKGLLTVKVDIGLQKGEKRMVGFINCTHLHAPEGDGAIRFEQLNMLSKWTSEFQTLNRRDDELPLFDVLCGDFNFDNCSPDDRLEQSHSVFDEYTDPCRAAAGKEKPWVIGTLLEQPTLYDENMRTPDNLQRTLESEDLRKDFISPPVALDGVPLVYPEADQPWIGRRIDYLLYREKSGHRTEVEELTYVTQLAGLTDHIPVGFRLSVSLDSEQN | 3.1.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19429680}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:D6MZJ6}; | ceramide biosynthetic process [GO:0046513]; glycosphingolipid metabolic process [GO:0006687]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966] | metal ion binding [GO:0046872]; phospholipase activity [GO:0004620]; sphingomyelin phosphodiesterase activity [GO:0004767] | PF03372; | 3.60.10.10; | Neutral sphingomyelinase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19429680}; Single-pass type II membrane protein {ECO:0000305|PubMed:19429680}; Intermembrane side {ECO:0000269|PubMed:19429680}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D6MZJ6}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:19429680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000305|PubMed:19429680}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-hexadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72959, ChEBI:CHEBI:78646, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:D6MZJ6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45645; Evidence={ECO:0000250|UniProtKB:D6MZJ6}; | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:19429680}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:19429680}; | null | FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000269|PubMed:19429680}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QGH7 | CTNB1_DANRE | MATQSDLMELEMAMDPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEDDDVDNQVLYEWEQGFNQSFNQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTSGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQDAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDIHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMTWNETGDLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDAMGMDPMMEHEMAGHHPGPDYPVDGLPDLGHTQDLIDGLPPGDSNQLAWFDTDL | null | null | canonical Wnt signaling pathway [GO:0060070]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; convergent extension [GO:0060026]; determination of dorsal/ventral asymmetry [GO:0048262]; dorsal/ventral pattern formation [GO:0009953]; ectoderm development [GO:0007398]; embryonic axis specification [GO:0000578]; glomerular filtration [GO:0003094]; liver development [GO:0001889]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification [GO:2000055] | adherens junction [GO:0005912]; catenin complex [GO:0016342]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; intercalated disc [GO:0014704]; membrane [GO:0016020]; microvillus [GO:0005902]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; zonula adherens [GO:0005915] | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; DNA-binding transcription factor binding [GO:0140297]; protein phosphatase binding [GO:0019903]; transcription coactivator activity [GO:0003713] | PF00514; | 1.25.10.10; | Beta-catenin family | PTM: Phosphorylation by gsk3b promotes ubiquitination and subsequent degradation by the proteasome. {ECO:0000250|UniProtKB:P35222}.; PTM: Ubiquitinated when phosphorylated by gsk3b, leading to its degradation. {ECO:0000250|UniProtKB:P35222}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10456847}. Nucleus {ECO:0000269|PubMed:15494018, ECO:0000269|PubMed:25371059, ECO:0000269|PubMed:26938059, ECO:0000269|PubMed:30467143}. Cell membrane {ECO:0000269|PubMed:15494018, ECO:0000269|PubMed:25371059, ECO:0000269|PubMed:26938059, ECO:0000269|PubMed:30361324, ECO:0000269|PubMed:30467143}. Cell junction {ECO:0000269|PubMed:10456847}. Cell junction, adherens junction {ECO:0000269|PubMed:10456847, ECO:0000269|PubMed:19101534}. Note=Cytoplasmic when it is un-stable (highly phosphorylated). Translocates to the nucleus when it is stabilized (low level of phosphorylation). The majority of beta-catenin is localized to the cell membrane. Localized in the ooplasm during the initial stages of oogenesis (PubMed:10456847). {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:10456847}. | null | null | null | null | null | FUNCTION: Key downstream component of the canonical Wnt signaling pathway (By similarity). In the absence of Wnt, forms a complex with axin1, axin2, apc, csnk1a1 and gsk3b that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of ctnnb1 and its subsequent degradation by the proteasome (By similarity). In the presence of Wnt ligand, ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Plays a key role in dorsoventral patterning: in prospective ventral blastomeres, its down-regulation by axin1 and axin2 leads to inhibit the Wnt signaling pathway, while in prospective dorsal blastomeres, degradation of axin results in stabilization and nuclear translocation of ctnnb1 (PubMed:30467143, PubMed:8562427). {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:30467143, ECO:0000269|PubMed:8562427}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QGZ6 | MELK_DANRE | MPVDSTSELLKHYEVYETIGSGGFAKVKLGRHKLTGEKVAIKIMEKKDLGDDLPRVKIEIEAMKNLSHQHVCRLYHVIETTSKIYMVLEYCPGGELFDYIIAKDRLSEEETRVFFRQIISALAYVHSQGYAHRDLKPENLLIDEDHNLKLIDFGLCAKPKGGLGFELLTCCGSPAYAAPELIQGKAYIGSEADVWSMGVLLYALLCGFLPFDDDNCMVLYRKITRGKYSNPHWLSPSSILLLNQMMQVDPKRRLTVKHLLDHPWVMRGYSTPVEWHSKYPLGHIDEDCITEMAVTFKQSKQRTIQLVSEWKYDQITATYLLLLAKKRQGRPVRLRAECPVIDIVCSPLQDMQLKKSLRFTEDDDGVHPVVLGSMVFPPDCYDDENPWTPLTPKNTHTTNTPRMKLYPETTEKWNEMAYSPVIEHSRPCRQKPERRERTKENKENLAVPGTDGDVFALPAPRTPTSSRKVKSNRTVMTTPNHNNNKSSEVNKGAGSATKEGSRRREVEQQQNGQQGELNILAFSPERRSRSLDLAGCQVDSGQKRKGGKVFGSLERGLDKVITMLTPSKKRGPRDGPRKIKAQYNVTLTNQTNADQVLNQILSILPEKNVDFVQKGYTLKCHTQSDFGKVTMQFELEVCLLQKPEVVGIRRQRLKGDAWVYKHLVEDILSSSSQWSA | 2.7.11.1 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell population proliferation [GO:0008283]; erythrocyte development [GO:0048821]; hemopoiesis [GO:0030097]; intracellular signal transduction [GO:0035556]; neural precursor cell proliferation [GO:0061351]; positive regulation of apoptotic process [GO:0043065]; protein autophosphorylation [GO:0046777]; regulation of heart contraction [GO:0008016] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; lipid binding [GO:0008289]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF02149;PF21594;PF00069; | 3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: Autophosphorylated: autophosphorylation of the T-loop at Thr-169 and Ser-173 is required for activation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {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 involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation (By similarity). Also plays a role in primitive hematopoiesis, possibly by affecting the expression of genes critical for hematopoiesis. {ECO:0000250, ECO:0000269|PubMed:16024803}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QLG5 | ADN1A_DANRE | MFQLPVNNLTRLRKARKKVKRLLSDIGLDYCKEHVEDYKDVDPDDSDDSNESHLDLCTWDPTWTKSQDYRTKQFCCSDCPFASKYFSAYKNHFRNVHREDFESRILLNCSYCTYSGNKRTLETHVRLFHMPHNVMRQGVVGPHGAPVGAKDGMRVDKPMLGDRKELPVYYCKKCTYRDRLYNVVRRHIYREHFQHVATPYLGKNSEKQVNSGEAQANSHGIHCKSCHFTPRSYEALVQHVIEFHERIGHQVTAMIGHTNVIVPRLQTNPIQRGVPITSGVRPQTPQMNRFSMPKVVGLPVGNHFKQSLAGNSVPGQPVRVTLPDKAFVSSAVSHSHSGKHLGGFGVHGAAHLNAQSASFSPSLKSLPLSSSVHAATATLTSLQAKKASANALNTSQTQKWKICTICNELFPESAYSAHFEKEHQAEKVRAMAKYIMKIHNFTSKCLYCNRYLPSDSLLNHMLVHGLSCPHCHSTFHEVEKIVAHNRLAHPNEQGDQPTGSPLTFDLTLQQGNLKNVQLLVTTYNMKETPEAAAAAAAANQLSQNSAMPKPVKVSVRQPDTQSDSLVRNMSQSPVSQKKEVGKTLCPLCFTILKGPISDALAHHLRDSHQVLQTLHPVEKKLTYKCIHCLGVYTSNMTASTITLHLVHCRGVCQTPKGSKPITTGLRSPGAGSLKRELVTPDPSDPKRRKMVDQSRFYPTGFAEKPEEPIVLALDPKGYGDKSYEVRKAFLTAYFNRHPYPSQREVEKLAASLWLWKSDVASHFGNHRRLCDRDFTSRKPVVLLGFNMRLLSQIKHDMSFDDSCLFEVFDDEKSGYSRTSSFRLKSPIGFPADFIGSKQPLNTGQSSQSNCAFKTCPGSSSEPIAIDSDSDSELEVIPNENVSQHTPALRPSIVQSQTKGALLRESLRCERDVRANRSSPRVGPKVLDGSVSSSSPDEATWSGNMSSEESHYIPAGRFEVKGKKVGLLGR | null | null | erythrocyte maturation [GO:0043249]; regulation of gene expression [GO:0010468]; regulation of neurogenesis [GO:0050767]; Wnt signaling pathway involved in dorsal/ventral axis specification [GO:0044332] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF19627;PF00046; | 3.30.160.60;1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation (PubMed:23071114, PubMed:32533114). Positively modulates wnt-beta-catenin/ctnnb1 signaling (PubMed:32533114). Required for embryonic neurogenesis (PubMed:32533114). Required for progression through late erythroid differentiation (PubMed:23071114). {ECO:0000269|PubMed:23071114, ECO:0000269|PubMed:32533114}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QLP1 | DHI2_DANRE | MEDFAVSFWIYIGVMSIFVGGAVKKFLAFNIGAMPSVVVWLGATLLVERLCALCMPAVLARLVLCVCCWLYFTWATPKPSLPVEDKAVFITGCDSGFGNATAKKLDAMGFEVFATVLNLEGEGAKHLRKVCSSRLTLLQVDITQPQQVQQALLDTKAKLGIRDLWGLVNNAGWCVNIGDAELSLMSNYRGCMEVNFFGTVTVTRTFLPLLRQSKGRIVTISSPSGEHPFPCLASYGASKAALNLFINTLRHELDPWGVKVSTILPSAYKTGQSSNAEYWEKQYKSLLQGLSPNLLEEYGEEYLLETKELFQNYAKTANEDLSPVIDTIVEALLSPQPQVRYYAGPGLILMYFICSYLPLSISDRFLQKLFVQKKVMPRALIKQQGLSPNDNNNSIKENMNDSSSNNSNFTKCID | null | null | cortisol metabolic process [GO:0034650]; glucocorticoid metabolic process [GO:0008211]; multicellular organismal response to stress [GO:0033555] | intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | 11-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0070523] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH; Xref=Rhea:RHEA:53116, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346, ChEBI:CHEBI:47787, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:22796344, ECO:0000269|PubMed:23042946, ECO:0000269|PubMed:27927697, ECO:0000269|PubMed:33387577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53117; Evidence={ECO:0000269|PubMed:23042946, ECO:0000305|PubMed:22796344, ECO:0000305|PubMed:27927697, ECO:0000305|PubMed:33387577}; CATALYTIC ACTIVITY: Reaction=cortisol + NAD(+) = cortisone + H(+) + NADH; Xref=Rhea:RHEA:50208, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:22796344, ECO:0000269|PubMed:23042946, ECO:0000269|PubMed:33387577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50209; Evidence={ECO:0000269|PubMed:23042946, ECO:0000305|PubMed:22796344, ECO:0000305|PubMed:33387577}; CATALYTIC ACTIVITY: Reaction=corticosterone + NAD(+) = 11-dehydrocorticosterone + H(+) + NADH; Xref=Rhea:RHEA:42204, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600; Evidence={ECO:0000269|PubMed:22796344}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42205; Evidence={ECO:0000305|PubMed:22796344}; CATALYTIC ACTIVITY: Reaction=11beta,17beta-dihydroxyandrost-4-ene-3-one + NAD(+) = 17beta-hydroxyandrost-4-ene-3,11-dione + H(+) + NADH; Xref=Rhea:RHEA:69368, ChEBI:CHEBI:15378, ChEBI:CHEBI:34133, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:81481; Evidence={ECO:0000269|PubMed:22796344, ECO:0000269|PubMed:27927697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69369; Evidence={ECO:0000305|PubMed:22796344, ECO:0000305|PubMed:27927697}; CATALYTIC ACTIVITY: Reaction=11beta-hydroxyandrost-4-ene-3,17-dione + NAD(+) = androst-4-ene-3,11,17-trione + H(+) + NADH; Xref=Rhea:RHEA:69408, ChEBI:CHEBI:2495, ChEBI:CHEBI:15378, ChEBI:CHEBI:27967, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P80365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69409; Evidence={ECO:0000250|UniProtKB:P80365}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72 nM for cortisol {ECO:0000269|PubMed:22796344}; KM=147 nM for corticosterone {ECO:0000269|PubMed:22796344}; KM=206 nM for 11beta,17beta-dihydroxyandrost-4-ene-3-one {ECO:0000269|PubMed:22796344}; | PATHWAY: Steroid metabolism. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) (PubMed:22796344, PubMed:23042946, PubMed:27927697, PubMed:33387577). Cortisol is the primary glucocorticoid in teleosts and is released to increase glucose bioavailability in order to meet the increased energy demands in response to stress (PubMed:23042946). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, regulating the hypothalamus-pituitary-interrenal (HPI) axis function in adult fish (PubMed:23042946). Decreasing the excess glucocorticoids may be of relevance to brain function and neural proliferation (PubMed:23042946). Plays a key role by catalyzing the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), the major fish androgen, that activates androgen receptor transcriptional activity (PubMed:22796344, PubMed:27927697). Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone (PubMed:27927697). Exerts a dual role in fish by inactivating glucocorticoids and activating androgens (PubMed:22796344, PubMed:27927697). {ECO:0000269|PubMed:22796344, ECO:0000269|PubMed:23042946, ECO:0000269|PubMed:27927697, ECO:0000269|PubMed:33387577, ECO:0000303|PubMed:22796344, ECO:0000303|PubMed:23042946, ECO:0000303|PubMed:27927697}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QLR3 | FXR1_DANRE | MEELTVEVRGSNGAYYKGFVRDVHDDSLSISFENNWQPERQVPFSDVRLPPSADTKKEIGEGEEVEIFSRANEQEPCGWWLAKVRMMKGDFYVIEYAACDATYNEIVTFERLRPVNRNKAVTESTFFRCSVPVPEDLRAACESEQAHKEFKKAVGAIRIVYSPEKSELVVLSLSEATVKRVSLLSDIHLRSIRTKLMLMSRNQEATKHLESTKQLASAFQEEFTVREDLMGLAIGSHGSNIQQARKVPGVTAIELEEETGTFRIYGESTEAVQKARNYLEFLEDSVQIPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNDNKLPRQEGMVPFTFVGTKESISNVQVLLEYHIAYLNEVEQLRLERLQIDEQLRQIGMGFRSVPNRPADKEKGFGPDESSSGSIHTQRSYRGRGRRGPAHTSAYGTNSEHSYTSETDSERKAELSDWSLAADESERNPRPQRDSRRRDLRGRGRGSRGRGASNSISSVLKDPDGNPYSLLDNTETDQTADTDGSESQMNTSRRRRSRRRRTDEDTTVMDGMSESDNASLSENGLVTVADYISRAESQSRQTNPRDTRKSKKDMTRGDFISEHSAAESVSNGPNNADEPSESAKAVVNGVS | null | null | animal organ development [GO:0048513]; dentate gyrus development [GO:0021542]; heart development [GO:0007507]; mRNA destabilization [GO:0061157]; mRNA transport [GO:0051028]; muscle cell development [GO:0055001]; negative regulation of inflammatory response [GO:0050728]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of translation [GO:0017148]; negative regulation of tumor necrosis factor production [GO:0032720]; non-membrane-bounded organelle assembly [GO:0140694]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of translation [GO:0045727]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of filopodium assembly [GO:0051489]; regulation of mRNA stability [GO:0043488]; regulation of neurogenesis [GO:0050767]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of translation at presynapse, modulating synaptic transmission [GO:0099577]; skeletal muscle tissue development [GO:0007519]; somitogenesis [GO:0001756]; spermatid development [GO:0007286] | cytoplasmic stress granule [GO:0010494]; dendritic filopodium [GO:1902737]; dendritic spine neck [GO:0044326]; growth cone [GO:0030426]; intracellular non-membrane-bounded organelle [GO:0043232]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; presynapse [GO:0098793] | molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; translation regulator activity [GO:0045182] | PF05641;PF12235;PF16096;PF16097;PF00013;PF17904;PF18336; | 2.30.30.140;3.30.1370.10; | FMR1 family | PTM: Phosphorylation at Ser-447 by PAK1 promotes its activity. {ECO:0000269|PubMed:20417602}. | SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q61584}. Cytoplasm {ECO:0000250|UniProtKB:Q61584}. Note=Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments. {ECO:0000250|UniProtKB:Q61584}. | null | null | null | null | null | FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as heart and muscle development (PubMed:19648401, PubMed:20417602). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity). {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:19648401, ECO:0000269|PubMed:20417602}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QLY4 | RORAA_DANRE | MMYFVISAMKAQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNAAYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRLQQQQRDHQQQPGEAEPLTPTYGLSTNGLTELHDDLSGYMNGHTPDGTKPDSGVSSFYLDIQPSPDQSGLDINGIKPEPICDFTPGSGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHMETCQYLREELQQMTWQAFLQEEVENYQSKPREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFVRMCRAFDPQNNTVYFDGKYAGPDVFKSLGCDDLISSVFEFGKNLCSMHLSEDEIALFSAFVLMSADRSWLQEKVKVEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCSRHTEKLTAFKAIYPDIVRAHFPPLYKELFGSDFEQSMPVDG | null | null | negative regulation of inflammatory response [GO:0050728]; positive regulation of gene expression [GO:0010628]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; rhythmic process [GO:0048511] | nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; oxysterol binding [GO:0008142]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35398, ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) (By similarity). Required for proper cerebellum development (PubMed:29656859). {ECO:0000250|UniProtKB:P35398, ECO:0000269|PubMed:29656859}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QN48 | FA53B_DANRE | MCVAMVIIHTKTLEKKAVDDVTSEASLQPQEPLTMSQGTALFSCGIMDSGRWADVGSVCGVQQRPVGSSLESLWDSMREAGATGGISGLLRDLSLSEASPASAAPPSKRQCRSLSCSDELGCRSSWRPQGSRVWTTVEKRRCHSGGSVQRGVFNPSGFPAMQRSSSFSLPAHSSHLEPFTHGFPFQAFSECPQTPQTLYRSHEQICPAEASSPESTPELQRRSGQSGLARSRSQPCVHNHQKIGVKRRRPADSHKQRPSLDLLKMTQKLQDFHSLSCPGFSGDDKTLPSSSPALLNDTCERAQNDSSADAPIHQSESSSEDALIHQSDSSSADALIHQSESSRPAGKERECLWAGLCSRRGRDLFQLGGELDIEQIERN | null | null | axon extension [GO:0048675]; fin regeneration [GO:0031101]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein import into nucleus [GO:0006606]; Wnt signaling pathway [GO:0016055] | nucleus [GO:0005634] | null | PF15242; | null | FAM53 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25183871}. | null | null | null | null | null | FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) nuclear localization (PubMed:25183871). Required for appendage regeneration by regulating cell proliferation (PubMed:19014929). {ECO:0000269|PubMed:19014929, ECO:0000269|PubMed:25183871}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QN54 | KIF3B_DANRE | MSKSKSSESVKVVVRCRPMNEKERVANFNRVVSVDVKLGQVAVCNPRGASSHEHPKVFTFDSVYDWNSKQMELYDETFRPLVDSVLFGFNGTIFAYGQTGTGKTYTMEGVRNDPERRGVIPNSFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQARRLELKERPDTGVYVKDLSSFVTKSVREIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSELGPDGENHIRVGKLNLVDLAGSERQTKTGAQGERLKEATKINLSLSALGNVISALVDGRSTHIPYRDSKLTRLLQDSLGGNARTVMVANIGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKEQLEKRSGRKRRRRRRRRVGEGGEEFEDGEDEEDDDDDDEDEEEGVDADKNIADYWHEQQEKLEKERRAIMEDHSLVAEEKQRLLKEKERKMTDLHKEKEASEMLTAKVKAMESKLLVGGKNIVDHTNEQQKVLELKRQEIAEQKRREREMKQEMECRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQSVKSEIQDAQDEHVKYRQELEQTQNELTRELKLKHLIIENFIPMEEKNKIVTRATFDEEDDLWKMTPITRIQNSDHQMMKRPVSAVGYRRPLSQHARMAMLMRPDVRYKAENILLLELDLPSRTTKDYEGPVIAPKVAAALEDALREEDEIQVDASGFHASLGSSPGLSASAAGFSKKPKSGRPKTGKKVSTPTSAHSPLSGSGSPLYPQSRGLVPK | null | null | cilium assembly [GO:0060271]; inner ear development [GO:0048839]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; neuromast development [GO:0048884]; nose development [GO:0043584]; opsin transport [GO:0036372]; photoreceptor cell development [GO:0042461]; photoreceptor cell differentiation [GO:0046530]; photoreceptor cell outer segment organization [GO:0035845]; pronephros development [GO:0048793]; retina development in camera-type eye [GO:0060041]; retina morphogenesis in camera-type eye [GO:0060042]; spindle elongation [GO:0051231] | cilium [GO:0005929]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q61771}. Cell projection, cilium {ECO:0000250|UniProtKB:Q61771}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61771}. | null | null | null | null | null | FUNCTION: Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation. Required for photoreceptor development (PubMed:22308397, PubMed:28855254). {ECO:0000250|UniProtKB:Q61771, ECO:0000269|PubMed:22308397, ECO:0000269|PubMed:28855254}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QNW4 | DRC4_DANRE | MPPKRKSSPKGKTPTVVDGLSTEEMSKEQLEEHIMRLREELDREREERNYFQLERDKIHTFWEITRRHLEENKCELRNRERELEEVEERHQVEIKVYKQKVKHLLYEQQNMLSELKAESIISTKLLQDEHADLEKEQWKDMRSLKLELKQQELSSENVLKRIHLKHDEETTDLRNDFARQVQEIGSKYEKRMQKLRQEEELRRKTEIHEIEERKNTHINMLMKNHEKAFRDIRNYFSDIVYKNLDLITSLKEELKEMKKNEEKRNKEMAEVLEQNKELKESSQKAKEQVAELQKQLANYEKDKSILTRSRARLKMSDREMKELKWELEVLEQRFSKVQLERDELYMKFTKAILEVQQKSGFKNLLLECKLNTLNDTLEKKEAQLSEVLSASNLDPTTLSVVTHKLEEVLESKNHTIKDLQYEVARVCKAHNDLLKTSEAKLRAFGIPVEELCFEPLKSNGQSVGQGPAMFVSSSN | null | null | axoneme assembly [GO:0035082]; cilium movement involved in otolith formation [GO:0003355]; flagellated sperm motility [GO:0030317]; muscle cell development [GO:0055001]; otolith tethering [GO:0035889]; positive regulation of protein localization to cilium [GO:1903566]; positive regulation of smoothened signaling pathway [GO:0045880] | ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; motile cilium [GO:0031514] | microtubule binding [GO:0008017]; small GTPase binding [GO:0031267] | PF13851; | null | DRC4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95995}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:O95995}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q60779}. Golgi apparatus {ECO:0000250|UniProtKB:O95995}. Cell projection, cilium {ECO:0000250|UniProtKB:O95995}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7XJ96}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper slow muscle development and positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway (PubMed:21659505). Required for tether cilia motility which is essential for normal otolith formation and localization in the developing inner ear (PubMed:19043402). {ECO:0000250|UniProtKB:Q7XJ96, ECO:0000269|PubMed:19043402, ECO:0000269|PubMed:21659505}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QQA8 | ZN219_DANRE | MDSPPECMLALSCEPPLSPPSMPSLDHSPQFLPQSPQSTPSSPQTELYAPVSPCPLPEASLQDEEEEDEELSTPPSPTPAVALFPGELELGSPSSESSPPATPLAPFPSFGALEKAISSGQSTTCNDELDLQLFNNESIAVTGGTSSGPGLRFPCHVCGKRFRFQSILSLHARAHSLDRERRASAPYRTTHSKLQQNHESNSMIQNPLSGSFQKSMNEDMVPEEPLQTASSPQFLFEGTTALTPPLTEEAPISTSFSPLGHAQLEDNTPSPAAPAFRCHACKGKFRTASELARHVRILHNPYKCTMCPFSASQEERLAAHLQESHPPEDPPAEAVFPSGAIKAPPETPVPQMSVIPAFRCETCGQRFTQSWFLKGHMRKHKDSLDHKCQVCGRGFKEPWFLKNHMKVHLNKLGLKAGLGNLGPPGADQSKGPASSQVLGALYSNLLLARSMAGGGGSGSRTERSDASAGSSKSSILGYLGLPKDSSNGSCMERLQAVAQVAEMGNGGGRGGDSADGADQAAMWQLVARSLVAAQHNQQQQQQQRSHSLHQHPSSRATVAGEAKNMRAYLGGLGSREELDGSSAPWECPDCGKLFRSLQQVVAHAHVHVQKTQKGQSARGGMSREEDIINRVSGTQATGGAGQRTGENESRQEGKQLPSGVGASGSFHSVISHLSGQNGLRGSSPSSSSPRERVRGTGMKDCPYCGKAFRSSHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRNAMATSPNSPSPSLPSLTGSPREGAKKRRLPSMSQQSSFGRVPGEAPSSRHTQSWTIGLSEKKEGSSASAHHREGDLESQYRGLSGMMGALLPSGLEQSWIGEVTLPKVPKVSRRKPQITSRMVSANGFQDKMTSQEGGFEPLDLSRRPLQDEGGVSQSGSGPSSGSKGGNDILNQCVFCPFRTSSVELMAMHLQVNHTSKSRRKRGAPISSNNHSQKLARPDRDPLALWKFLGVEDGVASPEDWVSARAENGVSPENRETEDNLELASGAMGSFRSRKKKPQMSEHVDEEDEEIDEEENDLEANGSFANVPQNQSRRAQSVSSDLPDDDLPKEEEGVLGE | null | null | notochord development [GO:0030903]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:24155663, ECO:0000305|PubMed:24269816}. | null | null | null | null | null | FUNCTION: Transcriptional regulator (PubMed:24155663, PubMed:24269816). Recognizes and binds to the core DNA sequence motif 5'-GGGGG-3' (PubMed:24155663, PubMed:24269816). Binds to the col2a1a promoter and activates col2a1a expression (PubMed:24155663). Binds to the sncgb promoter and activates sncgb expression, as part of a complex with sox9a (PubMed:24269816). {ECO:0000269|PubMed:24155663, ECO:0000269|PubMed:24269816}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QQC3 | LOL2A_DANRE | MAVSSALCIFSLLVLAQAQSELQQPKIELRLAGDKRKHYEGRLEVFYNNEWGTVCDDDFSIEAAHVACRQLGFLGAVAWSPSAKFGQGEGRIWLDNVHCTGRENSLAACPSNGFGVSDCRHSEDVGVICNQKRIPGHRFINIMNNNVETLEERVEEIRIRPISSHLKRIPITEGYVEVKERGKWRQICDEEWTPLNSRVACGMYGFPGEKNYNNKVYRSLSMRKKKNYWGFSVNCTGNEAHVSSCRLGKALEPKRNGTCGRGLPVVVSCVPGRAFAPSSSIGFRKAYRPEQPLVRLRGGANVGEGRVEVLKNGVWGTVCDDNWNLKAATVVCRELGFGSAKEALTGAKLGQGMGPVHMNEVECSGFEKSLTDCYFNNDALGCSHEEDAAVRCNVPAMGFQKRIRLSGGRNPFEGRVEVLAEKNGSLVWGTVCSENWGIIEAMVVCRQLGLGFASHAFQETWYWAGDANADNVVMSGVRCSGTEMSLPQCLHHGKHINCPKGGGRFAAGVSCSDTAPDLVLNAQLVEQTTYLEDRPMYALQCALEENCLSSTARKNDHSSYRRLLRFSSQIHNVGQSDFRPKLGYHAWTWHECHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDTHCDEGISKRYHCANFGEQGITVGCWDTYRHDIDCQWIDVTDVKPGDYIFQVVINPNYDVAESDYTNNVMKCKCRYDGYRIWTYSCHIGGSRSSDMDEYSGMSNQLNHLR | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040] | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2b for correct expression of Sox2 and for neural differentiation (PubMed:25959397). {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0, ECO:0000269|PubMed:21835952, ECO:0000269|PubMed:25959397}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QQI2 | SPXN1_DANRE | MKDLRTLAAYALALLLLATFVSHSWSAPKGSFQRRNWTPQAMLYLKGTQGRRFVSEDRNEGDLYDTIRLESRSQNTENLSISKAAAFLLNILQQARDEDEPY | null | null | cholesterol homeostasis [GO:0042632]; glucose homeostasis [GO:0042593]; long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; negative regulation of eating behavior [GO:1903999]; negative regulation of heart rate [GO:0010459]; negative regulation of renal sodium excretion [GO:0035814]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of sensory perception of pain [GO:0051930]; triglyceride homeostasis [GO:0070328] | dense core granule [GO:0031045]; extracellular space [GO:0005615]; nucleus [GO:0005634]; transport vesicle [GO:0030133] | neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF15171; | null | Spexin family | null | SUBCELLULAR LOCATION: [Spexin-1]: Secreted {ECO:0000250|UniProtKB:Q9BT56}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9BT56}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q9BT56}. | null | null | null | null | null | FUNCTION: Plays a role in the regulation of food intake and energy metabolism (PubMed:29116147). May also be involved in suppressing the anxiety response by promoting the expression of serotonin-related genes such as fev, tph2 and slc6a4a (PubMed:31474838). {ECO:0000269|PubMed:29116147, ECO:0000269|PubMed:31474838}.; FUNCTION: [Spexin-1]: Acts as a ligand for galanin receptors galr2a and galr2b (PubMed:24517231). Brain administration of the peptide inhibits food consumption and elevates levels of glucose, triacylglycerol and cholesterol in the serum (PubMed:29116147). Likely to control food intake by regulating appetite related genes which includes the negative regulation of the orexigenic factor agrp (PubMed:29116147). By controlling food intake it may act as a satiety factor in energy metabolism (PubMed:29116147). {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:29116147}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QR43 | GLCEB_DANRE | MMRCLAARVHYKTLIVICALLSLLTVLLWNKCTSEKALRFLPRHPQPPPSPKIDSHPQQPQPPEPPPVVGGVRYEEIDCLINDDATIKGRREGSEVYMPFSWMEKYFEVYGKVVQYDGYDRFEFSHSYSKVYAQREQYHPNGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYAIQIAQYGLSHYSKNLTERPPHVEVYDTAEERDSRSSAWTVPKGCSLTRVYDKTRATSVRQFSAPENSEGVSLPLGNTKDFIISFDLKFTSNGSVSVILETTEKGPPFVIHYVTTTQLILLKDRDITYGIGPRTTWTTVTRDLLTDLRKGIGLSNTKAVKATKTMPRRVVKLVVHGTGTIDNITISTTSHMAAFYAASDWLVRNQDERGGWPIMVTRKLGEGFRALEPGWYSAMAQGQAMSTLVRAYLMTKDDTYLKAALRATGPFKLPSEQHGVKAVFMNKYDWYEEYPTIPSSFVLNGFIYSLIGLFDLAQTAGEKLGRDAGQLYSKGMESLKVMLPLYDTGSGTIYDLRHFILGTAPNLARWDYHTTHINQLQLLGTIDNSPIFRDSVKRWKSYLKGGRAKHN | 5.1.3.17 | null | heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06662;PF21174; | null | D-glucuronyl C5-epimerase family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}. | CATALYTIC ACTIVITY: Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n); Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557, ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17; Evidence={ECO:0000269|PubMed:25568314, ECO:0000305|PubMed:16156897}; | null | PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:16156897, ECO:0000305|PubMed:25568314}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305|PubMed:16156897, ECO:0000305|PubMed:25568314}. | null | null | FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains (PubMed:16156897, PubMed:25568314). Plays a role in dorso-ventral axis specification during early development, together with glcea, where it may potentiate signaling via the BMP pathway (PubMed:16156897). {ECO:0000269|PubMed:16156897, ECO:0000269|PubMed:25568314}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QSQ0 | DSC2L_DANRE | MRTPPRPEGLYPSPTVRYTQFMVETGHIQLLQITYPHTHSRFRMYERAHFAACLLALVLFQRAESCDPRPVLVQVPNTVPAGYFITQVTLNGCTAIPVSFTSSDPDFTVNTDGSIVTLRSLVISTKRFSVLVQDNSGLDWRVEIILSCKNEDSQKSGSVAQKRAKRRWRPLPFSVVENASPPFPKDVEMIASDSSVNYTVHYVISGQGVTEEPIGLFQLDQKTGMVRVTGPVDREKNPEFNFIARAFDQNNREVDQFLPITVMVEDVNDNAPEFTGNRFFTVEERCRAGTRVGQVNATDRDQPKTPHSLIKYILLNATDMFSIDQSTGIITAKSNTLDREAQDKVFVGVEIRDMGGAPNGLFNRGTAVISLTDVNDNPPTFKEKLYKGTIKENLANVLVTRIPVEDKDLVNTPNWKAVYEVTKGNENGNFRMETDPKTNEGLLYVVKGLDFEKTPVMNLEVTARNEAPLVGTDAKWQSVPLQLNVEDVDEGPEFNPNIMYLKVKENLPNGTVIGTYKALDPETKNSNGIKYYKLTDPGNWITVVESTGELKVANTIDRESSLVHNDTYNITIKAVDESKKTGNGVVILQIEDVNDNIPVIQRPDLNMCNRGDAVSSVLVEAVDQDKPPYSTPFIFELGAEQEGKWKLKDITDSSVVLQQVEPMPNGMYTVPITVKDLQGTGKEQIVNVRVCSCQREDSGVGICGARSASVSLGNYGILALVLSGLLLLLLCLFLIFFCTTKRDKLQITDDTGTGGILLKSNTEAPGEEVKDGTLLLIPTADVVDGSFQSAVTESKNVNTAPGRYGQQFFQSGGVYNTTTQEFGTDQYYTSGRYDNKIYGNGTLQKFSNTGTLDTWRTNGCYLDRKLAYFGEQEDGRYADDLLKNYGNEGVGSSAGSVGCCSILGEQESMEFLNTLGPKFRPLADICYTTNKTGK | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; convergent extension involved in gastrulation [GO:0060027]; desmosome assembly [GO:0002159]; epiboly involved in gastrulation with mouth forming second [GO:0055113]; heart contraction [GO:0060047]; heart development [GO:0007507]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; sprouting angiogenesis [GO:0002040] | adherens junction [GO:0005912]; catenin complex [GO:0016342]; desmosome [GO:0030057] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:Q02487}. Cell membrane {ECO:0000250|UniProtKB:Q02487}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of intercellular desmosome junctions (PubMed:22235774). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion (PubMed:22235774). Involved in the formation and structural organization of desmosome cell-cell junctions during embryonic development (PubMed:22235774). Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation (PubMed:22235774). Required for the development of desmosomal-rich midlines in the heart (PubMed:17186466). Plays an important role in ventricular contraction and resulting heart stroke volume (PubMed:17186466, PubMed:33784018). {ECO:0000269|PubMed:17186466, ECO:0000269|PubMed:22235774, ECO:0000269|PubMed:33784018}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QU13 | ALPK2_DANRE | MTAKRVDMAAPDNLLFLDSDAVNSSPASVPIEQNEPTHVLDNQTDDSLRSMPDPHTNTALESTGLMPVPCQDETLETHSQHNEGENESSLVSTQHMDHTRLTEMTINDEKSNNWDFDISGVKENDNSTNLNPDLIHHAGTDSVMERNLNDKQTDLNHKDETFGSLMSSEVLLLKENRQQEMSQDTNLHQCSSSESTGIEYSQTANDAISDAMNSEQSPDQPFSIASNDTDKTTSECSVQTCWDTVESAATSKTQPELHDDVKDVMCESFTTSQTLNIDYLSTDISVCLADLPETDSLNILTPASTLLGILGKNNNVLKTADVPINDSEMVQSINKDLASPNADISKTVFTQMDQNLLHVTDHNVKVLESNRADTVVDQYVFSENIGQEVSQASSHDEDLNSSVQSHDQQLSTANSEIEETSSEFHTQTCQDIHEGVIIAEEAMNGHNTLPEMHDIADVTTSQTPIMKDPMIDEPSYLPDLHKADTPNVITTASTLSDTLETDDSIFETADVSVSDCELIQTVTLKTVTTYETLLMMHDVGEDLTCCDFTTSAIEEPETSHPLSLDDLHESNTPNIPPHASALLDSLGMNKNFLETADVPVSDCEVIQTVTFETVTTYETFPVMHDIAEDLTCCDFTTSETPKIEEPETSHSLSLDDLNEANTPNILPHASALLESLGMNNNFLEAADMPVSDREIIHPVNKDLDSSSVEICTVVLTQTDPKEVQDSDLDEKETESNRIDDSIDGMIDTKFSLDVSKLQPVCSNDLSGTVIHSESLFSQSIPDTPQIGEKYKNDLLQVISPPTPVTNEDLGNCSEEIDDACLKFTGTERDVEGDSELWLEPSQFLAGEEDEGAIFDKWGRSCSSSPPTTHPDNTKASDYTWRENISIDHNAEDWELTFPPVERWSSSDSWASALSDWFQAVNTYPEDSFKSASTGSKLGMAIQDNILEQRTSSDNANNDEQTCLSLNLMQPDEPGQALERGLVKSDNTNGTVFKQGDKERLASCLDMDKDTTTMESQMSLLETSTPESHKADNNAVMETFNASLTHEFNAKLHGSLDISGKLLSAKREGNVLVEVTGGKVSQLGLVFEEERQSIFTSPSSSAYTRDKNLTGCVSNEERCHSSDVHLCICPSQSDSHVSSKAGHAEGNGSFLHSNIGNCTVKPYVEENIPQFIMPFAPICTGNTFLHRSFLKEDRSQADLDLPDKKIINKINLKSNKKSSSSDDSSEDNFHTCPDQSLSSSSGDSDDPSITDSGRKPAYSDTCDIGKELSKLLLLTGEHFMVSEDKRIAYVTLDLDESQHFGRFSLPNCEKQSKPDNMPHKTSKTSSDGKMRSKHKEKPDDKQQHGIQASKKQDPQPQSQVKNEGAGCEDCPVAVIETIVITEKIIPKTQGKKKKKHVQHGTPKPENDAPTDVRSESRQKNVNGKAENLELKVASNSLNKPVAQPSGKTDITKKDSAQKVMSVRPKVEPSMAKMDPAGVNATQKSSPIKLKADTFNTAKMENKTCTTDSLSTCLPSMLNDDIKRRRIADDLSRAVPIRTRPQLPAIFRQARKDGEDVTRRAYSEVVKQKNSTPKEVVVPRVVSEIQADPVPADPQNISLWCQFSPIPPEATIKWTKEAAVLSEINKVEKEDGRFTLTIIKACSKDLGFYKCSLIVANISVSTSEYHLTSEVLMELVIPSHDQPAEPRVMEGDEENIQCSPLLFKEDFLSDQYFGKNQPASILTEKVHFGEGMHRKAFRTTLTEGNLPRFRPGHPCVLKVHNSISYGTKNNEELVQKNYSLAVEECHVQNTAREYIKAYNSVAKSAESFGDLPEIIPIYLVHRPSNDIPYATLEEELLGDFVKYSVKDGKEINLMRRDSEAGQKCCAFQHWVYTQTEGNLLVTDMQGVGMKLTDVGIATCKKGYKGFRGNCATSFIDQFKALHQCNRYCELLGLVSLQPKPKRTVAPPKPKTQPVPKKKTFGPVLNAKS | 2.7.11.1 | null | cardiac muscle cell development [GO:0055013]; epicardium morphogenesis [GO:1905223]; heart contraction [GO:0060047]; heart morphogenesis [GO:0003007]; phosphorylation [GO:0016310] | basolateral plasma membrane [GO:0016323] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF02816; | 2.60.40.10;3.20.200.10; | Protein kinase superfamily, Alpha-type protein kinase family, ALPK subfamily | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q86TB3}. | 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; Evidence={ECO:0000250|UniProtKB:Q86TB3}; 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; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Protein kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation (By similarity). Regulates cardiac development and cardiomyocyte differentiation by negatively regulating Wnt/beta-catenin signaling (PubMed:29888752). {ECO:0000250|UniProtKB:Q86TB3, ECO:0000269|PubMed:29888752}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QVU0 | LTK_DANRE | MDYITRQTFVKLALFIFTVLRSSCALLEKAAEDPVHPNPLQSSPAEDSDVSFCDFESPCSWTLSSHSTGGDWFITSAQQHRSSRRDTQPIRDYSTGKSEGHFLLLKPSSSHLSAGRCSFHMTSPVVLSSGPFCHLQLARFQPEPHAGNISAFVKHTDSTDIKPIDLTIKEQESDSSQWEVLEAVIGQLNEPFQVTVQYSACSSHEVGFLAFDSLELKNCVMGDDYVDLGSDCEKYSSLQCHSGGCIEKQRVCDFHTDCPEGEDEGLICSTLPLGSYCSFELGSCGWLAADTQSSWRLVSGQQLIEDTHLLGTTLKNTQGHFLFLKVRGHGDEREALVQSPALPSTISNQDCQLQFSLYRYGDFNGTVLLSVVESGASAPALIWERSGHWKDAWQEITLPITEILNGFHLKVQAFWTSGSKADIALDDISLSAACFDTELNELLHEGLPHDLDFSPLPEPSASEASPITWWFTSCGASGPFGPTQAQCDSAYRNTNVSVVVGKEGPLRGVQMWKVPATNTYKISAYGAAGGKGAKNHNKRSHGVFISATFPLEKGDILYILIGHQGEDACPGRNPQTHKICLGESSVIEDGFDSDGSALKWAGGGGGGGGATYIYRMENGQPLPLLIAAGGGGKAYLEDPESSQDQSFREQYENDTTVSGVSGRSGAAGGGGGWSDVSSLSWAGKSLVEGGQGGSSCPEALSVLGWATFGGFGGGGGACSAGGGGGGYRGGDAPLLDDISADGQDGLSFVHPMGKIFLQPLAAMESHGEAEIVVYLNCSHCKTQSCKRDEDTKLILCLCDSDEVLAPDNVTCAGTKHSLCQFINKHLQHNSSPLVCPPLVVPMGSLADGPPSLVFIMAVIVSTVVTGVVLTCASLTLIYYRKKNHLHAVRIRLQSPEYKLSKIRSSTIMTDYNPNYGYFGKAASLSELKEVPRKNITLLRALGHGAFGEVYEGQVLGMNGENTAMQVAIKTLPEICSEQDEMDFLMEALIMSKFSHQNIVRCIGVSLQILPRFILLELMTGGDMKSFLRLNRPRTNHSSSLSMLELLHMARDIALGCRYLEENHFIHRDIAARNCLLTCPGPDRVAKIGDFGMARDIYRASYYRKGGRAMLPVKWMPPEAFLEGIFTCKTDTWSFGVLLWEIFSLGYMPYPCKTNQEVLEFVTGGGRMDPPKSCPGPVYRIMTQCWQHCPEHRPNFTTILERINYCTQDPDVINTPLPVECGPPVEEEGGTVIRPDGSGSMTPLLVARSLSQDASPRASITSVTPQALKPRLQLQRPVHLTQEVGTYRETLEPCWAEPVPASGVCPGPWLQVPEHRPCSRSSSSSGSQKLKNKTKNLWNPTYGSWVLESFGRGKSALCHTQSMPLSCNPTSVSAPSSTSEHTDPVVEVNANVSASPPPSAAPSQTTLTPTAAPSRKSPTGAAGVSLATVMDLAKLQSFPCGNVNYAYDEQSYETESLPVVVSKSLEPSTSSAATSSLVALSQPGSFTHKPLVKRHASYGHEDVRRYTQPEKPTRDRDSGFSLSEDLSVTPV | 2.7.10.1 | null | developmental pigmentation [GO:0048066]; iridophore differentiation [GO:0050935]; maintenance of cell number [GO:0098727]; melanocyte differentiation [GO:0030318]; melanocyte migration [GO:0097324]; phosphorylation [GO:0016310]; pigment cell development [GO:0070285]; pigmentation [GO:0043473]; regulation of cell population proliferation [GO:0042127]; regulation of developmental pigmentation [GO:0048070]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF12810;PF00629;PF07714; | 2.60.120.200;4.10.400.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29376}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000250|UniProtKB:P29376}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells (PubMed:18369445, PubMed:23821036, PubMed:26801003, PubMed:29078341, PubMed:29317532). Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes (PubMed:18369445, PubMed:23821036, PubMed:26801003). Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:29078341, PubMed:29317532). Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen-activated protein kinase (MAPK) pathway (By similarity). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity). {ECO:0000250|UniProtKB:Q9UM73, ECO:0000269|PubMed:18369445, ECO:0000269|PubMed:23821036, ECO:0000269|PubMed:26801003, ECO:0000269|PubMed:29078341, ECO:0000269|PubMed:29317532}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QWA8 | SARM1_DANRE | MFLSLVVYLSKICRYLSMFSSDRLTVPEYVSSRLHNRRTAPDPRAVSPGISTDVQAVLDGSLPALRSAIRTLRSSKDTGDLEETRRAIAETFQLVEEAWVLPTVGRRVAEEICNRIRLDGGLELLLQLMQTPAVEITYESAKLLEQILVSENRDYVARMGLGVILNLTREQEDAQLARSVSGILEHMFKHTEETSAQLITNGALDTILYWCRGTDPTVLRHCAVALSNCAMYGGHRCQRLMIEKQAAEWLFPLAFSKEDELIRFHACLAVAVLAANREMEKEVVKSGTLELVEPFIASLDPDEFARNMLDSADSMQGRTAADLQHLLPLLDGTRLEGKCIAAFYLCVETSIKSRQRNTKIFQEIGAVQSLKRIVMYSSNATVCSLAKRALKMMSEEVPRRILSSVPNWKSGEVQTWLQQIGFSAFSERFQELQVDGDLLLNITEQDLIQDLGMTSGLTRKRFLRDLRVLKTYANYSTCDPNNLADWLADADPRFRQYTYGLVQSGVDRNNIVHITDQQLLTDCHVENGIHRAKILSAARRPSKPCLTDSQPKGPDVFISYRRTTGSQLASLLKVHLQLRGFSVFIDVEKLEAGRFEEKLITSVQRARNFILVLSANALDKCMGDVAMKDWVHKEIVTALNGKKNIVPVTDNFVWPDPTSLPEDMSTILKFNGIKWSHEYQEATIEKILRFLEGCPSQEKPDGAKTDKKEPQKK | 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]; regulation of axon regeneration [GO:0048679]; response to axon injury [GO:0048678]; signal transduction [GO:0007165] | axon [GO:0030424]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; synapse [GO:0045202] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]; signaling adaptor activity [GO:0035591] | PF00536;PF07647;PF13676; | 1.25.10.10;3.40.50.10140;1.10.150.50; | SARM1 family | null | 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:0000269|PubMed:28334607}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:28334607}; 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 (PubMed:32001778). 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 (By similarity). Wallerian degeneration is triggerred 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 (PubMed:28334607). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (By similarity). Can activate neuronal cell death in response to stress (By similarity). {ECO:0000250|UniProtKB:Q6SZW1, ECO:0000269|PubMed:28334607, ECO:0000269|PubMed:32001778}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QWW8 | KDSR_DANRE | MLLVVAAFIVAFVLLLYMISPLISPKPLKLNGAHVVVTGGSSGIGKCIAMECYKHGAFITLVARDEHKLVQAKKEVEKFAINDKQVVLCISVDVAKDYSQVESVIKQAQEKLGPVDMLVNCAGTSLSGKFEEVEVDHFKKMMEVNYLGSVYPTRAVITTMKERRMGRIMFVSSQAGQIGLFGYTAYSPSKFALRGLAEALQMEMKPYNIYVTVAYPPDTDTPGFAEENKTKPLETKLISETSGVSQPEQVAKIVVKDAVQGNFTSSFGPDGYMLSALTCGMSPVTSITEGLQQIVTMGLFRTIALFYLGSFDSIVRRCMIQREQCKAADKRE | 1.1.1.102 | null | 3-keto-sphinganine metabolic process [GO:0006666]; intracellular sphingolipid homeostasis [GO:0090156]; platelet formation [GO:0030220]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid mediated signaling pathway [GO:0090520]; sphingomyelin biosynthetic process [GO:0006686] | endoplasmic reticulum membrane [GO:0005789] | 3-dehydrosphinganine reductase activity [GO:0047560] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH; Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349; EC=1.1.1.102; Evidence={ECO:0000305|PubMed:30467204}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22642; Evidence={ECO:0000305|PubMed:30467204}; | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the reduction of 3'-oxosphinganine (3-ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis. {ECO:0000269|PubMed:30467204}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QXD3 | ZH15B_DANRE | MALSRALRCCQRIFSWIPVIIISSVVLWSYYAYVFELCFVTLSNNLERVTYLLIFHVCFIMFCWTYWKAIFTPPSTPTKKFHLSYTDKERYEMEERPEVQKQILVDIAKKLPIFTRAQSGAIRFCDRCQVIKPDRCHHCSVCETCVLKMDHHCPWVNNCVGFSNYKFFLLFLSYSMIYCVFIASTVFQYFLKFWVGDLPNGPAKFHVLFLLFVALMFFVSLMFLFGYHCWLVAKNRSTLEAFSPPVFQNGPDRNGFNVGLSKNLRQVFGEHKKLWFIPVFTSQGDGHYFPLRTLRESENPLLANEEKWVEDGGSDEESADENGSSLLIRTES | 2.3.1.-; 2.3.1.225 | null | peptidyl-L-cysteine S-palmitoylation [GO:0018230]; protein localization to membrane [GO:0072657]; protein targeting to Golgi apparatus [GO:0140450] | Golgi membrane [GO:0000139]; postsynaptic density [GO:0014069] | protein-cysteine S-myristoyltransferase activity [GO:0019705]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; protein-cysteine S-stearoyltransferase activity [GO:0140439]; zinc ion binding [GO:0008270] | PF01529; | null | DHHC palmitoyltransferase family | PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:29326245}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Postsynaptic density {ECO:0000250|UniProtKB:Q2TGJ4}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000269|PubMed:29326245}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684; Evidence={ECO:0000305|PubMed:29326245}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; | null | null | null | null | FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:29326245). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regulate target proteins association and localization to membranes (By similarity). In the nervous system, probably catalyzes the palmitoylation of synaptic proteins and is involved in the differentiation of dopaminergic neurons and the development of the diencephalon (PubMed:26095893). {ECO:0000250|UniProtKB:Q8BGJ0, ECO:0000250|UniProtKB:Q96MV8, ECO:0000269|PubMed:26095893, ECO:0000269|PubMed:29326245}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1QZ88 | E2F8_DANRE | MSSTLSEGQTLIKKSLSPSKATSTNNKGHVFVEPQTPLKNSNKASTSEAALPETLKIMGPLTTPTKVLDAPSSDPWTPTSNLKMLISAASPEIRNREKERAVDSSESENSQETEQGEEVEKLHISRKDKSLGLLCYKFLARYPNYPNPALNNGISLDDVAAELHVERRRIYDIMNVLESLNMVSRLAKNRYTWHGRVKLAQTLAVLKRAGKENRYEQLMQQIRQRSQEREEREFDLDGEEKENEEMSSFEVDGDSGLADLPGADSKAASANSRKDKSLRVMSQKFVMLFLVSSPPVVSLDVAAKILIGEDHVVDQDKNKFKTKIRRLYDIANVLSSLELIKKVHVTEDKGRKPAFKWTGPEDIPSPKDLEISTTSSAPKPLESRSSVENCAKNLFSSPGTKRGFTRHHSLVKLVKSIQDDRRKINSAPSSPIKMTGDSADSDFYTTKMAHLAAICKKHLDEQSADGRPNNAVTDSSQSSKQPESTSASNHGPPGMQIPVLPAGAISYLPTKCSPIIPLLIPQHQTGGPYAVYMHPTSLRPQPTSLAVRSMTFESPVGANAKTSPATLTSNNQTNQSSSYGKEQTSPVNLKRASGEKSSVGSPSKMQRTEPKSVSPKLCEILQARLKARRGALTSNRPSARALHLEFSKPSESQPTVQTGTASLEHSLETFLEKEEKSQTSDNEAGLTPVRQPHSQPQKLSAPFQDMVLPSGPIHTETLIPAGYLIPISQQSIVNFREPQCSNESSKASTPTYNIYHTPTAGSRPAFPQEVTPTRLPLHRIPPISPFPSHGHRLHSPSPAILNFTLQNLGLIPGSVTPNPHTPEQSSSLQSPHPGLPHQGMIFVKPMSPARALQQTSIHGQPVTLISIPQALVTTPKGGQAFQQSFFHTPVSFPTVNTTAPKKIYIPQRKLDVSPEEI | null | null | cell cycle comprising mitosis without cytokinesis [GO:0033301]; chorionic trophoblast cell differentiation [GO:0060718]; hepatocyte differentiation [GO:0070365]; lymphangiogenesis [GO:0001946]; motor neuron axon guidance [GO:0008045]; negative regulation of cytokinesis [GO:0032466]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA endoreduplication [GO:0032877]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sprouting angiogenesis [GO:0002040] | RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF02319; | 1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as e2f1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes (By similarity). Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator and promoting expression of vegfa. {ECO:0000250, ECO:0000269|PubMed:22903062}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R237 | TDRD6_DANRE | MCSIPGLPSKGSNVPVLITRVNLNPSCVLVEFWGNFDEDRKFAYQQLKKEIQYPRECFSESDGNPGDLCLVQVYETWYRARIVSRDSDEYSVFLIDEGRTLRAAVNTLAWGKSDFFYLPPEVEFCILANALPLSPENNWSSMALEFMKTFCGRRVNATVQDVLVAHRTFLLDIPCLSRQMFEMGFAKKLYSDQFMEFVVRSLQASTGTSDLKRISSIRTKPVEIIEQKEKQQAYMFPELQTDTVETVVITEVTSPFRIFCQLKVFSQELKKLTEQITQYYEGRVGSYFARAENLGSPCASRGSDGKWYRSVLQQVMSANNVVEVLHVDYGKKQFVQVENVKPLASEFFRMPVVTYVCSLHGIVDKGVGWTASQIDYLKSLLLNRTVIAKFQYQSLSEGVHYVTLYGEENTNINKLFELKPKCSLDSDMTLADFAVQKSPSSQKSKISRTTESTHINETYSDLKVNKPVFFTETLTPNSTHMAVVQHVDSPGKFWIQTQRYADEFDLLMNGLGNLYSDPTSTESLIRKPVVGLICAAKAQDGVFYRAAVYKVIDKTAEVYFLDYGNTEVVDSFNLRQLPLRFQQLPAVAVKCSLHGVKPRLKLWEERATLFFSKLVRDRIIDLHVQDKQQDTHIVQLVDPSLDGEKDVSKLLCNAGFAVSEKSIVDYSATRSCGLKTTHASGVFLTGTQPQTPCSSSVVMDSASAFKEYLFPIGSSLEVTVSYIENPNDFWCQKARNAACLEVLMQDIQRFYSHSEFEPLLEAACVARHPETGIWYRALVIQKHQTPHVDVLFIDYGQTKKVAIEDLRKITPAFLKMKGQAFRCSLYNLIHPVLHSSSDWSTEATLEFQEFVDAAASMNVPLKCTIFAVMYDSQKVVFNVVDLETPFQSICNLLVQRRLADRAPSKRSPLPPFRLDTYYYSTHGVKTGCDEKVSITCVKGVNQFFCHLARNSDEVEKLAEKVNFLCHQLEATKCPQTFGTVCFAKYTDGLWYRGQIKSTKPSVVINFVDYGDTLEVDKSDLLPVPIEAGDIMSVPVQAIECGLSDMPEELPCEVDNWFRKFADSHCFTALIVAKEPAGKLILELYDGKTQVNALIKQKFHNEIHKNDASTFKIYGLKSRAAESVEASACKKESSTGPKRDAIDQVPKSRESHAIQRSNDVASKQPQSRWGFSTNGRPEPTRDSGTINNCQKQPELRTSQGNLRHPCTSSKPEVVKPKPQALLKESALPIKSIKPGLEAEVFISHCNSPCSFFVQFATDEDDIYSLVEKLNADQSRCRNIDSSDIHEGDLVCAMFPDDSSWYRAVVRKNTNEKIDVEFVDFGNTAVISSKNVCHLGQSFASFPRYSIHCSVHKLNVDSKDQELAPNFKQVLEQNIEKVICTFVKMSGTMWEVRLDVNGVVLGSVCKDHVKPEIAIPDLKDAASEIKVCTYYKNPDISIGQVITGYTSYIKGPQLFWCQYVAMDKLQEISDMLQNIGNASETTLREDCMPVGSACIALFTEDNLWYRAKVTSKDLDTLSITFVDYGNESKVKIGDVKALPPKLSDVPPHAFDCQLEGFDVSEGFWDETADDAFYELVHDKPLNITIEKMGNSEMPHIVKLDCDGVDINTTMKSHWKTRNPETPPAELFNGAEMASDDDYVASKVNIDSVVTFDTDTDPADNETCTSALEMELSEQENLLSSTGVENEAQIDPLKMATENVTLPITESTVLSETHKKLETITEDEPVLGFTGLSDTNQHAVSKETDVGLPQHSEGASSVTIDSFLMNNTDSQLCIVEEPEAPSYEIIQSNLGCLRRATEKKPVGSECVIWSQVRRSWCTARVLKVSEEATLVLLEKYDSEVVVDPINIFEIMPEKPLQIACIEAAIANDDATKETDATLENSASKLYQTEVSDANGIAVALESEDLNGKEETFIDQMAPNDELAGQPQEEESVSCSAFLEDSKAKHMLVEGAQVHDLVQGLCPDDVESKDPQDDLNTSFEEQNDGAKMSTAVDLLLDFLDTAPRDKVQDVSETDALLEEFNIHVTEDLIVLTSDDGAESDTASDGTLHGDAVAMEVGPDTEESSCFQERSNASDCTSAEDSQVTHLTLKVEDASDDVIFVGVLQESQAVVHEPESEKEKRD | null | null | germ cell development [GO:0007281]; organelle assembly [GO:0070925]; P granule assembly [GO:1903863]; P granule organization [GO:0030719]; piRNA processing [GO:0034587]; regulation of oogenesis [GO:1905879]; spermatogenesis [GO:0007283] | chromatoid body [GO:0033391]; germ plasm [GO:0060293]; mitochondrial cloud [GO:0032019]; P granule [GO:0043186] | null | PF00567; | 2.30.30.140;2.40.50.90; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30086300}. Note=Presents in chromatoid body (CB) of spermatids, also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids (By similarity). Localizes to nuage, the Balbiani body during oogenesis, and in the grem plasm upon fertilization (PubMed:30086300). {ECO:0000250|UniProtKB:P61407, ECO:0000269|PubMed:30086300}. | null | null | null | null | null | FUNCTION: Tudor domain-containing protein involved in germ cell development, more specifically the formation of chromatoid body (during spermiogenesis), Balbiani body (during oogenesis), germ plasm (upon fertilization), and for proper miRNA expression and spliceosome maturation (By similarity) (PubMed:30086300). Required for Balbiani body and germ plasm formation and mobility through interaction with dimethylated arginines in the prion-like protein Bucky ball (buc) (PubMed:30086300). Coordinates transcript deposition into future primordial germ cells (PubMed:30086300). Interacts with known germ plasm mRNAs such as vasa, dazl, nanos3 and hook2 (PubMed:30086300). {ECO:0000250|UniProtKB:P61407, ECO:0000269|PubMed:30086300}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R2J1 | PNX_DANRE | MHEETSNSTLQGKTSFSIADILDPAKFNGTRETREISNNRESPKTTSPTQDPSAPNIANASAAKVKSKRIRTAFTLDQLRILERSFQSSHYLSVFERHCIASALGLSETQVKIWFQNRRTKWKKELDGHGGEEQSHCAPTALTQNPIMYALPGHHANHHVHYYPQQTHYLNTSFHPQTLMMY | null | null | cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; nervous system development [GO:0007399]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | NK-1 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:12642490}. | null | null | null | null | null | FUNCTION: Transcriptional repressor. Activity as a repressor is enhanced by binding to the corepressor tle3a. {ECO:0000269|PubMed:12642490}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R345 | DDX11_DANRE | MESKSGRFPFPFQPYPIQESFMEALYTALDQRKVGIFESPTGTGKSLSLICGALTWLRDYEEQRKQEAARLLEGQKDSDVVKEKNSNSGPPEPDWVSEFVQKKAERDMVNKLKDEELKRKKREERLEMIRHNAQLRYAMKRKADEDDEAVKLLQLSREGAEPETHSPEEEGLIVAEYESDDEATPKSRLCDDDNDDDDDLEEEHVTKIYYCSRTHSQLAQFVHEVQKSPYGDAVRLVNLGSRQNLCINPEVVRLGNVQMMNERCLEMQKNKHEKRQKASDSESKRSRGLAKATCVFSRFENLMAMKDEVLVKVRDVEQLIQHGRETHTCPYYSTRMSIPAAQVVVLPYQSLLHASTRKASGIKLKDQIVIIDEAHNLMDTISAIHSAEISGGQLCRAHSQLSQYCERYRSRLKAKNLMYIKQILFVLEGLVRTLGGKVGQNPNTQSCQTGSELLTINDFLFKAQVDNINLFKVQKYFEKSMISRKLCGFAEKYEGSGINTHSSSKNKENRRTEGLGRFLQTLQSKPTDVSEQQMAVEDKPIMASPMMLAESFLFALTNANKDGRVVIQRQACVAQSSLKFLLLNAAVHFAQILQECRAVIIAGGTMQPVADFKEQLLFSAGVTEERILEFSCGHVIPPENILPIVLCAGPSGQQLEFTFQTRDSPQMMEETGRVLSNLCNIVPGGVVCFFPSYEYEKRILGHWESTGILQRLQSKKKIFQEPKKASQVEQVLSEYSKCIQRCSNIGGGQTGALLFSVVGGKMSEGINFSDDLGRCIVMVGMPYPNIKSPELQEKMAYLDKHMPHVAGKSPGKALVESLCMKAVNQSIGRAIRHRGDYACIVLCDHRYARTGTLQKLPEWIRSSTHTHATFGPAFASARRFFLEKRQKATL | 3.6.4.12 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; | DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; establishment of sister chromatid cohesion [GO:0034085]; nucleolar chromatin organization [GO:1990700]; regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901836]; rRNA transcription [GO:0009303] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle pole [GO:0000922] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF06733;PF13307; | 3.40.50.300; | DEAD box helicase family, DEAH subfamily, DDX11/CHL1 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96FC9}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96FC9}. Midbody {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96FC9}. | 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:Q96FC9}; | null | null | null | null | FUNCTION: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Plays a role in the regulation of sister chromatid cohesion and mitotic chromosome segregation. Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner. Also plays a role in heterochromatin organization (By similarity). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (PubMed:26089203). Plays a role in embryonic development (PubMed:26089203). Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity). {ECO:0000250|UniProtKB:Q6AXC6, ECO:0000250|UniProtKB:Q96FC9, ECO:0000269|PubMed:26089203}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R4C4 | PIS4A_DANRE | MAAELVEAMNMVKSFRVSDLQTLLASMGRSKSGLKQDLVGRALRLVQTEYSPELLKNVRQLYETRFPKASAWLAARRPETVAVNYPALNSSPRGTGQGTDYLNGIPKPAPPPAAEVKLVPLPFYHNLETLLPPTELVAQNSEKLQESQCVFDLTPNQVDQIRNSSELRPGMKSVQVVLRICYTDSIGVQEDQYPPNIAVKVNQSYCHVPGYYPSNKPGVEPRRPCRPVNITPWLHLSTVTNRVTITWGNFGKRYSVAVYLVRVFTSGELFNQLKHCSVENPDRCRERIQDKLRFDPESEIATTGLRVSLICPLVKMRLGVPCRVLTCAHLQCFDAVFFLQMNEKKPTWTCPVCDKPAPFELLTIDGLLSEILKETPEDVEEIEYLTDGSWRPIRDDKEKERERENSRTPDYPVVDICVPEANGHSPAHSGTNQTGKSGSGGASAGTGSTSGGSGGGTVVDLTLDDSSEEEGGGGAEDSEETDDSQDSPAPKRGRYDYDKDLVTAY | 2.3.2.27 | null | negative regulation of type I interferon production [GO:0032480]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; protein sumoylation [GO:0016925]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA binding [GO:0003677]; SUMO ligase activity [GO:0061665]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270] | PF14324;PF02891; | 2.60.120.780;1.10.720.30;3.30.40.10; | PIAS family | PTM: Sumoylated. Lys-35 is the main site of sumoylation. {ECO:0000250|UniProtKB:Q8N2W9}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22345667}. | 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; Evidence={ECO:0000250|UniProtKB:Q8N2W9}; | null | PATHWAY: Protein modification; protein sumoylation. {ECO:0000250|UniProtKB:Q8N2W9}. | null | null | FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase (By similarity). May play a role as a transcriptional coregulator in various cellular pathways (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (By similarity). Negatively regulates induction of interferon phi 1 (ifnphi1) mediated by mavs and ticam1/trif. Also inhibits ifnphi1-mediated activation of the interferon-stimulated genes (ISGs) pkz and cd40, and to a lesser extent rsad2 and isg15 (PubMed:22345667). May inhibit ticam1/trif-mediated activation of NF-kappa-B (PubMed:22345667). {ECO:0000250|UniProtKB:Q8N2W9, ECO:0000269|PubMed:22345667}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R4U0 | TXTPB_DANRE | MSGSPKFVSPFHRPHCLSAAAPAGQAKLTHPGKAILAGGIAGGIEICITFPTEYVKTQLQLDEKANPPRYKGIVDCVKQTVQGHGVKGLYRGLSSLLYGSIPKAAVRFGVFEFLSNQMRDESGKLDSTRGLICGLGAGVAEAVVVVCPMETVKVKFIHDQTSANPKYRGFFHGVREIVRTQGLKGTYQGLTATVLKQGSNQAIRFYVMTALRNWYKGDNPNKSINPVVTGLFGAVAGAASVFGNTPLDVIKTRMQGLEAHKYKSTVDCAIKIMKYEGPAAFYKGTVPRLGRVCMDVAIVFIIYEEVVKVLNKVWKTD | null | null | mitochondrial citrate transmembrane transport [GO:0006843]; neuromuscular junction development [GO:0007528] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | antiporter activity [GO:0015297]; citrate secondary active transmembrane transporter activity [GO:0071913]; tricarboxylic acid transmembrane transporter activity [GO:0015142] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: Possesses a short cleavable presequence, which, however, is found to be dispensable both for targeting to mitochondria and insertion into the inner membrane. However, the presequence is required to keep SLC25A1 in a soluble state and thus in an import-competent state. Mature SLC25A1 lacking the presequence is prone to aggregation. {ECO:0000250|UniProtKB:P32089}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8JZU2}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + citrate(out) = (S)-malate(out) + citrate(in); Xref=Rhea:RHEA:72483, ChEBI:CHEBI:15589, ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=citrate(out) + D-threo-isocitrate(in) = citrate(in) + D-threo-isocitrate(out); Xref=Rhea:RHEA:72471, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=citrate(out) + succinate(in) = citrate(in) + succinate(out); Xref=Rhea:RHEA:28835, ChEBI:CHEBI:16947, ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=cis-aconitate(in) + citrate(out) = cis-aconitate(out) + citrate(in); Xref=Rhea:RHEA:72475, ChEBI:CHEBI:16383, ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=citrate(out) + trans-aconitate(in) = citrate(in) + trans-aconitate(out); Xref=Rhea:RHEA:72479, ChEBI:CHEBI:15708, ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=citrate(out) + phosphoenolpyruvate(in) = citrate(in) + phosphoenolpyruvate(out); Xref=Rhea:RHEA:72487, ChEBI:CHEBI:16947, ChEBI:CHEBI:58702; Evidence={ECO:0000250|UniProtKB:P53007}; CATALYTIC ACTIVITY: Reaction=citrate(out) + maleate(in) = citrate(in) + maleate(out); Xref=Rhea:RHEA:72491, ChEBI:CHEBI:16947, ChEBI:CHEBI:30780; Evidence={ECO:0000250|UniProtKB:P53007}; | null | null | null | null | FUNCTION: Mitochondrial electroneutral antiporter that exports citrate from the mitochondria into the cytosol in exchange for malate. Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis-aconitate and to a lesser extend cis-aconitate, maleate and succinate (By similarity). Required for proper neuromuscular junction formation (PubMed:26870663). {ECO:0000250|UniProtKB:P53007, ECO:0000269|PubMed:26870663}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R520 | CSTN1_DANRE | MRIRGVKPFASAVGLLLGLLYAVDAAKVNKHKPWIETTYHGIVTENDDKVLLDPPLIALDKDAPLRYAGEICGFRIHGQNVPFEAVVLDKSTGEGVIRAKDKLDCELQKEHTFTIQAYDCGEGPDGGNMKKSHKATVHIQVNDVNEYSPVFKEKSYKATVIEGKKYDSIMKVEAVDADCSFQFSQICSYEIVTPDVPFTIDKDGNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINIKPTCKPSWQGFNKRIEYEPGTGSLALFPSMHLETCEEPITSIQASIMLETNHIGKGCDRDTYSEKSLHKLCGASSGTVELLPAPSNSANWTVGLPTDNGHDSDQVFEFNGTQAIKVPEGVVSTTLKEPFTISVWMRHGPGGREKETILCNSDKTEMNRHHYSLYVHNCRLVLLLRQEPTESESYKPAEFHWKLDQVCDKEWHHYVLNIEFPAVTLFVDGGTFEPFLVTEDYPLHTSKIETQLTIGACWQGGSARMTQFFRGNLAGLMIRSGKLENKKVIDCLYTCKEGLDVQLPEEVASAVKVEFNPNQSSLSLEGDDIESFEKVMQHISYLNSRQFPTPGIRHLRVSTTVKCFNEETCISVPDSEGYVMVLQPEEPKISLSGIDHFARGAAEFESVEGVTLFPELRIVSTITREVEVEAEAETEAEGEDDPTVQETVVSEEIMHNLDTCEVTVVGEDLNGDHESLEVDLAQIQQRALEMSSSNVGMVITGVNTMANYEQVLHLIRYRNWHTEALFDRKFKLVCSELNGRYISNEFKVEVNVIHTANPMDHANNAMVQPQFISQVQHASVDLSGHNLVNTHQASVVPSAATIVIVVCVSFLVFMIILGVFRIRAAHQRTMRDQENGKENEMDWDDSALTITVNPMETYEDQHSSEEEGDEEEEESEDGEEEDDITSAESDSSEDEAGEQEDQQGSSRQQQLEWDDSTLTY | null | null | axon arborization [GO:0140060]; axonal transport [GO:0098930]; endocytic recycling [GO:0032456]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; regulation of collateral sprouting [GO:0048670] | axon [GO:0030424]; cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; postsynaptic membrane [GO:0045211] | amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988] | PF00028;PF19699; | 2.60.120.200;2.60.40.60; | Calsyntenin family | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9EPL2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9EPL2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9EPL2}. Note=Localized in the postsynaptic membrane of both excitatory and inhibitory synapses. {ECO:0000250|UniProtKB:Q9EPL2}. | null | null | null | null | null | FUNCTION: Postsynaptic adhesion molecule involved in vesicle trafficking; required for branching of peripheral but not central axons of sensory neurons (PubMed:25009257, PubMed:25463516). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000269|PubMed:25009257, ECO:0000269|PubMed:25463516}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R5H6 | BRD4_DANRE | MGDGLDAVQMSGSSSSQGQPSSQAPSSFNPNPPETSNPTRPKRQTNQLQYLLKVVLKSLWKHQFAWPFHAPVDAVKLNLPDYYKIIKNPMDMGTIKKRLESAFYTSAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKVFLTKISEMPQQEVEISTTAGKGRGRGRRDPDMNMKVGPVLEPLTASPQTRGLSNLTPGPQTRGPPQGPPTLPPQPIVQIQALPPRVPPSLPTIPLHAPQLGPPFSLGPTDCNPPAPIITAVPPPTQTALPPVHIQQSAAPPILQTPISIPNKRKSQKRKADTTTPTANDQLNESSPAESKSGKTLPRRDNTRPSKLPKKEAPDSQHHWTAAPGTPSPKQQEQLRYCSGIVKDMFAKKHAAYAWPFYKPVDVDTLGLHDYHDIIKHPMDLSTIKDKLETRQYREAQEFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEMLAPAPAPVLHPAPVKTQPVMATASSSDTSSDSSSESESSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQASKPKKKEKEKKEKKKDKHKKKAGVMPALEEILEPPPALKPQGKPKNKDPLPKKSKKLSKKEGGKSNRSMAPPGAAPPTLQPVPGLDTEEDLGLTGGAAMAGMAAGEKCKPMSYEEKRQLSLDINKLPGDKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVSSCLRKKKKPAVPEKSMEAISAVKTKGTSSDSGSSSESSSSESEDSETGMASKPKKRGRGEGKKAHHQTTAPGMPLPQVPLQPQTPALQPSIQLKQQQPQHPSPAAYMPPPVTALEPSQLLENPFDPLAHFMHLPHHANDSSSPAPPHLNAHPPGGPVSPETHPFLNQHPILPSPALHNALPQQPSRPSNRAAPLPPKPLQQSTSQQQPPPQQTLVPPQQLQPQQQQPAPPQQQHLPHHPLHAPQQMRPRPLSPPTLTPQGLLSSQPPQMLLEDDEEPVPSMSLPMYLQHLQPNRLQATPTSLMQSLQSRPQPPGQPSLLQSVQVQSHLPPPQLPVQTQVQPQQPAPHQPSPQLSQHQARHMQQLGFPQGPLQTAQTQPGQHKVSMPSTKAQQIIQQQQATQHHSPRQHKADSYNSAHLRDNPSPLMMHSPQIPQYSLVHQSPSQDKKEPQRGPSALGGIKEEKLPPSPVMRGEPFSPAMRPESHKHPDSKPTMPGHSQQRADMKPLEMSRPVIRSSEQSGPPPSMQDKEKFKQEPKTPSAPKKVQDVKFKNMGSWASLAQKSSTTPSSGLKSSSDSFEQFRRAAREKEEREKALKAQVEQAEKDRLRKEQEKLRGRDEEDSIEPPRRPLEEPRRRQEPQQVQPPPQQHQTQAQAQTLNPAQSPSASQPTQAPPQSPASSQSALDQQREMARRREQERRRREAMAATIDMNFQSDLMAIFEENLF | null | null | chromatin remodeling [GO:0006338]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of T-helper 17 cell lineage commitment [GO:2000330]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of DNA-templated transcription [GO:0006355]; regulation of inflammatory response [GO:0050727]; thrombocyte differentiation [GO:0002574] | chromatin [GO:0000785]; condensed chromosome [GO:0000793]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039] | PF17035;PF17105;PF00439; | 1.20.1270.220;1.20.920.10; | BET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18498094}. Chromosome {ECO:0000269|PubMed:18498094}. Note=Associates with acetylated chromatin. | null | null | null | null | null | FUNCTION: Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (By similarity). {ECO:0000250|UniProtKB:O60885}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1R777 | MTA70_DANRE | MSDTWSHIQAHKKQLDSLRERLQRRRKDPTQLGTEVGSVESGSARSDSPGPAIQSPPQVEVEHPPDPELEKRLLGYLSELSLSLPTDSLTITNQLNTSESPVSHSCIQSLLLKFSAQELIEVRQPSITSSSSSTLVTSVDHTKLWAMIGSAGQSQRTAVKRKADDITHQKRALGSSPSIQAPPSPPRKSSVSLATASISQLTASSGGGGGGADKKGRSNKVQASHLDMEIESLLSQQSTKEQQSKKVSQEILELLNTSSAKEQSIVEKFRSRGRAQVQEFCDYGTKEECVQSGDTPQPCTKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDSPPEAEGDALGPQAGAAELGLHSTVGDSNVGKLFPSQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRKLNIPILQDDGFLFLWVTGRAMELGRECLSLWGYDRVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNRGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPEVVARFKKRYPDGVISKPKNM | 2.1.1.348 | null | adenosine to inosine editing [GO:0006382]; cellular response to UV [GO:0034644]; DNA damage response [GO:0006974]; endothelial to hematopoietic transition [GO:0098508]; flagellated sperm motility [GO:0030317]; forebrain radial glial cell differentiation [GO:0021861]; gliogenesis [GO:0042063]; hematopoietic stem cell proliferation [GO:0071425]; mRNA catabolic process [GO:0006402]; mRNA destabilization [GO:0061157]; mRNA methylation [GO:0080009]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; Notch signaling pathway involved in arterial endothelial cell fate commitment [GO:0060853]; oocyte maturation [GO:0001556]; oogenesis [GO:0048477]; positive regulation of cap-independent translational initiation [GO:1903679]; positive regulation of translation [GO:0045727]; primary miRNA processing [GO:0031053]; regulation of apoptotic process [GO:0042981]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of meiotic cell cycle [GO:0051445]; regulation of mRNA modification [GO:0090365]; regulation of T cell differentiation [GO:0045580]; sex determination [GO:0007530]; spermatogenesis [GO:0007283]; stem cell population maintenance [GO:0019827] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396] | mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; mRNA (N6-adenosine)-methyltransferase activity [GO:0001734]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]; RNA methyltransferase activity [GO:0008173]; S-adenosyl-L-methionine binding [GO:1904047] | PF05063; | null | MT-A70-like family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86U44}. Nucleus speckle {ECO:0000250|UniProtKB:Q86U44}. Cytoplasm {ECO:0000250|UniProtKB:Q86U44}. Note=Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components. {ECO:0000250|UniProtKB:Q86U44}. | CATALYTIC ACTIVITY: Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348; Evidence={ECO:0000250|UniProtKB:Q86U44, ECO:0000250|UniProtKB:Q8C3P7}; | null | null | null | null | FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing (PubMed:28869969). In the heterodimer formed with mettl14, mettl3 constitutes the catalytic core (By similarity). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing and translation efficiency (By similarity). M6A is also involved in hematopoietic stem cells specification: m6A methylation and subsequent destabilization of mRNAs, such as notch1a, leads to decreased Notch signaling, promoting endothelial to hematopoietic transition (PubMed:28869969). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (By similarity). Mediates methylation of pri-miRNAs (By similarity). {ECO:0000250|UniProtKB:Q86U44, ECO:0000250|UniProtKB:Q8C3P7, ECO:0000269|PubMed:28869969}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RA39 | MCA2B_DANRE | MGETEEERTSQAGQLFENFIQATTCKGTLQAFSVLCRQLELNPSDHRGFYSSLKTAVTFWKAKGLWGKLDKRAGHKEYSKGRACADTRCLIIGGGPCGFRTAIELALLGAKVVVIEKRDTFSRNNVLHLWPYTIHDLRNLGAKKFYGKFCAGSIDHISIRQLQLMLLKIALIVGVEVHVNVEFVKLLEPPEDQSTDGQGWRAEIRPADNPVSDYEFDVIIGADGRRSTLDGFRRKEFRGKLAIAITANFVNRNTTAEAKVEEISGVAFIFNQKFFLELKEETGIDLENIVYYKDNTHYFVMTAKKQSLLDKGVIINDYIETERLLAFDNVNQEALLSYAREAADFGTNYQLPSLDYAINHYGQPDVAMFDFTCMYASENAALVREKSHRQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMIKGWAQGKEPLDLLSERESIYRLLPQTTAENISKNFEQYTIDPATRYPNLNSSCVRPHQVRHLFISGEQDLSSLERSGQTRRSVSISRRESEVRPGRLLLWCQNQTQDYRGVNVTDLNTSWRSGLALCALIHRQRPELIDFDSLNEADCAKNNQLAFDVAEREFGIQPVTTGKEMDAERGPDKLIMVLYLSKFYEMFHKSTQSVTGLPKEIDANNGDCSSKTANSLYNSINHARKRIPKLDKKLEESDVNRKRKKASSHHEELMSCQTAPPAGEREEQKENKVRSMATQLLARFEENAPSCALRRQSDSESDSDADRPVSLDLTENPRFARPKIEPTHPSTTPDKAKWQPSPYLRLLESNTRSETLHTEHYVESQSSHRLTEIQSECQYSSVSSAYKSSERRPRSPLIPFTPTLSPMMHCLQQLEEQVIQQRKREPLNRKSIKERAQKLSSLFTGNPAQPQTDESSPAVSPSSPPQTIPESSTLSCLLSPAPSLTHKQCSEASETHLKADKHTEIRRVERLDPSKQRTVGKVSSAIGVKAATLAILYETDHRPNNPITLSLTEARRCAESGLVSVRKEFSASLGGSDTCVFCQKRVYIMERLSAEGFFFHRECFRCHICGCSLRLGAHTFDSQQGTFYCKMHFSQRKTSTRHRRGEIQDGGIRSSSITISNHTSTDGTRGQPSGGEFDSSTQQDLQTLPDSKEIISVSEVKDSSKKADPADSAPACPDSPLQKVKRSTAKGEITNKNILWKKKIRSTLPLVLMKKFHRGKPEDKTEVLAEEDGNSDFEEIHESLSSKKPSNPSTDSNCLPTKDNSSTPLDEIPKIPLYRTHVLPEYPKPSSSSPEPIVTSISSDPISFSPKKKLTLSLSEKEKLLNWDLTNPGKSGAEEQQQQHVKPSISLQHDHPEPTHPQPEPAPPLFGFQQWANNLRKSFSKGSNPVVLRRNRPMKARPLSEGSFNVGAVFQDEERCGSLVDEGEARPRTESEIASLLEQVALGSKTSRGTKDDMASLPPRKLNFFSSLRIKRVEGAEQSRGEGQKDILSILSRFRNKASAQQQQQQKSNSSSEDEQEPKLTHSGALQKKKEKIAIRQTKSDELKRLHRAQVIQRQLEEVEEKQRSLEEKGVALEKVLRGENGDDGSTDEAALLQTWFKLVLEKNKLSRYESELMIFAQELELEDTQSRLQQDLRRRMATEDCEKSASELVEEQNILVEIMKVVEKRDKLVSLLEEQRLKEKAEDRDLESLILSRGYQFHWT | 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] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491] | 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: Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin and regulates the srf signaling. Acts by modifying nuclear actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (By similarity). 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 (PubMed:24440334). {ECO:0000250|UniProtKB:O94851, ECO:0000269|PubMed:24440334}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RAX4 | STRA6_DANRE | MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFNIILSNDRQEVVRIVVYYLWCVEICYVSAVTLSCLVNLLMLMRSMVLHRSNLKGLYRGDSLNVFNCHRSIRPSRPALVCWMGFTSYQAAFLCLGMAIQTLVFFICILFAVFLIIIPILWGTNLMLFHIIGNLWPFWLTLVLAALIQHVASRFLFIRKDGGTRDLNNRGSLFLLSYILFLVNVMIGVVLGIWRVVITALFNIVHLGRLDISLLNRNVEAFDPGYRCYSHYLKIEVSQSHPVMKAFCGLLLQSSGQDGLSAQRIRDAEEGIQLVQQEKKQNKVSNAKRARAHWQLLYTLVNNPSLVGSRKHFQCQSSESFINGALSRTSKEGSKKDGSVNEPSKEAESAAASN | null | null | chordate embryonic development [GO:0043009]; retinol transport [GO:0034633]; vitamin A import into cell [GO:0071939] | plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632]; signaling receptor activity [GO:0038023] | PF14752; | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27563101}; Multi-pass membrane protein {ECO:0000269|PubMed:27563101}. | null | null | null | null | null | FUNCTION: Retinol transporter. Accepts retinol from the extracellular retinol-binding protein rbp4, mediates retinol transport across the cell membrane, and then transmits retinol to the cytoplasmic retinol-binding protein rbp1 (PubMed:27563101). Required for normal vitamin A homeostasis (PubMed:18316031). {ECO:0000269|PubMed:18316031, ECO:0000269|PubMed:27563101}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RB95 | RNF14_DANRE | MSADQEAKEDELLALASIYDEEEFHRAESGKEGEIHLCLELPPNFKLLVKGQKSAEHNISFLPPLVLSFDLPDDYPSTSAPIFTISSKWLTRVQITALCRKLDELWEENQGNVVLFTWIQFLKEETLDFLGIQSPLEIQRSGSQPQCEPAQKHAADASGEKSKVQDLDPRAVQEVDAQTDILTQLLDFDEAQKQRVFDGKAFCCGICYSEKLGCDCLLFKECEHVYCKACIKEYFQIQIKDGKVQCLNCPEPKCASTATPTQVKLLVGEDEFARYDRLLLQSSLDLMADVVYCPRMSCCMAVMVEPDSTMGICPSCRYAFCTLCRRSYHGLSHCIATADELRSLRDEYLSSSEEGKKFLEKRFGKRVIQRAVEESFSTDWLKTNCKQCPCCGTNIQKAHGCNKMTCSSCQKYFCWICLGALSRVNPYSHFNNPDSPCYNQLFHGMEMEEDEAFGSDEDD | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; protein-RNA covalent cross-linking repair [GO:0160127]; regulation of canonical Wnt signaling pathway [GO:0060828]; rescue of stalled ribosome [GO:0072344]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01485;PF05773; | 1.20.120.1750;2.20.25.20;3.10.110.10;3.30.40.10; | RBR family, RNF14 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBS8}. Nucleus {ECO:0000250|UniProtKB:Q9UBS8}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9UBS8}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9UBS8}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Recruited to stalled ribosomes by the ribosome collision sensor GCN1 and mediates 'Lys-6'-linked ubiquitination of target proteins, leading to their degradation (By similarity). Mediates ubiquitination of eef1a1/eEF1A and etf1/eRF1 translation factors on stalled ribosomes, leading to their degradation (By similarity). Specifically required to resolve RNA-protein cross-links caused by reactive aldehydes, which trigger translation stress by stalling ribosomes: acts by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, leading to their removal by the ATP-dependent unfoldase VCP and subsequent degradation by the proteasome (By similarity). Independently of its function in the response to stalled ribosomes, acts as a regulator of transcription in Wnt signaling via its interaction with TCF transcription factors (tcf7/tcf1, tcf7l1/tcf3 and tcf7l2/tcf4) (PubMed:23449499). {ECO:0000250|UniProtKB:Q9UBS8, ECO:0000269|PubMed:23449499}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RBC8 | ABCD1_DANRE | MSVYSKLPSQLKKPLVKKAVVLLIALYGVKKLSPYFFGKLKGRTSKQVKGADPLTSNGEPLVEAARKRKRSPAVNREFFDRLIRLLKILFPRLFCKELGLLGFHSLALISRTFLSIYVANLDGQIVKTIVKKDPRAFVVELTKWLLIAIPATFVNSAIRYLEGQLTLAFRTRLVTHAYMLYFSDQTYYRVSNMDGRLANPDQSLTEDVVMFAASVAHLYSNLTKPILDVVVTCYTLIKTAESKGANTTWPSVIAGIVVALTAKVLRAFSPRFGKLVAEEARRKGDLRYMHSRIIANSEEIAFYGGHKIEMLQLQRSYNSLSRQINLILFKRLWYVMLEQFLMKYLWSASGLVMVAVPIITATGYSKYDSEDVKQAALDMKEEDLVSERTQAFTTARSLLNAAADAVERIMVSYKEVTELAGYTARVYEMFEVFEDVRDGVYRRSATEVKPEETGAPQNVTHGMRVEGPLQIRGQVIDVEQGIKCENLPIITPTGDVVVSSLNMQVDEGMHLLITGPNGCGKSSLFRILSGLWPVYSGVLYKPSPDHMFYIPQRPYMSVGTLRDQVIYPHSVQEMQEKGITDRQLEEILQTVSLRYILEREGGWDAVSDWKDVLSGGEKQRMGMARMFYHKPQYALLDECTSAVSIDVEGKIFEAAKDAGISLLSITHRPSLWKYHSHLLQFDGEGGWRFEKLDASTRISLQDEKIRLETQLSGIPKMQQRLTELCRILGEDSSLPTPGDEEEDEEEDEKQTERDVQSAGKEKDLME | 3.1.2.-; 7.6.2.- | null | adrenal gland development [GO:0030325]; cholesterol transport [GO:0030301]; fatty acid beta-oxidation [GO:0006635]; long-chain fatty acid import into peroxisome [GO:0015910]; motor behavior [GO:0061744]; oligodendrocyte development [GO:0014003]; peroxisome organization [GO:0007031]; positive regulation of myelination [GO:0031643]; swimming behavior [GO:0036269]; very long-chain fatty acid catabolic process [GO:0042760]; very long-chain fatty acid metabolic process [GO:0000038] | peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | ABC-type fatty-acyl-CoA transporter activity [GO:0015607]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acid transporter activity [GO:0005324]; very long-chain fatty acyl-CoA hydrolase activity [GO:0052817] | PF06472;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000255}. | 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}; 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: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. 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. 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 (By similarity). Involved in oligodendrocyte patterning and myelination (PubMed:28911205). {ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:28911205}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RCP1 | BECN1_DANRE | METLRFSSNTMQVSFVCQRCNQPLKLDTSFNVLDRMTIHELTAPLVMVTANKQQDSGESSSFPEETFLENKQDGVARKFIPPARMMSAESTNSFTLIGEASDGGTMENLSRRLKVTSNLFDIMSGQTDIDHPLCEECTDTLLDHLDTQLNITENECQNYKSCLELLSQLPEEEEASLLNALQQLKQEEESLIQELESIETKREAVAKELDEGRNHSQLMDTEELRYQKEYCEFKRQQLELDDDLKSVDNQMRYCQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALASKMGLCFQRYQLVPYGNHSYLESLSDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKDDTGFCLPYRMDVDKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNR | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to nitrogen starvation [GO:0006995]; cellular senescence [GO:0090398]; early endosome to late endosome transport [GO:0045022]; heart development [GO:0007507]; late endosome to vacuole transport [GO:0045324]; mitophagy [GO:0000423]; positive regulation of autophagy [GO:0010508]; regulation of skeletal muscle tissue regeneration [GO:0043416] | autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; mitochondrial membrane [GO:0031966]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272] | phosphatidylinositol 3-kinase binding [GO:0043548]; protein-macromolecule adaptor activity [GO:0030674] | PF04111;PF17675;PF15285; | 6.10.250.3110;1.10.418.40; | Beclin family | PTM: Polyubiquitinated at Lys-399 with 'Lys-48'-linkages (PubMed:28445460). 'Lys-48'-linked polyubiquitination of Lys-399 leads to degradation (PubMed:28445460). Deubiquitinated by ATXN3, leading to stabilization (PubMed:28445460). {ECO:0000305|PubMed:28445460}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14457}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome {ECO:0000250|UniProtKB:Q14457}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays a central role in autophagy (PubMed:24441423, PubMed:27467399, PubMed:28445460). Acts as a core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis (By similarity). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms (By similarity). Involved in endocytosis including endosome formation in neuronal cells (By similarity). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:24441423, ECO:0000269|PubMed:27467399, ECO:0000305|PubMed:28445460}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
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