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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A6NDG6 | PGP_HUMAN | MAAAEAGGDDARCVRLSAERAQALLADVDTLLFDCDGVLWRGETAVPGAPEALRALRARGKRLGFITNNSSKTRAAYAEKLRRLGFGGPAGPGASLEVFGTAYCTALYLRQRLAGAPAPKAYVLGSPALAAELEAVGVASVGVGPEPLQGEGPGDWLHAPLEPDVRAVVVGFDPHFSYMKLTKALRYLQQPGCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGATCGLKTILTLTGVSTLGDVKNNQESDCVSKKKMVPDFYVDSIADLLPALQG | 3.1.3.21; 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8}; | glycerol biosynthetic process [GO:0006114]; glycerophospholipid metabolic process [GO:0006650]; negative regulation of gluconeogenesis [GO:0045721] | cytoplasm [GO:0005737] | ADP phosphatase activity [GO:0043262]; glycerol-1-phosphatase activity [GO:0000121]; glycerol-3-phosphatase activity [GO:0043136]; magnesium ion binding [GO:0000287]; phosphoglycolate phosphatase activity [GO:0008967]; protein tyrosine phosphatase activity [GO:0004725] | PF13344;PF13242; | 3.40.50.1000; | HAD-like hydrolase superfamily, CbbY/CbbZ/Gph/YieH family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:26755581}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:26755581}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for glycerol-3-phosphate {ECO:0000269|PubMed:26755581}; KM=1.5 mM for 2-phosphoglycolate {ECO:0000269|PubMed:26755581}; Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate {ECO:0000269|PubMed:26755581}; Vmax=500 nmol/min/mg enzyme with 2-phosphoglycolate as substrate {ECO:0000269|PubMed:26755581}; Note=Given the respective intracellular concentrations of glycerol-3-phosphate and 2-phosphoglycolate, glycerol-3-phosphate with a concentration of 2 to 10 mM is most probably the physiological substrate. {ECO:0000269|PubMed:26755581}; | null | null | null | FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:26755581). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity). {ECO:0000250|UniProtKB:Q8CHP8, ECO:0000269|PubMed:26755581}. | Homo sapiens (Human) |
A6NDV4 | TMM8B_HUMAN | MNMPQSLGNQPLPPEPPSLGTPAEGPGTTSPPEHCWPVRPTLRNELDTFSVHFYIFFGPSVALPPERPAVFAMRLLPVLDSGGVLSLELQLNASSVRQENVTVFGCLTHEVPLSLGDAAVTCSKESLAGFLLSVSATTRVARLRIPFPQTGTWFLALRSLCGVGPRFVRCRNATAEVRMRTFLSPCVDDCGPYGQCKLLRTHNYLYAACECKAGWRGWGCTDSADALTYGFQLLSTLLLCLSNLMFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDQPGIVVFCIMDYDVLQFCDFLGSLMSVWVTVIAMARLQPVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGILATAWTVRSVRRRHCYPPTWRRWLFYLCPGSLIAGSAVLLYAFVETRDNYFYIHSIWHMLIAGSVGFLLPPRAKTDHGVPSGARARGCGYQLCINEQEELGLVGPGGATVSSICAS | null | null | cell-matrix adhesion [GO:0007160]; regulation of mitotic cell cycle [GO:0007346] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | PF12036; | null | TMEM8 family | PTM: Isoform 2 is N-glycosylated. {ECO:0000269|PubMed:15498789}. | SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17641538}; Multi-pass membrane protein {ECO:0000269|PubMed:17641538}. Cytoplasm {ECO:0000269|PubMed:17641538}. Nucleus {ECO:0000269|PubMed:17641538}. Mitochondrion {ECO:0000269|PubMed:17641538}. Endoplasmic reticulum {ECO:0000269|PubMed:17641538}. Note=Also detected in mitochondrion and endoplasmic reticulum (PubMed:17641538). | null | null | null | null | null | FUNCTION: May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion. {ECO:0000269|PubMed:15498789, ECO:0000269|PubMed:15723283, ECO:0000269|PubMed:17270023, ECO:0000269|PubMed:17641538}. | Homo sapiens (Human) |
A6NED2 | RCCD1_HUMAN | MAEERPGAWFGFGFCGFGQELGSGRGRQVHSPSPLRAGVDICRVSASWSYTAFVTRGGRLELSGSASGAAGRCKDAWASEGLLAVLRAGPGPEALLQVWAAESALRGEPLWAQNVVPEAEGEDDPAGEAQAGRLPLLPCARAYVSPRAPFYRPLAPELRARQLELGAEHALLLDAAGQVFSWGGGRHGQLGHGTLEAELEPRLLEALQGLVMAEVAAGGWHSVCVSETGDIYIWGWNESGQLALPTRNLAEDGETVAREATELNEDGSQVKRTGGAEDGAPAPFIAVQPFPALLDLPMGSDAVKASCGSRHTAVVTRTGELYTWGWGKYGQLGHEDTTSLDRPRRVEYFVDKQLQVKAVTCGPWNTYVYAVEKGKS | null | null | chromatin organization [GO:0006325] | chromosome [GO:0005694]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | null | PF00415; | 2.130.10.30; | null | PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of ARG-141 by KDM8. {ECO:0000269|PubMed:29563586}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24981860}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000269|PubMed:24981860}. | null | null | null | null | null | FUNCTION: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with KDM8 (PubMed:24981860). Possibly together with KDM8, is involved in proper mitotic spindle organization and chromosome segregation (PubMed:24981860). Plays a role in regulating alpha-tubulin deacetylation and cytoskeletal microtubule stability, thereby promoting cell migration and TGF-beta-induced epithelial to mesenchymal transition (EMT), potentially through the inhibition of KDM8 (PubMed:28455245). {ECO:0000269|PubMed:24981860, ECO:0000269|PubMed:28455245}. | Homo sapiens (Human) |
A6NEM1 | GG6L9_HUMAN | MWPQPRLPPHPAMSEKTQQGKLAAAKKKLKAYWQRKSPGIPAGANRKKKINGSSPDTFTSGGYHSPGDSATGIYGEGRASSTTLQDLESQYQELAVALDSSSAIISQLTENINSLVRTSKEEKKHEIHLVQKLGRSLFKLKNQTAEPLAPQPPAGPSKMEQLQDETNHLRKELESVGRQLQAEVENNQMLSLLNRRQEERLREQEERLREQEERLCEQEERLCEQEERLREQEERLCEQEKLPGQERLLEEVEKLLEQERRQEEQERLLERERLLDEVEELLEQERLRQQDERLWQQETLRELERLRELERMLELGWEALYEQRAEPRSGFEELNNENKSTLQLEQQVKELEKSGGAEEPRGSESAAAARPVAGAPVPQGAWMCGQAGWTPQEHPGLSGEAVGTGEAAGGAGEAACHSFRAAENRELNITII | null | null | null | null | null | PF15070; | null | GOLGA6 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A6NFA1 | TIKI2_HUMAN | MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRDPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTRVYFELDLTDPYTISALASCQLLPHGENLQDVLPHELYWRLKRHLDYVKLMMPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTERDVRFRGVPVLDLYLAQQAEKMKKTTGAVEQVEEQCHPLNNGLNFSQVLFALNQTLLQQESVRAGSLQASYTTEDLIKHYNCGDLSAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLRENEDKICFFAFGAGHFLGNNTVIDILRQAGLEVDHTPAGQAIHSPAPQSPAPSPEGTSTSPAPVTPAAAVPEAPSVTPTAPPEDEDPALSPHLLLPDSLSQLEEFGRQRKWHKRQSTHQRPRQFNDLWVRIEDSTTASPPPLPLQPTHSSGTAKPPFQLSDQLQQQDPPGPASSSAPTLGLLPAIATTIAVCFLLHSLGPS | 3.4.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22726442}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:22726442}; Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000269|PubMed:22726442}; | negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of protein oxidation [GO:1904808]; positive regulation of protein-containing complex assembly [GO:0031334]; proteolysis [GO:0006508]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; Wnt-protein binding [GO:0017147] | PF01963; | null | TIKI family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22726442}; Single-pass type I membrane protein {ECO:0000269|PubMed:22726442}. | null | null | null | null | null | FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation. {ECO:0000269|PubMed:22726442}. | Homo sapiens (Human) |
A6NFQ2 | TCAF2_HUMAN | MATIAAAAFEALMDGVTCWDVPRGPIPSELLLIGEAAFPVMVNDKGQVLIAASSYGRGRLVVVSHEGYLSHTGLAPFLLNAVSWLCPCPGAPVGVHPSLAPLVNILQDAGLEAQVKPEPGEPLGVYCINAYNDTLTATLIQFVKHGGGLLIGGQAWYWASQHGPDKVLSRFPGNKVTSVAGVYFTDTYGDRDRFKVSKKVPKIPLHVRYGEDVRQDQQQLLEGISELDIRTGGVPSQLLVHGALAFPLGLDASLNCFLAAAHYGRGRVVLAAHECLLCAPKMGPFLLNAVRWLARGQTGKVGVNTNLKDLCPLLSEHGLQCSLEPHLNSDLCVYCCKAYSDKEAKQLQEFVAEGGGLLIGGQAWWWASQNPGHCPLAGFPGNIILNCFGLSILPQTLKAGCFPVPTPEMRSYHFRKALSQFQAILNHENGNLEKSCLAKLRVDGAAFLQIPAEGVPAYISLHRLLRKMLRGSGLPAVSRENPVASDSYEAAVLSLATGLAHSGTDCSQLAQGLGTWTCSSSLYPSKHPITVEINGINPGNNDCWVSTGLYLLEGQNAEVSLSEAAASAGLRVQIGCHTDDLTKARKLSRAPVVTHQCWMDRTERSVSCLWGGLLYVIVPKGSQLGPVPVTIRGAVPAPYYKLGKTSLEEWKRQMQENLAPWGELATDNIILTVPTTNLQALKDPEPVLRLWDEMMQAVARLAAEPFPFRRPERIVADVQISAGWMHSGYPIMCHLESVKEIINEMDMRSRGVWGPIHELGHNQQRHGWEFPPHTTEATCNLWSVYVHETVLGIPRAQAHEALSPPERERRIKAHLGKGAPLCDWNVWTALETYLQLQEAFGWEPFTQLFAEYQTLSHLPKDNTGRMNLWVKKFSEKVKKNLVPFFEAWGWPIQKEVADSLASLPEWQENPMQVYLRARK | null | null | negative regulation of anion channel activity [GO:0010360]; positive regulation of cell migration [GO:0030335]; positive regulation of protein targeting to membrane [GO:0090314] | cell junction [GO:0030054]; plasma membrane [GO:0005886] | transmembrane transporter binding [GO:0044325] | PF17291;PF13402; | 3.40.390.80;1.10.390.30; | TCAF family | null | SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:25559186}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000269|PubMed:25559186}. | null | null | null | null | null | FUNCTION: [Isoform 2]: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}. | Homo sapiens (Human) |
A6NFX1 | MFS2B_HUMAN | MAAPPAPAAKGSPQPEPHAPEPGPGSAKRGREDSRAGRLSFCTKVCYGIGGVPNQIASSATAFYLQLFLLDIAQIPAAQVSLVLFGGKVSGAAADPVAGFFINRSQRTGSGRLMPWVLGCTPFIALAYFFLWFLPPFTSLRGLWYTTFYCLFQALATFFQVPYTALTMLLTPCPRERDSATAYRMTVEMAGTLMGATVHGLIVSGAHRPHRCEATATPGPVTVSPNAAHLYCIAAAVVVVTYPVCISLLCLGVKERPDPSAPASGPGLSFLAGLSLTTRHPPYLKLVISFLFISAAVQVEQSYLVLFCTHASQLHDHVQGLVLTVLVSAVLSTPLWEWVLQRFGKKTSAFGIFAMVPFAILLAAVPTAPVAYVVAFVSGVSIAVSLLLPWSMLPDVVDDFQLQHRHGPGLETIFYSSYVFFTKLSGACALGISTLSLEFSGYKAGVCKQAEEVVVTLKVLIGAVPTCMILAGLCILMVGSTPKTPSRDASSRLSLRRRTSYSLA | null | null | carbohydrate transport [GO:0008643]; lipid transport [GO:0006869]; positive regulation of platelet aggregation [GO:1901731]; sphingolipid biosynthetic process [GO:0030148]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376] | plasma membrane [GO:0005886] | sphingolipid transporter activity [GO:0046624]; symporter activity [GO:0015293] | PF13347; | 1.20.1250.20; | Major facilitator superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29045386, ECO:0000269|PubMed:29563527}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane and intracellular membranes. {ECO:0000269|PubMed:29045386}. | CATALYTIC ACTIVITY: Reaction=sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38667, ChEBI:CHEBI:60119; Evidence={ECO:0000305|PubMed:29563527}; CATALYTIC ACTIVITY: Reaction=sphinganine 1-phosphate(in) = sphinganine 1-phosphate(out); Xref=Rhea:RHEA:38671, ChEBI:CHEBI:57939; Evidence={ECO:0000250|UniProtKB:Q3T9M1}; CATALYTIC ACTIVITY: Reaction=sphinga-4E,14Z-dienine-1-phosphate(in) = sphinga-4E,14Z-dienine-1-phosphate(out); Xref=Rhea:RHEA:70207, ChEBI:CHEBI:149632; Evidence={ECO:0000250|UniProtKB:Q3T9M1}; | null | null | null | null | FUNCTION: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets (PubMed:29045386). Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology (By similarity). Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation (By similarity). Mediates the export of different sphingosine-1-phosphate (S1P) species, including S1P(d18:0) (sphinganine 1-phosphate), S1P (d18:1) (sphing-4-enine 1-phosphate) and S1P (d18:2) (sphinga-4E,14Z-dienine-1-phosphate) (Probable). Release of sphingosine-1-phosphate is facilitated by a proton gradient (By similarity). In contrast, cations, such as sodium, are not required to drive sphingosine-1-phosphate transport (Probable). In addition to export, also able to mediate S1P import (By similarity). Does not transport lysophosphatidylcholine (LPC) (Probable). {ECO:0000250|UniProtKB:Q3T9M1, ECO:0000269|PubMed:29045386, ECO:0000305|PubMed:29563527}. | Homo sapiens (Human) |
A6NFY7 | SDHF1_HUMAN | MSRHSRLQRQVLSLYRDLLRAGRGKPGAEARVRAEFRQHAGLPRSDVLRIEYLYRRGRRQLQLLRSGHATAMGAFVRPRAPTGEPGGVGCQPDDGDSPRNPHDSTGAPETRPDGR | null | null | mitochondrial respiratory chain complex II assembly [GO:0034553] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | null | PF05347; | null | Complex I LYR family, SDHAF1 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:19465911}. | null | null | null | null | null | FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:19465911, PubMed:24954417). Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants (PubMed:24954417). May act together with SDHAF3 (PubMed:24954417). Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241). {ECO:0000269|PubMed:19465911, ECO:0000269|PubMed:24954417, ECO:0000269|PubMed:26749241}. | Homo sapiens (Human) |
A6NGG8 | PCARE_HUMAN | MGCTPSHSDLVNSVAKSGIQFLKKPKAIRPGCQGGSERGSIPLLVKNSTCYDAGEGLAEEQPSPRRNQTTAKGLCQLMGDPASGKRKDMEGLIPGTKTSSSQLNKSQSHMAKDIPFKTQGSHGSQGADFSGDESEESSTQDTSKWKRTAKCHTSSTQSHCYQTIHPAHEPEGKVDFPEPLVKAHQQAYTYLHSSLSKYEAILCIIHQATQTRELLQPMVSFLLLCFEEISQLLGEISKDGEVLLQEVREDLAWPLKKREPQEQPNLLQQLLQYTVSKLQVLNGTVASLTGSFLEGSSSYLHSTATHLENKLSTKRNVDERLLRALRQLESLASGCGDPGVQGLPLCSEDSGIGADNESVQSVDKLGKQTSWDLAPEPEEWKSVTSPHTEARQSGHTWQQSPFCLGSGRPQDCLLSGAPMAKVQPRAQDEARSPCLSSTSPENITSPPLKLGTSTPCDSFGIGVSVEPHLSKTSRPMDASSLSDSEDSSPEEEEEDKMSSMSLCAWQEKTPHSRPQSSPADRESPFQARTRRLRSLQAQEMILKMKESISERIKFVPVPCGHQDWSEEEEGRTVVPPRPSTVSGSRRAPERQTRSQSESCLQSHVEDPTFQELRRVQRDLSQKLEAFYALGAKGQGQSQEQILQPRAAAVWPNGTCRVSPSNTTSRLKASLTKNFSILPSQDKSILQKCNPHPEDEQGKAGKLPNAIPSGEVSEAAKATDWNVRGCPTRTSVKKLIETFSPTESLRMLGDSKDAGASPCLRNCIMPPRFPKYTGLAPLYPKPQISPASGRESLKMGIGWKPLAPIFPPLPKAEAAKSEELSCEMEGNLEHLPPPPMEVLMDKSFASLESPESSKSTENSPKETQEPGPGEAGPTRRTWASPKLRASVSPLDLLPSKSTASLTKPHSTGPGSGRSSCQPRKPALDLSSPPATSQSPEVKGGTWSQAEKATSLYRQPRKAIAWHHSGPPSGQNRTSESSLARPRQSRERSPPVGRKASPTRTHWVPQADKRRRSLPSSYRPAQPSPSAVQTPPSPPVSPRVLSPPTTKRRTSPPHQPKLPNPPPESAPAQCKVPSPPTQHPEASPPFSIPSPSPPMSPSQEHKETRDSEDSQAVIAKVSGNTHSIFCPATSSLFEAKPPLSTAHPLTPPSLPPEAGGPLGNPAECWKNSSGPWLRADSQRRAALCALNPLPFLRRTASDRQPGGRPQPPTLDPTSTSYESQLGQNSSSEESPKKDTEPGSSPCSPELQGGTRRASPPEFCVLGHGLQPEPRTGHIQDKSQPEAQPQQEEVS | null | null | photoreceptor cell outer segment organization [GO:0035845]; protein localization to photoreceptor outer segment [GO:1903546]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | cilium [GO:0005929]; cone photoreceptor outer segment [GO:0120199]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | null | PF15449; | null | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:20398886}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q6PAC4}. | null | null | null | null | null | FUNCTION: Plays an essential role for normal photoreceptor cell maintenance and vision. {ECO:0000269|PubMed:20398886}. | Homo sapiens (Human) |
A6NGQ2 | OOEP_HUMAN | MVDDAGAAESQRGKQTPAHSLEQLRRLPLPPPQIRIRPWWFPVQELRDPLVFYLEAWLADELFGPDRAIIPEMEWTSQALLTVDIVDSGNLVEITVFGRPRVQNRVKSMLLCLAWFHREHRARAEKMKHLEKNLKAHASDPHSPQDPVA | null | null | actin filament organization [GO:0007015]; embryonic pattern specification [GO:0009880]; establishment of spindle localization [GO:0051293]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of meiotic nuclear division [GO:0045836]; regulation of cell division [GO:0051302]; regulation of establishment of protein localization [GO:0070201]; regulation of protein localization [GO:0032880]; replication fork processing [GO:0031297] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; subcortical maternal complex [GO:0106333] | RNA binding [GO:0003723] | PF16005; | 3.30.1370.10; | KHDC1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25542835}. Nucleus {ECO:0000269|PubMed:25542835}. | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3L scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Positively regulates the homologous recombination-mediated DNA double-strand break (DSB) repair pathway by regulating ATM activation and RAD51 recruitment to DSBs in oocytes (By similarity). Thereby contributes to oocyte survival and the resumption and completion of meiosis (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). {ECO:0000250|UniProtKB:Q9CWE6}. | Homo sapiens (Human) |
A6NGU5 | GGT3_HUMAN | MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTRKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYCAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNMDDFSSPSITNEFGAPPSPANFIQPGKQPLLSMCPTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY | 2.3.2.2; 3.4.19.13 | null | glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; leukotriene D4 biosynthetic process [GO:1901750]; peptide modification [GO:0031179]; proteolysis [GO:0006508]; regulation of immune system process [GO:0002682]; regulation of inflammatory response [GO:0050727] | extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250|UniProtKB:P19440}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}. | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P19440}; | null | PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P19440}. | null | null | FUNCTION: Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. {ECO:0000250|UniProtKB:P19440}. | Homo sapiens (Human) |
A6NHL2 | TBAL3_HUMAN | MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQDQLENAKMEHTNASFDTFFCETRAGKHVPRALFVDLEPTVIDGIRTGQHRSLFHPEQLLSGKEDAANNYARGRYSVGSEVIDLVLERTRKLAEQCGGLQGFLIFRSFGGGTGSGFTSLLMERLTGEYSRKTKLEFSVYPAPRISTAVVEPYNSVLTTHSTTEHTDCTFMVDNEAVYDICHRKLGVECPSHASINRLVVQVVSSITASLRFEGPLNVDLIEFQTNLVPYPRIHFPMTAFAPIVSADKAYHEQFSVSDITTACFESSNQLVKCDPRLGKYMACCLLYRGDVVPKEVNAAIAATKSRHSVQFVDWCPTGFKVGINNRPPTVMPGGDLAKVHRSICMLSNTTAIVEAWARLDHKFDLMYAKRAFLHWYLREGMEEAEFLEAREDLAALERDYEEVAQSF | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P99024, ECO:0000250|UniProtKB:Q71U36}.; PTM: Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363}; | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Homo sapiens (Human) |
A6NHR9 | SMHD1_HUMAN | MAAADGGGPGGASVGTEEDGGGVGHRTVYLFDRREKESELGDRPLQVGERSDYAGFRACVCQTLGISPEEKFVITTTSRKEITCDNFDETVKDGVTLYLLQSVNQLLLTATKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPADSQDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPSDSVHITNDDERFLHHLIIEEKEKDSFTAVVITGVQPEHIQYLKNYFHLWTRQLAHIYHYYIHGPKGNEIRTSKEVEPFNNIDIEISMFEKGKVPKIVNLREIQDDMQTLYVNTAADSFEFKAHVEGDGVVEGIIRYHPFLYDRETYPDDPCFPSKLKDEDDEDDCFILEKAARGKRPIFECFWNGRLIPYTSVEDFDWCTPPKKRGLAPIECYNRISGALFTNDKFQVSTNKLTFMDLELKLKDKNTLFTRILNGQEQRMKIDREFALWLKDCHEKYDKQIKFTLFKGVITRPDLPSKKQGPWATYAAIEWDGKIYKAGQLVKTIKTLPLFYGSIVRFFLYGDHDGEVYATGGEVQIAMEPQALYDEVRTVPIAKLDRTVAEKAVKKYVEDEMARLPDRLSVTWPEGDELLPNEVRPAGTPIGALRIEILNKKGEAMQKLPGTSHGGSKKLLVELKVILHSSSGNKEIISHISQHGGKWPYWFKKMENIQKLGNYTLKLQVVLNESNADTYAGRPLPSKAIKFSVKEGKPEKFSFGLLDLPFRVGVPFNIPLEFQDEFGHTSQLVTDIQPVLEASGLSLHYEEITKGPNCVIRGVTAKGPVNSCQGKNYNLKVTLPGLKEDSQILKIRLLPGHPRRLKVKPDSEILVIENGTAFPFQVEVLDESDNITAQPKLIVHCKFSGAPNLPVYVVDCSSSGTSILTGSAIQVQNIKKDQTLKARIEIPSCKDVAPVEKTIKLLPSSHVARLQIFSVEGQKAIQIKHQDEVNWIAGDIMHNLIFQMYDEGEREINITSALAEKIKVNWTPEINKEHLLQGLLPDVQVPTSVKDMRYCQVSFQDDHVSLESAFTVRPLPDEPKHLKCEMKGGKTVQMGQELQGEVVIIITDQYGNQIQAFSPSSLSSLSIAGVGLDSSNLKTTFQENTQSISVRGIKFIPGPPGNKDLCFTWREFSDFIRVQLISGPPAKLLLIDWPELKESIPVINGRDLQNPIIVQLCDQWDNPAPVQHVKISLTKASNLKLMPSNQQHKTDEKGRANLGVFSVFAPRGEHTLQVKAIYNKSIIEGPIIKLMILPDPEKPVRLNVKYDKDASFLAGGLFTDFMISVISEDDSIIKNINPARISMKMWKLSTSGNRPPANAETFSCNKIKDNDKEDGCFYFRDKVIPNKVGTYCIQFGFMMDKTNILNSEQVIVEVLPNQPVKLVPKIKPPTPAVSNVRSVASRTLVRDLHLSITDDYDNHTGIDLVGTIIATIKGSNEEDTDTPLFIGKVRTLEFPFVNGSAEIMSLVLAESSPGRDSTEYFIVFEPRLPLLSRTLEPYILPFMFYNDVKKQQQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNIDIPTTQQVPHIEALLKRKLSEQEELKKKPRRSCTLPNYTKGSGDVLGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQGRQQVLPLDSIYKKTLPDWKRSLPHFRNGKLYFKPIGDPVFARDLLTFPDNVEHCETVFGMLLGDTIILDNLDAANHYRKEVVKITHCPTLLTRDGDRIRSNGKFGGLQNKAPPMDKLRGMVFGAPVPKQCLILGEQIDLLQQYRSAVCKLDSVNKDLNSQLEYLRTPDMRKKKQELDEHEKNLKLIEEKLGMTPIRKCNDSLRHSPKVETTDCPVPPKRMRREATRQNRIITKTDV | 3.6.1.- | null | chromosome organization [GO:0051276]; dosage compensation by inactivation of X chromosome [GO:0009048]; double-strand break repair [GO:0006302]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; nose development [GO:0043584]; positive regulation of DNA repair [GO:0045739]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034] | Barr body [GO:0001740]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; protein homodimerization activity [GO:0042803] | PF13589;PF06470; | 3.30.565.10; | SMC family | PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q6P5D8}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24790221, ECO:0000269|PubMed:25294876}. Note=Recruited to inactivated chromosome X in females by Xist RNA (By similarity). Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:24790221, PubMed:25294876). {ECO:0000250|UniProtKB:Q6P5D8, ECO:0000269|PubMed:24790221, ECO:0000269|PubMed:25294876}. | 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:0000269|PubMed:29748383}; | null | null | null | null | FUNCTION: Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (By similarity). Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (By similarity). Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin (PubMed:23542155). Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (By similarity). Required to facilitate Xist RNA spreading (By similarity). Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus (PubMed:23143600). Has ATPase activity; may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation (PubMed:29748383). Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks (PubMed:24790221, PubMed:25294876). Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair (PubMed:25294876). {ECO:0000250|UniProtKB:Q6P5D8, ECO:0000269|PubMed:23143600, ECO:0000269|PubMed:23542155, ECO:0000269|PubMed:24790221, ECO:0000269|PubMed:25294876, ECO:0000269|PubMed:29748383}. | Homo sapiens (Human) |
A6NHX0 | CAST2_HUMAN | MELHILEHRLQVASVAKESIPLFTYGLIKLAFLSSKTRCKFFSLTETPEDYTIIVDEEGFLELPSSEHLSVADATWLALNVVSGGGSFSSSQPIGVTKIAKSVIAPLADQNISVFMLSTYQTDFILVRERDLPFVTHTLSSEFTILRVVNGETVAAENLGITNGFVKPKLVQRPVIHPLSSPSNRFCVTSLDPDTLPAVATLLMDVMFYSNGVKDPMATGDDCGHIRFFSFSLIEGYISLVMDVQTQQRFPSNLLFTSASGELWKMVRIGGQPLGFDECGIVAQISEPLAAADIPAYYISTFKFDHALVPEENINGVISALKVSQAEKH | null | null | cellular response to L-arginine [GO:1903577]; negative regulation of TORC1 signaling [GO:1904262] | cytosol [GO:0005829] | identical protein binding [GO:0042802] | PF13840;PF21389;PF18700; | 3.30.2130.10; | GATS family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26972053}. | null | null | null | null | null | FUNCTION: Functions as a negative regulator of the TORC1 signaling pathway through the GATOR complex. As part of homodimers or heterodimers with CASTOR1, directly binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Does not directly bind arginine, but binding of arginine to CASTOR1 disrupts the interaction of CASTOR2-containing heterodimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway. {ECO:0000269|PubMed:26972053}. | Homo sapiens (Human) |
A6NI15 | MSGN1_HUMAN | MDNLRETFLSLEDGLGSSDSPGLLSSWDWKDRAGPFELNQASPSQSLSPAPSLESYSSSPCPAVAGLPCEHGGASSGGSEGCSVGGASGLVEVDYNMLAFQPTHLQGGGGPKAQKGTKVRMSVQRRRKASEREKLRMRTLADALHTLRNYLPPVYSQRGQPLTKIQTLKYTIKYIGELTDLLNRGREPRAQSA | null | null | cell differentiation [GO:0030154]; mesoderm formation [GO:0001707]; regulation of transcription by RNA polymerase II [GO:0006357]; segment specification [GO:0007379]; somitogenesis [GO:0001756] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A6NI61 | MYMK_HUMAN | MGTLVAKLLLPTLSSLAFLPTVSIAAKRRFHMEAMVYLFTLFFVALHHACNGPGLSVLCFMRHDILEYFSVYGTALSMWVSLMALADFDEPKRSTFVMFGVLTIAVRIYHDRWGYGVYSGPIGTAILIIAAKWLQKMKEKKGLYPDKSVYTQQIGPGLCFGALALMLRFFFEDWDYTYVHSFYHCALAMSFVLLLPKVNKKAGSPGTPAKLDCSTLCCACV | null | null | muscle organ development [GO:0007517]; myoblast fusion [GO:0007520]; myoblast fusion involved in skeletal muscle regeneration [GO:0014905]; plasma membrane fusion [GO:0045026]; positive regulation of skeletal muscle hypertrophy [GO:1904206] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | null | PF12036; | null | TMEM8 family | PTM: Palmitoylated at the C-terminus; palmitoylation promotes localization to the Golgi apparatus. {ECO:0000250|UniProtKB:Q9D1N4}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D1N4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D1N4}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D1N4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D1N4}. Note=Localizes on the plasma membrane of myoblasts, where it mediates myoblasts fusion. Also localizes in the Golgi apparatus and post-Golgi following palmitoylation; the role of Golgi localization is unclear. {ECO:0000250|UniProtKB:Q9D1N4}. | null | null | null | null | null | FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers (PubMed:28681861). Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of MYMX. Acts independently of MYMX (By similarity). Involved in skeletal muscle regeneration in response to injury by mediating the fusion of satellite cells, a population of muscle stem cells, with injured myofibers (By similarity). Also involved in skeletal muscle hypertrophy, probably by mediating the fusion of satellite cells with myofibers (By similarity). {ECO:0000250|UniProtKB:Q9D1N4, ECO:0000269|PubMed:28681861}. | Homo sapiens (Human) |
A6NI73 | LIRA5_HUMAN | MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR | null | null | cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of interleukin-13 production [GO:0032696]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cell activation [GO:0050867]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of tumor necrosis factor production [GO:0032760] | cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | inhibitory MHC class I receptor activity [GO:0032396] | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12393390}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:12393390}. | null | null | null | null | null | FUNCTION: May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition. {ECO:0000269|PubMed:16675463}. | Homo sapiens (Human) |
A6NIH7 | U119B_HUMAN | MSGSNPKAAAAASAAGPGGLVAGKEEKKKAGGGVLNRLKARRQAPHHAADDGVGAAVTEQELLALDTIRPEHVLRLSRVTENYLCKPEDNIYSIDFTRFKIRDLETGTVLFEIAKPCVSDQEEDEEEGGGDVDISAGRFVRYQFTPAFLRLRTVGATVEFTVGDKPVSNFRMIERHYFREHLLKNFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSFYFVDNKLIMHNKADYAYNGGQ | null | null | cilium assembly [GO:0060271]; lipoprotein transport [GO:0042953]; nervous system development [GO:0007399] | ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytosol [GO:0005829] | lipid binding [GO:0008289] | PF05351; | 2.70.50.40; | PDE6D/unc-119 family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:22085962}. Note=Enriched at the transition zone and extended into the proximal end of the cilium. | null | null | null | null | null | FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells. {ECO:0000269|PubMed:22085962}. | Homo sapiens (Human) |
A6NIX2 | WTIP_HUMAN | MQRSRAGADEAALLLAGLALRELEPGCGSPGRGRRGPRPGPGDEAAPALGRRGKGSGGPEAGADGLSRGERGPRRAAVPELSAQPAGSPRASLAGSDGGGGGGSARSSGISLGYDQRHGSPRSGRSDPRPGPGPPSVGSARSSVSSLGSRGSAGAYADFLPPGACPAPARSPEPAGPAPFPLPALPLPPGREGGPSAAERRLEALTRELERALEARTARDYFGICIKCGLGIYGAQQACQAMGSLYHTDCFTCDSCGRRLRGKAFYNVGEKVYCQEDFLYSGFQQTADKCSVCGHLIMEMILQALGKSYHPGCFRCSVCNECLDGVPFTVDVENNIYCVRDYHTVFAPKCASCARPILPAQGCETTIRVVSMDRDYHVACYHCEDCGLQLSGEEGRRCYPLAGHLLCRRCHLRRLQPGPLPSPTVHVTEL | null | null | cell projection organization [GO:0030030]; cytoskeleton organization [GO:0007010]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; negative regulation of hippo signaling [GO:0035331]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; regulation of cell morphogenesis [GO:0022604]; regulation of DNA-templated transcription [GO:0006355]; response to hypoxia [GO:0001666] | adherens junction [GO:0005912]; nucleus [GO:0005634]; P-body [GO:0000932]; transcription regulator complex [GO:0005667] | metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction. Nucleus {ECO:0000250}. Cytoplasm, P-body. Note=Following podocyte injury, caused by treatment with LPS, puromycin aminonucleoside, ultraviolet or hydrogen peroxide, translocates from sites of cell-cell contacts into the cytosol and nucleus. The shift from cell contacts to intracellular plaques starts as early as 1 hour after LPS stimulation and intranuclear localization begins 3 hours after LPS treatment. Maximal nuclear localization is achieved 6 hours after LPS treatment. Nuclear translocation requires dynein motor activity and intact microtubule network (By similarity). Returns to cell-cell contacts 24 hours after LPS stimulation. In the presence of ROR2, localizes to the plasma membrane (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo signaling pathway and antagonizes phosphorylation of YAP1. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. In podocytes, may play a role in the regulation of actin dynamics and/or foot process cytoarchitecture (By similarity). In the course of podocyte injury, shuttles into the nucleus and acts as a transcription regulator that represses WT1-dependent transcription regulation, thereby translating changes in slit diaphragm structure into altered gene expression and a less differentiated phenotype. Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:A9LS46, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}. | Homo sapiens (Human) |
A6NJ46 | NKX63_HUMAN | MESNLQGTFLLNNTPLAQFPEMKAPVCQYSVQNSFYKLSPPGLGPQLAAGTPHGITDILSRPVAAPNNSLLSGYPHVAGFGGLSSQGVYYSPQVGNFSKAGNEYPTRTRNCWADTGQDWRGGRQCSNTPDPLSDSIHKKKHTRPTFTGHQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKSALEPSSSTPRAPGGAGAGAGGDRAPSENEDDEYNKPLDPDSDDEKIRLLLRKHRAAFSVLSLGAHSV | null | null | cell differentiation [GO:0030154]; cell fate determination [GO:0001709]; enteroendocrine cell differentiation [GO:0035883]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; 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]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Putative transcription factor, which may be involved in patterning of central nervous system and pancreas. {ECO:0000250}. | Homo sapiens (Human) |
A6NJ78 | MET15_HUMAN | MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSVRQQVMKTSQLGSDHENTEEVSMRRAPLMWELIHKKVLSPQDQDVQDNPRGRSAKLRAAIKL | 2.1.1.- | null | rRNA base methylation [GO:0070475] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | rRNA (cytosine-N4-)-methyltransferase activity [GO:0071424] | PF01795; | 1.10.150.170;3.40.50.150; | Methyltransferase superfamily, RsmH family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}. | CATALYTIC ACTIVITY: Reaction=cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62524, Rhea:RHEA-COMP:16109, Rhea:RHEA-COMP:16110, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; Evidence={ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62525; Evidence={ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}; | null | null | null | null | FUNCTION: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA (PubMed:31665743, PubMed:32371392). Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits (PubMed:31665743, PubMed:32371392). {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}. | Homo sapiens (Human) |
A6NK06 | IRG1_HUMAN | MMLKSITESFATAIHGLKVGHLTDRVIQRSKRMILDTLGAGFLGTTTEVFHIASQYSKIYSSNISSTVWGQPDIRLPPTYAAFVNGVAIHSMDFDDTWHPATHPSGAVLPVLTALAEALPRSPKFSGLDLLLAFNVGIEVQGRLLHFAKEANDMPKRFHPPSVVGTLGSAAAASKFLGLSSTKCREALAIAVSHAGAPMANAATQTKPLHIGNAAKHGIEAAFLAMLGLQGNKQVLDLEAGFGAFYANYSPKVLPSIASYSWLLDQQDVAFKRFPAHLSTHWVADAAASVRKHLVAERALLPTDYIKRIVLRIPNVQYVNRPFPVSEHEARHSFQYVACAMLLDGGITVPSFHECQINRPQVRELLSKVELEYPPDNLPSFNILYCEISVTLKDGATFTDRSDTFYGHWRKPLSQEDLEEKFRANASKMLSWDTVESLIKIVKNLEDLEDCSVLTTLLKGPSPPEVASNSPACNNSITNLS | 4.1.1.6 | null | cellular response to interferon-beta [GO:0035458]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to molecule of bacterial origin [GO:0071219]; cellular response to progesterone stimulus [GO:0071393]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; defense response [GO:0006952]; defense response to virus [GO:0051607]; embryo implantation [GO:0007566]; inflammatory response [GO:0006954]; negative regulation of inflammatory response [GO:0050728]; negative regulation of innate immune response [GO:0045824]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of toll-like receptor 2 signaling pathway [GO:0034136]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]; negative regulation of type I interferon production [GO:0032480]; positive regulation of antimicrobial humoral response [GO:0002760]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; tolerance induction to lipopolysaccharide [GO:0072573] | mitochondrion [GO:0005739] | aconitate decarboxylase activity [GO:0047613]; protein homodimerization activity [GO:0042803] | PF19305;PF03972; | 1.10.4100.10;3.30.1330.120; | PrpD family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P54987}. | CATALYTIC ACTIVITY: Reaction=cis-aconitate + H(+) = CO2 + itaconate; Xref=Rhea:RHEA:15253, ChEBI:CHEBI:15378, ChEBI:CHEBI:16383, ChEBI:CHEBI:16526, ChEBI:CHEBI:17240; EC=4.1.1.6; Evidence={ECO:0000269|PubMed:23610393, ECO:0000269|PubMed:31548418, ECO:0000269|PubMed:35662396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15254; Evidence={ECO:0000269|PubMed:23610393, ECO:0000269|PubMed:31548418, ECO:0000269|PubMed:35662396}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.61 mM for cis-aconitate {ECO:0000269|PubMed:31548418}; Note=kcat is 0.94 sec(-1) for cis-aconitate. {ECO:0000269|PubMed:31548418}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:31548418}; | null | FUNCTION: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response (PubMed:23609450, PubMed:23610393, PubMed:31548418, PubMed:35662396). Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages (PubMed:23609450). Involved in antimicrobial response of innate immune cells; ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages by generating itaconate, leading to alkylation of proteins, such as TFEB (PubMed:23610393, PubMed:35662396). Involved in antiviral response following infection by flavivirus in neurons: ACOD1-mediated itaconate production inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). Plays a role in the embryo implantation (By similarity). {ECO:0000250|UniProtKB:P54987, ECO:0000269|PubMed:23609450, ECO:0000269|PubMed:23610393, ECO:0000269|PubMed:31548418, ECO:0000269|PubMed:35662396}. | Homo sapiens (Human) |
A6NK58 | LIPT2_HUMAN | MRQPAVRLVRLGRVPYAELLGLQDRWLRRLQAEPGIEAPSGTEAGALLLCEPAGPVYTAGLRGGLTPEETARLRALGAEVRVTGRGGLATFHGPGQLLCHPVLDLRRLGLRLRMHVASLEACAVRLCELQGLQDARARPPPYTGVWLDDRKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSKELQRHVTVEEVMPPFLVAFKEIYKCTLISEDSPN | 2.3.1.181 | null | carboxylic acid metabolic process [GO:0019752]; positive regulation of oxygen metabolic process [GO:2000376]; protein lipoylation [GO:0009249] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ligase activity [GO:0016874]; lipoyl(octanoyl) transferase activity [GO:0033819] | null | null | LipB family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28628643, ECO:0000269|PubMed:28757203}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; Evidence={ECO:0000250|UniProtKB:Q9D009}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17666; Evidence={ECO:0000250|UniProtKB:Q9D009}; | null | PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. | null | null | FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein (octanoyl-ACP) onto the lipoyl domains of lipoate-dependent enzymes such as the protein H of the glycine cleavage system (GCSH) (PubMed:28757203). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). {ECO:0000250|UniProtKB:Q9D009, ECO:0000269|PubMed:28757203}. | Homo sapiens (Human) |
A6NK89 | RASFA_HUMAN | MDPSEKKISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRLGSAGDPHGPGELPEPPNEDDEDDDEALPQGMLCGPPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEASLPNAGPRSAEARVVLSRERPCPARGAPARPSLAMTQEKQRRVVRKAFRKLAKLNRRRQQQTPSSCSSTSSSTASSCSSSPRTHESASVERMETLVHLVLSQDHTIRQQVQRLHELDREIDHYEAKVHLDRMRRHGVNYVQDTYLVGAGIELDGSRPGEEPEEVAAEAEEAAAAPPLAGEAQAAALEELARRCDDLLRLQEQRVQQEELLERLSAEIQEELNQRWMRRRQEELAAREEPLEPDGGPDGELLLEQERVRTQLSTSLYIGLRLNTDLEAVKSDLDYSQQQWDSKKRELQGLLQTLHTLELTVAPDGAPGSGSPSREPGPQACADMWVDQARGLAKSGPGNDEDSDTGLSSMHSQDSDSLPMCESLV | null | null | nervous system development [GO:0007399]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neurogenesis [GO:0050769]; signal transduction [GO:0007165] | centrosome [GO:0005813]; cytosol [GO:0005829]; spindle pole [GO:0000922] | null | PF21712; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20956940}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20956940}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20956940}. Note=During interphase, predominantly cytoplasmic, although some nuclear staining in several tumor cell contexts. During prophase, observed at developing centrosomes. Displays persistent localization with centrosomally radiating microtubule bundles until late telophase. Associates with spindle poles particularly during metaphase and anaphase before relocating back to the cytoplasm. | null | null | null | null | null | FUNCTION: Plays an important role in regulating embryonic neurogenesis. {ECO:0000250|UniProtKB:Q8BL43}. | Homo sapiens (Human) |
A6NKB5 | PCX2_HUMAN | MVSQVLQLLRQGVWAALTGGWYHDPEQSKFTNSCHLYLWLFLLLLPLALHLAFPPNAIIVFFYCSAVTIFFTIIKLVSYRLHLMFDKGEVIQQKPSRKEEKPNKDKEAKGEHITNHRNPSNNRQIHNGKKEEASRNLSTPPLRCSSRGQSITSHHSSGPLELSAQETVEDLKGVILLEDHPIAPVSSTSPGIKVESLPASQAHMLETTTKSVIPVKPVATETLINGKGKERGGKGQPPLRHRSEGGLVDKGPLKKLPHLSLSQYDLLETDVSFQPWGSENSVLIPEPVSCPRGSIRERVQSKSPQDSLSSSCPQCDTIVAKPVEEPADTSCQVDTSCQGDLPLHQEVDSSDSEVAVTLIDTSQPGDPLSLHEPIKIVITMSSTPNSMTDLESSLHLRVVGTEKTSVKSDAEPTNPGAAGSPNAEQISIPVITLDLPEGGGGGVPCPEGNGSERTPERLKTRVSTNQCSGYGSGEGGNAIKDHSSSSREPWESVSRLTPDTGSESKVGKEGQTNLDPSSCKSSHEKRHARVLSVDSGTDVFLSKSSAEIVNDTEKTMPTSKSDLEAKEGQMPNESNFLEFVSLLESINTSKMTASSQLNGSAEQNEESGLLRDNCSQEKKEEILENEKPSGHSSKQGKPDLQSQDHTSTGPACTQPAKTTAFFQGNRQRQIIYRVTSQQDSSVLQVISGPETSVQEEISVDAMHVFIDEHGEIRSCYLKSGNQKEGPLQPLPSNNDCLSQAREMQVSSSSTTTSESQDPSSGDPAVSALQQQLLLMVARRTQSETPRHVSQDLEASSCSSTQGKFNREQFYKFIIFPGKWIKVWYDRLTLLALLDRTEDIKENVLAILLIVLVSLLGFLTLSQGFCKDMWVLLFCLVMASCQYSLLKSVQPDPASPIHGHNQIITYSRPIYFCVLCGLILLLDTGAKARHPPSYVVYGLKLFSPVFLQSARDYLIVFLYCFPAISLLGLFPQINTFCTYLLEQIDMLFFGGSAVSGITSAVYSVARSVLAAALLHAVCFSAVKEPWSMQHIPALFSAFCGLLVALSYHLSRQSSDPSVLMSFIQCRLFPKFLHQNLAESAADPLPKKMKDSVTDVLKWDLIVCAVVAVLSFAVSASTVFLSLRPFLSIVLFALAGAVGFVTHYVLPQLRKHHPWMWISHPILKNKEYHQREVRDVAHLMWFERLYVWLQCFEKYILYPALILNALTIDAFLISNHRRLGTHWDIFLMIIAGMKLLRTSFCNPVYQFINLSFTVIFFHFDYKDISESFLLDFFMVSILFSKLGDLLHKLQFVLTYVAPWQMAWGSSFHVFAQLFAIPHSAMLFFQTIATSIFSTPLSPFLGSVIFITSYVRPVKFWEKNYNTRRVDNSNTRLAVQIERDPGNDDNNLNSIFYEHLTRTLQESLCGDLVLGRWGNYSSGDCFILASDDLNAFVHLIEIGNGLVTFQLRGLEFRGTYCQQREVEAIMEGDEEDRGCCCCKPGHLPHLLSCNAAFHLRWLTWEITQTQYILEGYSILDNNAATMLQVFDLRRILIRYYIKSIIYYMVTSPKLLSWIKNESLLKSLQPFAKWHYIERDLAMFNINIDDDYVPCLQGITRASFCNVYLEWIQHCARKRQEPSTTLDSDEDSPLVTLSFALCTLGRRALGTAAHNMAISLDSFLYGLHVLFKGDFRITARDEWVFADMDLLHKVVAPAIRMSLKLHQDQFTCPDEYEDPAVLYEAIQSFEKKVVICHEGDPAWRGAVLSNKEELLTLRHVVDEGADEYKVIMLHRSFLSFKVIKVNKECVRGLWAGQQQELIFLRNRNPERGSIQNNKQVLRNLINSSCDQPLGYPMYVSPLTTSYLGTHRQLKNIWGGPITLDRIRTWFWTKWVRMRKDCNARQHSGGNIEDVDGGGAPTTGGNNAPSGGSQESSAEQPRKGGAQHGVSSCEGTQRTGRRKGRSQSVQAHSALSQRPPMLSSSGPILESRQTFLQTSTSVHELAQRLSGSRLSLHASATSLHSQPPPVTTTGHLSVRERAEALIRSSLGSSTSSTLSFLFGKRSFSSALVISGLSAAEGGNTSDTQSSSSVNIVMGPSARAASQATRHLSEPCEPPDATEQGQLHDRCLAEAVADTLGVVCRRASQEDMGLDDTASQQSVSDEQ | null | null | null | membrane [GO:0016020] | null | PF05041; | null | Pecanex family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May play a role in tumorigenesis of colorectal carcinomas with high microsatellite instability (MSI-H). {ECO:0000269|PubMed:12140758, ECO:0000269|PubMed:14507650}. | Homo sapiens (Human) |
A6NMY6 | AXA2L_HUMAN | MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNIVTNRDNAQRQDIVFSYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDAQDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQRIQNKPLYFADQLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD | null | null | positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602] | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; protease binding [GO:0002020]; virion binding [GO:0046790] | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane. In melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. {ECO:0000250}. | Homo sapiens (Human) |
A6NMZ7 | CO6A6_HUMAN | MMLLILFLVIICSHISVNQDSGPEYADVVFLVDSSDRLGSKSFPFVKMFITKMISSLPIEADKYRVALAQYSDKLHSEFHLSTFKGRSPMLNHLRKNFGFIGGSLQIGKALQEAHRTYFSAPANGRDKKQFPPILVVLASSESEDNVEEASKALRKDGVKIISVGVQKASEENLKAMATSQFHFNLRTVRDLSMFSQNMTHIIKDVIKYKEGAVDDIFVEACQGPSMADVVFLLDMSINGSEENFDYLKGFLEESVSALDIKENCMRVGLVAYSNETKVINSLSMGINKSEVLQHIQNLSPRTGKAYTGAAIKKLRKEVFSARNGSRKNQGVPQIAVLVTHRDSEDNVTKAAVNLRREGVTIFTLGIEGASDTQLEKIASHPAEQYVSKLKTFADLAAHNQTFLKKLRNQITHTVSVFSERTETLKSGCVDTEEADIYLLIDGSGSTQATDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADSWDLEFEINKYSNKQDLGKAIENIRQMGGNTNTGAALNFTLSLLQKAKKQRGNKVPCHLVVLTNGMSKDSILEPANRLREEHIRVYAIGIKEANQTQLREIAGEEKRVYYVHDFDALKDIRNQVVQEICTEEACKEMKADIMFLVDSSGSIGPENFSKMKTFMKNLVSKSQIGPDRVQIGVVQFSDINKEEFQLNRFMSQSDISNAIDQMAHIGQTTLTGSALSFVSQYFSPTKGARPNIRKFLILITDGEAQDIVKEPAVVLRQEGVIIYSVGVFGSNVTQLEEISGRPEMVFYVENFDILQRIEDDLVFGICSPREECKRIEVLDVVFVIDSSGSIDYDEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDDFGTKLEVISVLQNDQAMGGSTYTAEALGFSDHMFTEARGSRLNKGVPQVLIVITDGESHDADKLNATAKALRDKGILVLAVGIDGANPVELLAMAGSSDKYFFVETFGGLKGIFSDVTASVCNSSKVDCEIDKVDLVFLMDGSTSIQPNDFKKMKEFLASVVQDFDVSLNRVRIGAAQFSDTYHPEFPLGTFIGEKEISFQIENIKQIFGNTHIGAALREVEHYFRPDMGSRINTGTPQVLLVLTDGQSQDEVAQAAEALRHRGIDIYSVGIGDVDDQQLIQITGTAEKKLTVHNFDELKKVNKRIVRNICTTAGESNCFVDVVVGFDVSTQEKGQTLLEGQPWMETYLQDILRAISSLNGVSCEVGTETQVSVAFQVTNAMEKYSPKFEIYSENILNSLKDITVKGPSLLNANLLDSLWDTFQNKSAARGKVVLLFSDGLDDDVEKLEQKSDELRKEGLNALITVALDGPADSSDLADLPYIEFGKGFEYRTQLSIGMRELGSRLSKQLVNVAERTCCCLFCKCIGGDGTMGDPGPPGKRGPPGFKGSEGYLGEEGIAGERGAPGPVGEQGTKGCYGTKGPKGNRGLNGQEGEVGENGIDGLNGEQGDNGLPGRKGEKGDEGSQGSPGKRGTPGDRGAKGLRGDPGAPGVDSSIEGPTGLKGERGRQGRRGWPGPPGTPGSRRKTAAHGRRGHTGPQGTAGIPGPDGLEGSLGLKGPQGPRGEAGVKGEKGGVGSKGPQGPPGPGGEAGNQGRLGSQGNKGEPGDLGEKGAVGFPGPRGLQGNDGSPGYGSVGRKGAKGQEGFPGESGPKGEIGDPGGPGETGLKGARGKMISAGLPGEMGSPGEPGPPGRKGVKGAKGLASFSTCELIQYVRDRSPGRHGKPECPVHPTELVFALDHSRDVTEQEFERMKEMMAFLVRDIKVRENSCPVGAHIAILSYNSHARHLVRFSDAYKKSQLLREIETIPYERSSASREIGRAMRFISRNVFKRTLPGAHTRKIATFFSSGQSADAHSITTAAMEFGALEIIPVVITFSNVPSVRRAFAIDDTGTFQVIVVPSGADYIPALERLQRCTFCYDVCKPDASCDQARPPPVQSYMDAAFLLDASRNMGSAEFEDIRAFLGALLDHFEITPEPETSVTGDRVALLSHAPPDFLPNTQKSPVRAEFNLTTYRSKRLMKRHVHESVKQLNGDAFIGHALQWTLDNVFLSTPNLRRNKVIFVISAGETSHLDGEILKKESLRAKCQGYALFVFSLGPIWDDKELEDLASHPLDHHLVQLGRIHKPDHSYGVKFVKSFINSIRRAINKYPPINLKIKCNRLNSIDPKQPPRPFRSFVPGPLKATLKEDVLQKAKFFQDKKYLSRVARSGRDDAIQNFMRSTSHTFKNGRMIESAPKQHD | null | null | cell adhesion [GO:0007155] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391;PF00092; | 1.20.5.320;3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Deposed in the extracellular matrix of skeletal muscle. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. | Homo sapiens (Human) |
A6NNB3 | IFM5_HUMAN | MDTAYPREDTRAPTPSKAGAHTALTLGAPHPPPRDHLIWSVFSTLYLNLCCLGFLALAYSIKARDQKVVGDLEAARRFGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLARLAKDSAAFFSTKFDDADYD | null | null | bone mineralization [GO:0030282]; bone morphogenesis [GO:0060349]; in utero embryonic development [GO:0001701]; regulation of bone mineralization [GO:0030500] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | null | PF04505; | null | CD225/Dispanin family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:O88728}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24519609}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:24519609}. | Homo sapiens (Human) |
A6NNM8 | TTL13_HUMAN | MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIWLQEHSYNPGELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLNGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSCLDQEVKDALLCDAMTLVNLRGCDKRKVMEEDKRRVKERLFQCYRQPRESRKEKTESSHVAMLDQERYEDSHLGKYRRIYPGPDTEKYARFFKHNGSLFQETAASKAREECARQQLEEIRLKQEQQETSGTKRQKARDQNQGESAGEKSRPRAGLQSLSTHLAYRNRNWEKELLPGQLDTMRPQEIVEEEELERMKALLQRETLIRSLGIVEQLTRLQHPGPQGQKKLHESRDRLGSQELKSMSLVLLVLLRGAATEQGAPHFLHPVLPHESIPRILGALPSMNAAIPHVPRYHLQPKNFNWTGEPAAINSCSLSMKKAGRCYFSSARIRLTSQGQASRRLEAINRVLAGSVPPTLTPKQGYFLQPERVASDSWTECTLPSMVNSEHRAAKVPLCPASAPMLQRSRALLNINQFR | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | microtubule cytoskeleton organization [GO:0000226]; protein modification process [GO:0036211] | cilium [GO:0005929]; cytosol [GO:0005829]; microtubule [GO:0005874] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | null | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:A4Q9F6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000250|UniProtKB:A4Q9F6}; | null | null | null | null | FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates ATP-dependent polyglutamate side-chain elongation of the polyglutamylation reaction but not the initiation step. Preferentially modifies the alpha-tubulin tail over a beta-tail. {ECO:0000250|UniProtKB:A4Q9F6}. | Homo sapiens (Human) |
A6NNN8 | S38A8_HUMAN | MEGQTPGSRGLPEKPHPATAAATLSSMGAVFILMKSALGAGLLNFPWAFSKAGGVVPAFLVELVSLVFLISGLVILGYAAAVSGQATYQGVVRGLCGPAIGKLCEACFLLNLLMISVAFLRVIGDQLEKLCDSLLSGTPPAPQPWYADQRFTLPLLSVLVILPLSAPREIAFQKYTSILGTLAACYLALVITVQYYLWPQGLVRESHPSLSPASWTSVFSVFPTICFGFQCHEAAVSIYCSMRKRSLSHWALVSVLSLLACCLIYSLTGVYGFLTFGTEVSADVLMSYPGNDMVIIVARVLFAVSIVTVYPIVLFLGRSVMQDFWRRSCLGGWGPSALADPSGLWVRMPLTILWVTVTLAMALFMPDLSEIVSIIGGISSFFIFIFPGLCLICAMGVEPIGPRVKCCLEVWGVVSVLVGTFIFGQSTAAAVWEMF | null | null | amino acid transmembrane transport [GO:0003333] | axon [GO:0030424]; cell cortex [GO:0005938]; membrane [GO:0016020] | L-amino acid transmembrane transporter activity [GO:0015179] | PF01490; | null | Amino acid/polyamine transporter 2 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q5HZH7}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q5HZH7}. Cell projection, axon {ECO:0000250|UniProtKB:Q5HZH7}. | CATALYTIC ACTIVITY: Reaction=L-glutamine(out) = L-glutamine(in); Xref=Rhea:RHEA:73419, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-histidine(out) = L-histidine(in); Xref=Rhea:RHEA:72807, ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-aspartate(out) = L-aspartate(in); Xref=Rhea:RHEA:66332, ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-leucine(in) = L-leucine(out); Xref=Rhea:RHEA:73011, ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; | null | null | null | null | FUNCTION: Electrogenic sodium-dependent amino acid transporter with a preference for L-glutamine, L-alanine, L-histidine, L-aspartate and L-arginine. May facilitate glutamine uptake in both excitatory and inhibitory neurons. The transport mechanism and stoichiometry remain to be elucidated. {ECO:0000250|UniProtKB:Q5HZH7}. | Homo sapiens (Human) |
A6NNY8 | UBP27_HUMAN | MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEHESEKVKEMNTQAY | 3.4.19.12 | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of apoptotic process [GO:0043065]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; proteolysis [GO:0006508] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578] | PF00443; | 3.90.70.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CEG8}. Nucleus {ECO:0000250|UniProtKB:Q8CEG8}. | 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:31534008, ECO:0000269|PubMed:32027733}; | null | null | null | null | FUNCTION: Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and RIGI (PubMed:31534008, PubMed:32027733). Negatively regulates RIGI by mediating 'Lys-63'-linked deubiquitination of RIGI, inhibiting type I interferon signaling (PubMed:32027733). Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1 (PubMed:32027733). Acts as a positive regulator of the cGAS-STING pathway by catalyzing 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization (PubMed:31534008). Can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal (By similarity). By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity (By similarity). {ECO:0000250|UniProtKB:Q8CEG8, ECO:0000269|PubMed:31534008, ECO:0000269|PubMed:32027733}. | Homo sapiens (Human) |
A6NNZ2 | TBB8B_HUMAN | MREIVLTQTGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVHHHEASGGRYVPRAVLVDLEPGTMDSVHSGPFGQVFRPDNFISGQCGAGNNWAKGRYTEGAELTESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSRTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGCYLTVAAIFRGRMPMREVDEQMFNIQDKNSSYFADWFPDNVKTAVCDIPPRGLKMSATFIGNNAAIQELFTCVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intercellular bridge [GO:0045171]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P99024, ECO:0000269|PubMed:26875866}.; PTM: Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437, ECO:0000305|PubMed:19524510}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000269|PubMed:16371510}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Homo sapiens (Human) |
A6P320 | MARHB_RAT | MSDEGSKRGSRADSLEAEPPLPPPPPPPPPGESSLVPTSPRYRPPLPAPLERIVGSGEPPVELAPRRKGEPLPPLPPSRLPGDQEVSAAGDSCEGPRRLPEVKLPEAAAGKGSPAEPEAGACREGERRGTGDQPETRSVYSSRSSSSGGSGDQRSGHQHQHHQPICKICFQGAEQGELLNPCRCDGSVRYTHQLCLLKWISERGSWTCELCCYRYHVTAIKMKQPCQWQSISITLVEKVQMIAVILGSLFLIASVTWLLWSAFSPYAVWQRKDILFQICYGMYGFMDLVCIGLIVHEGAAVYRVFKRWRAVNLHWDVLNYDKATDIEESSRGESSTSRTLWLPLSALRNRNLVHPTQLTSPRFQCGYVLLHLFNRMRAHEDVSEDNGSGEVVMRVTSV | 2.3.2.27 | null | protein ubiquitination [GO:0016567] | cytoplasmic vesicle membrane [GO:0030659] | ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF12906; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17604280}; Multi-pass membrane protein {ECO:0000269|PubMed:17604280}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids. {ECO:0000269|PubMed:17604280}. | Rattus norvegicus (Rat) |
A6P3B2 | FMRF_MUSDO | MVAPLLVFLFSLQLCHTTSWAYVGGNSLNSNSLHASYSEFPAGTSNEVPEDAANGQDDNDDSQLTEPNDNNAPLVQSIDDETEMQFPKPIQWVSIDHLRNSIILRFQNPTPKILNKLDPEEMKRLRSLQENAMRWGKRSYESYPLNRNGLADKSSVGRMGFLSNHQVIRDSRGDNFMRFGRSVGGSGGNDDNFMRFGRASGSSDFMRFGRAGQDNFMRFGRAAGQDFMRFGRGSGQDFMRFGRSPGSQDFMRFGRNPGSQDFMRFGRSPGSQDFMRFGRNPGSQDFMRFGRNPGSQDFMRFGRNPGSQDFMRFGRASGGQDFMRFGRAPSGQDFMRFGRPDNFMRFGRTPAQSSDFMRFGRTPTQSSDFMRFGKSLDKSENKTSDLQK | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular region [GO:0005576] | null | PF01581; | null | FARP (FMRFamide related peptide) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | null | Musca domestica (House fly) |
A6P6V9 | CBDAS_CANSA | MKCSTFSFWFVCKIIFFFFSFNIQTSIANPRENFLKCFSQYIPNNATNLKLVYTQNNPLYMSVLNSTIHNLRFTSDTTPKPLVIVTPSHVSHIQGTILCSKKVGLQIRTRSGGHDSEGMSYISQVPFVIVDLRNMRSIKIDVHSQTAWVEAGATLGEVYYWVNEKNENLSLAAGYCPTVCAGGHFGGGGYGPLMRNYGLAADNIIDAHLVNVHGKVLDRKSMGEDLFWALRGGGAESFGIIVAWKIRLVAVPKSTMFSVKKIMEIHELVKLVNKWQNIAYKYDKDLLLMTHFITRNITDNQGKNKTAIHTYFSSVFLGGVDSLVDLMNKSFPELGIKKTDCRQLSWIDTIIFYSGVVNYDTDNFNKEILLDRSAGQNGAFKIKLDYVKKPIPESVFVQILEKLYEEDIGAGMYALYPYGGIMDEISESAIPFPHRAGILYELWYICSWEKQEDNEKHLNWIRNIYNFMTPYVSKNPRLAYLNYRDLDIGINDPKNPNNYTQARIWGEKYFGKNFDRLVKVKTLVDPNNFFRNEQSIPPLPRHRH | 1.21.3.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8GTB6}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000250|UniProtKB:Q8GTB6}; | cannabinoid biosynthetic process [GO:1901696]; terpenoid biosynthetic process [GO:0016114] | apoplast [GO:0048046] | cannabidiolate synthase activity [GO:0102779]; FAD binding [GO:0071949] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | PTM: Glycosylated. {ECO:0000269|PubMed:17544411}.; PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:Q8GTB6}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8663284}. Secreted, extracellular space, apoplast {ECO:0000250}. Note=Probably sorted from the secretory cells into the storage cavity of glandular trichomes. | CATALYTIC ACTIVITY: Reaction=cannabigerolate + O2 = cannabidiolate + H2O2; Xref=Rhea:RHEA:34411, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:66962, ChEBI:CHEBI:67136; EC=1.21.3.8; Evidence={ECO:0000269|PubMed:17544411, ECO:0000269|PubMed:8663284}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34412; Evidence={ECO:0000269|PubMed:17544411, ECO:0000269|PubMed:8663284}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.137 mM for cannabigerolic acid {ECO:0000269|PubMed:8663284}; KM=0.206 mM for cannabinerolic acid {ECO:0000269|PubMed:8663284}; Vmax=2.57 nmol/sec/mg enzyme with cannabigerolic acid as substrate {ECO:0000269|PubMed:8663284}; Vmax=0.39 nmol/sec/mg enzyme with cannabinerolic acid as substrate {ECO:0000269|PubMed:8663284}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:8663284}; | null | FUNCTION: Oxidoreductase involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:17544411, PubMed:8663284). Catalyzes the stereoselective oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA), producing cannabidiolate (CBDA), the major cannabioid in fiber-type Cannabis plants (PubMed:17544411, PubMed:8663284). Can also use cannabinerolic acid as substrate, but not cannabigerol or cannabinerol (PubMed:17544411, PubMed:8663284). {ECO:0000269|PubMed:17544411, ECO:0000269|PubMed:8663284}. | Cannabis sativa (Hemp) (Marijuana) |
A6P7H6 | FGF13_XENLA | MAAAIASSLIRQKRQAREREKSNACKCVSSPSKSKGNCEKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQPDGTIDGAKEEESSATVFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQQHSGRSWFLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSQNDST | null | null | establishment of neuroblast polarity [GO:0045200]; head development [GO:0060322]; inhibitory synapse assembly [GO:1904862]; microtubule polymerization [GO:0046785]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of microtubule depolymerization [GO:0007026]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; positive regulation of voltage-gated sodium channel activity [GO:1905152]; protein localization to plasma membrane [GO:0072659]; regulation of ERK5 cascade [GO:0070376] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; microtubule [GO:0005874]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | beta-tubulin binding [GO:0048487]; growth factor activity [GO:0008083]; microtubule binding [GO:0008017]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250|UniProtKB:P70377}. Cell projection, growth cone {ECO:0000250|UniProtKB:P70377}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70377}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P70377}. Cytoplasm {ECO:0000250|UniProtKB:P70377}. Note=Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes. {ECO:0000250|UniProtKB:P70377}. | null | null | null | null | null | FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Plays a crucial role in neuron polarization and migration (By similarity). Regulates voltage-gated sodium channel transport and function (By similarity). Required for proper head development, it is involved in neural differentiation through regulation of the mek5-erk5 pathway (PubMed:17584734). {ECO:0000250|UniProtKB:P70377, ECO:0000269|PubMed:17584734}. | Xenopus laevis (African clawed frog) |
A6PVC2 | TTLL8_HUMAN | MEPERKGLSLASSSDGDGREENKLKQGISQDLASSSRLDRYKIARQLTEKAIKEKKIFSIYGHYPVVRAALRRKGWVEKKFHFLPKVIPDVEDEGARVNDDTCAKVKENQEMALEKTDNIHDVMSRLVKNEMPYLLWTIKRDIIDYHSLTYDQMLNHYAKTASFTTKIGLCVNMRSLPWYVPANPDSFFPRCYSLCTESEQQEFLEDFRRTMASSILKWVVSHQSCSRSSRSKPRDQREEAGSSDLSSRQDAENAEAKLRGLPGQLVDIACKVCQAYLGQLEHEDIDTSADAVEDLTEAEWEDLTQQYYSLVHGDAFISNSRNYFSQCQALLNRITSVNPQTDIDGLRNIWIIKPAAKSRGRDIVCMDRVEEILELAAADHPLSRDNKWVVQKYIETPLLICDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNAVQKYLKNDVGRSPLLPAHNMWTSTRFQEYLQRQGRGAVWGSVIYPSMKKAIAHAMKVAQDHVEPRKNSFELYGADFVLGRDFRPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVAVDRSCDIGNFELLWRQPVVEPPPFSGSDLCVAGVSVRRARRQVLPVCNLKASASLLDAQPLKARGPSAMPDPAQGPPSPALQRDLGLKEEKGLPLALLAPLRGAAESGGAAQPTRTKAAGKVELPACPCRHVDSQAPNTGVPVAQPAKSWDPNQLNAHPLEPVLRGLKTAEGALRPPPGGKGEGTVCSRLPHHGHHVAACQTTGTTWDGGPGVCFLRQLLASELPMGPGLPRDPRAPPCLVCRGLLPPAGPCKRCRSFCAAVLQGASFVRLGGRSCSPRTP | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9F1}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9F1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9F1}. | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:A4Q9F1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181; Evidence={ECO:0000250|UniProtKB:A4Q9F1}; | null | null | null | null | FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine to the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferentially monoglycylates alpha-tubulin over beta-tubulin. Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility. Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1. {ECO:0000250|UniProtKB:A4Q9F1}. | Homo sapiens (Human) |
A6Q0K5 | CP12_CHLRE | MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED | null | null | negative regulation of reductive pentose-phosphate cycle [GO:0080153]; positive regulation of protein-containing complex assembly [GO:0031334]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507]; protein-containing complex [GO:0032991]; supramolecular complex [GO:0099080] | copper ion binding [GO:0005507]; enzyme binding [GO:0019899]; molecular adaptor activity [GO:0060090]; nickel cation binding [GO:0016151] | PF02672; | null | CP12 family | PTM: Contains two disulfide bonds; only the oxidized protein, with two disulfide bonds, is active in complex formation. | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. {ECO:0000269|PubMed:12846565}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A6QEK3 | HCHA_STAAE | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGINREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Staphylococcus aureus (strain Newman) |
A6QEP0 | CHDC_STAAE | MSQAAETLDGWYSLHLFYAVDWASLRIVPKDERDALVTEFQSFLENTATVRSSKSGDQAIYNITGQKADLLLWFLRPEMKSLNHIENEFNKLRIADFLIPTYSYVSVIELSNYLAGKSDEDPYENPHIKARLYPELPHSDYICFYPMNKRRNETYNWYMLTMEERQKLMYDHGMIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFFVGHIINTNEFDQFFAIS | 1.3.98.5 | COFACTOR: Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:27936663}; Note=Fe-coproporphyrin III acts both as a substrate and redox cofactor (Probable). Was originally thought to use heme as a cofactor (PubMed:23737523). {ECO:0000269|PubMed:23737523, ECO:0000305|PubMed:27936663}; | heme biosynthetic process [GO:0006783] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF06778; | null | ChdC family, Type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b; Xref=Rhea:RHEA:56516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344, ChEBI:CHEBI:68438; EC=1.3.98.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; CATALYTIC ACTIVITY: Reaction=Fe-coproporphyrin III + H(+) + H2O2 = CO2 + 2 H2O + harderoheme III; Xref=Rhea:RHEA:57940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:68438, ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + harderoheme III = CO2 + 2 H2O + heme b; Xref=Rhea:RHEA:57944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344, ChEBI:CHEBI:142463; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663}; | null | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:23737523, ECO:0000305|PubMed:26083961}. | null | null | FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:26083961). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:26083961, PubMed:27936663, PubMed:27982566). The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (PubMed:26083961, PubMed:27936663, PubMed:27982566). The first decarboxylation step is fast and yields the three-propionate harderoheme isomer III intermediate, while the slower second decarboxylation appears to control the overall rate. H(2)O(2) is the assumed biological oxidant, but either H(2)O(2) or peracetic acid yields the same intermediates and products (PubMed:26083961). Has weak peroxidase and catalase activities in vitro (PubMed:23737523). {ECO:0000269|PubMed:23737523, ECO:0000269|PubMed:26083961, ECO:0000269|PubMed:27936663, ECO:0000269|PubMed:27982566}. | Staphylococcus aureus (strain Newman) |
A6QG31 | ISDA_STAAE | MTKHYLNSKYQSEQRSSAMKKITMGTASIILGSLVYIGADSQQVNAATEATNATNNQSTQVSQATSQPINFQVQKDGSSEKSHMDDYMQHPGKVIKQNNKYYFQTVLNNASFWKEYKFYNANNQELATTVVNDNKKADTRTINVAVEPGYKSLTTKVHIVVPQINYNHRYTTHLEFEKAIPTLADAAKPNNVKPVQPKPAQPKTPTEQTKPVQPKVEKVKPTVTTTSKVEDNHSTKVVSTDTTKDQTKTQTAHTVKTAQTAQEQNKVQTPVKDVATAKSESNNQAVSDNKSQQTNKVTKHNETPKQASKAKELPKTGLTSVDNFISTVAFATLALLGSLSLLLFKRKESK | null | null | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872] | PF00746;PF05031; | 2.60.40.1850; | IsdA family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:19398548}; Peptidoglycan-anchor {ECO:0000305}. Note=Encodes an LPXTG motif-containing sorting signal that targets to the cell wall, which is catalyzed by sortase A. {ECO:0000305|PubMed:12574635}. | null | null | null | null | null | FUNCTION: Cell wall-anchored surface receptor that participates in the extraction of heme from oxidized methemoglobin/metHb to enable growth on hemoglobin as a sole iron source (PubMed:12574635, PubMed:17229211). Receives heme from IsdB and transfers it to IsdC (By similarity). Plays also a role in the inhibition of host immune response (PubMed:18005699, PubMed:18097052, PubMed:18227165). Protects S.aureus against the bactericidal protease activity of apolactoferrin (PubMed:18097052). Decreases bacterial cellular hydrophobicity, which renders S.aureus resistant to bactericidal human skin fatty acids as well as to beta-defensins and cathelicidin (PubMed:18005699). Also binds fibronectin and chains B-beta and gamma of fibrinogen, promoting clumping of S.aureus with fibrinogen. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization. {ECO:0000250|UniProtKB:Q7A152, ECO:0000269|PubMed:12574635, ECO:0000269|PubMed:17229211, ECO:0000269|PubMed:18005699, ECO:0000269|PubMed:18097052, ECO:0000269|PubMed:18227165}. | Staphylococcus aureus (strain Newman) |
A6QGC0 | PRKC_STAAE | MIGKIINERYKIVDKLGGGGMSTVYLAEDTILNIKVAIKAIFIPPREKEETLKRFEREVHNSSQLSHQNIVSMIDVDEEDDCYYLVMEYIEGPTLSEYIESHGPLSVDTAINFTNQILDGIKHAHDMRIVHRDIKPQNILIDSNKTLKIFDFGIAKALSETSLTQTNHVLGTVQYFSPEQAKGEATDECTDIYSIGIVLYEMLVGEPPFNGETAVSIAIKHIQDSVPNVTTDVRKDIPQSLSNVILRATEKDKANRYKTIQEMKDDLSSVLHENRANEDVYELDKMKTIAVPLKKEDLAKHISEHKSNQPKRETTQVPIVNGPAHHQQFQKPEGTVYEPKPKKKSTRKIVLLSLIFSLLMIALVSFVAMAMFGNKYEETPDVIGKSVKEAEQIFNKNNLKLGKISRSYSDKYPENEIIKTTPNTGERVERGDSVDVVISKGPEKVKMPNVIGLPKEEALQKLKSLGLKDVTIEKVYNNQAPKGYIANQSVTANTEIAIHDSNIKLYESLGIKQVYVEDFEHKSFSKAKKALEEKGFKVESKEEYSDDIDEGDVISQSPKGKSVDEGSTISFVVSKGKKSDSSDVKTTTESVDVPYTGKNDKSQKVKVYIKDKDNDGSTEKGSFDITSDQRIDIPLRIEKGKTASYIVKVDGKTVAEKEVSYDDV | 2.7.11.1 | null | cellular response to peptidoglycan [GO:0071224]; negative regulation of collateral sprouting [GO:0048671]; positive regulation of autophagy [GO:0010508]; protein phosphorylation [GO:0006468]; response to starvation [GO:0042594]; signal transduction [GO:0007165]; spore germination [GO:0009847] | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; peptidoglycan binding [GO:0042834]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03793;PF00069;PF21160; | 2.60.40.2560;3.30.10.20;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Spore membrane; Single-pass type II membrane protein. Note=Is associated with the inner membrane of the spore. {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: Probable protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate) or L-lys, which act as spore germinants. Probably autophosphorylates and phosphorylates FusA (EF-G, elongation factor G); the latter modification is likely necessary for germination in response to peptidoglycan. {ECO:0000269|PubMed:18984160}. | Staphylococcus aureus (strain Newman) |
A6QIG7 | CHIPS_STAAE | MKKKLATTVLALSFLTAGISTHHHSAKAFTFEPFPTNEEIESNKKMLEKEKAYKESFKNSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY | null | null | null | extracellular region [GO:0005576] | null | PF11434; | 3.10.20.390; | CHIPS/FLIPr family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14993252}. | null | null | null | null | null | FUNCTION: Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylated peptide receptor (FPR), thereby blocking the C5a- and fMLP-induced calcium responses. Prevents phagocytosis of the bacterium. {ECO:0000269|PubMed:14993252, ECO:0000269|PubMed:15153520}. | Staphylococcus aureus (strain Newman) |
A6QL29 | AGNO1_BFPYV | MSTPARDPNTAGTAALSPFSTPNHELRAPGPGEAHSPFTPTAAPGSQPAGSLSDPEDGPDPTFNFYIQGHRRRPYDRQNRFGKLESEIRETKSQLETLRQELKHLQADVDDLKETVYAAGTSTASTSVPPSQPNSPTPTATTPEASPAAPTTESTETTGPSVATNATEPSESRPAR | null | null | null | host cell nucleus [GO:0042025]; virion component [GO:0044423] | null | null | null | null | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11257197}. Host nucleus {ECO:0000269|PubMed:11257197}. | null | null | null | null | null | null | Budgerigar fledgling disease virus (BFPyV) (Aves polyomavirus 1) |
A6QLE5 | NLRP3_BOVIN | MRMVSVRCKLARYLEDLEDIDFKKFKMHLEDYPSQKGCTSIPRGQTEKADHVDLATLMIDFNGEEKAWAMAKWIFAAINRRDLYEKAKREEPEWENANISVLSQEESLEEEWMGLLGYLSRISICRKKKDYCKKYRKYVRSKFQCIKDRNARLGESVNLNKRFTRLRLIKEHRSQQEREHELLAIGRTWAKIQDSPVSSVNLELLFDPEDQHSEPVHTVVFQGAAGIGKTILARKIMLDWASEKLYQDRFDYLFYIHCREVSLGTQRSLGDLIASCCPGPNPPIGKIVSKPSRILFLMDGFDELQGAFDEHTEALCTNWRKVERGDILLSSLIRKRLLPEASLLITTRPVALEKLQHLLGQARHVEILGFSEARRKEYFLKYFSDEQQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMDSGKSLARTSKTTTAVYIFFLSSLLQSQGGSQENHNSATLWGLCSLAADGIWNQKILFQECDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEDNHGEMRNTPQACSKLPNRDVKVLLENYGKFEKGYLIFVVRFLFGLINQERTSYLEKKLSCKISQKIRLELLKWIEAKANAKTLQIEPSQLELFYCLYEMQEEDFVQRAMSHFPKIEIKLSTRMDHVVSSFCIENCRHVESLSLRLLHNSPKEEEEEEEVRHSHMDRSVLSDFEVAYSQGLVNYLTSSICRGIFSVLSNNWNLTELNLSGNTLGDPGMNVLCETLQQPGCNIRRLWLGQCCLSHQCCFNISSVLSNNQKLVELDLSHNALGDFGIRLLCVGLRHLFCNLKKLWLVSCCLTSASCEDLASVLSTNHSLTRLYLGENALGDSGVGILCEKVKNPHCNLQKLGLVNSGLTSGCCPALSSVLSTNQNLTHLYLQGNALGDMGVKLLCEGLLHRNCKLQVLELDNCSLTSHCCWDLSTLLTSNQSLRKLCLGNNDLGDLGVMLLCEVLKQQGCLLKSLRLCEMYFNYDTKRALETLQEEKPELTIVFEPSR | 3.6.4.- | null | detection of biotic stimulus [GO:0009595]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; NLRP3 inflammasome complex assembly [GO:0044546]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; positive regulation of T-helper 2 cell differentiation [GO:0045630]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type 2 immune response [GO:0002830]; protein homooligomerization [GO:0051260] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA-binding transcription factor binding [GO:0140297]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sequence-specific DNA binding [GO:0043565]; signaling adaptor activity [GO:0035591]; small molecule sensor activity [GO:0140299] | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-801 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation at Ser-5 in the pyrin domain inhibits homomultimerization of NLRP3 and activation of the NLRP3 inflammasome: dephosphorylation by protein phosphatase 2A (PP2A) promotes assembly of the NLRP3 inflammasome (By similarity). Phosphorylation at Ser-292 by PKD/PRKD1 promotes NLRP3 inflammasome assembly (By similarity). Phosphorylation by ERK1/MAPK3 promotes NLRP3 inflammasome assembly. Phosphorylation by BTK (at Tyr-131, Tyr-135 and Tyr-138) in the region that mediates binding to phosphatidylinositol phosphate, promotes relocalization of NLRP3 and assembly of the NLRP3 inflammasome. Phosphorylation at Tyr-856 inhibits NLRP3 inflammasome assembly: dephosphorylation by PTPN22 promotes inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination (By similarity). Ubiquitination does not lead to degradation, but inhibits inflammasome activation. Deubiquitination is catalyzed by BRCC3 and associated with NLRP3 activation and inflammasome assembly. This process can be induced by the activation of Toll-like receptors (by LPS), through a non-transcriptional pathway dependent on the mitochondrial production of reactive oxygen species, and by ATP (By similarity). Ubiquitinated by TRIM31 via 'Lys-48'-linked ubiquitination, leading to its degradation by the proteasome. Ubiquitinated at Lys-687 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). Ubiquitinated by TRIM35 via 'lys-48' and 'Lys-63'-linked ubiquitination leading to inhibition of NLRP3 inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: Palmitoylation by ZDHHC12 inhibits the NLRP3 inflammasome by promoting NLRP3 degradation by the chaperone-mediated autophagy pathway. Following palmitoylation, HSPA8/HSC70 recognizes and binds the KFERQ-like motifs on NLRP3 and promotes NLRP3 recruitment to lysosomes, where it is degraded via the chaperone-mediated autophagy pathway in a LAMP2-dependent process. Palmitoylation by ZDHHC5 enhances its binding to NEK7 leading to inflammasome assembly and activation. Depalmitoylated by ABHD17A. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes NLRP3 recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagy-dependent degradation. {ECO:0000250|UniProtKB:Q96P20}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R4B8}. Mitochondrion {ECO:0000250|UniProtKB:Q8R4B8}. Secreted {ECO:0000250|UniProtKB:Q8R4B8}. Nucleus {ECO:0000250|UniProtKB:Q8R4B8}. Note=In macrophages, under resting conditions, mainly located in the cytosol and on membranes of various organelles, such as endoplasmic reticulum, mitochondria and Golgi: forms an inactive double-ring cage that is primarily localized on membranes. Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes for the formation of an active inflammasome complex. Recruited to dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). After the induction of pyroptosis, inflammasome specks are released into the extracellular space where they can further promote IL1B processing and where they can be engulfed by macrophages. Phagocytosis induces lysosomal damage and inflammasome activation in the recipient cells. In the Th2 subset of CD4(+) helper T-cells, mainly located in the nucleus. Nuclear localization depends upon KPNA2. In the Th1 subset of CD4(+) helper T-cells, mainly cytoplasmic. {ECO:0000250|UniProtKB:Q8R4B8}. | 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:Q8R4B8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; | null | null | null | null | FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; FUNCTION: Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF. {ECO:0000250|UniProtKB:Q8R4B8}. | Bos taurus (Bovine) |
A6QLI1 | VGLU2_BOVIN | MESVKQRILTPGKEGLKNFAGKSLGQIYRVLEKKQDAGETIELTEDGKPLEVPEKKAPLCDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVDMVNNSTIHRGGKVIKEKAKFNWDPETVGMIHGSFFWGYIITQIPGGYIASRLAANRVFGAAILLTSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTSFCGSYAGAVIAMPLAGILVQYTGWSSVFYVYGSFGMIWYMFWLLVSYESPAKHPTITDEERRYIEESIGESANLLGAMEKFKTPWRKFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGMLSAVPHLVMTIIVPIGGQIADFLRSKQILSTTTVRKIMNCGGFGMEATLLLVVGYSHTRGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKNKSREEWQYVFLIAALVHYGGVIFYAIFASGEKQPWADPEETSEEKCGFIHEDELDEETGDITQNYINYGTTKSYGATTQANGGWPNGWEKKEEFVQEEVQNSYNYKDRDDYS | null | null | hyaloid vascular plexus regression [GO:1990384]; L-glutamate import [GO:0051938]; L-glutamate transmembrane transport [GO:0015813]; monoatomic anion transport [GO:0006820]; neurotransmitter loading into synaptic vesicle [GO:0098700]; phosphate ion homeostasis [GO:0055062]; phosphate ion transport [GO:0006817]; regulation of synapse structure or activity [GO:0050803]; sodium-dependent phosphate transport [GO:0044341]; synaptic transmission, glutamatergic [GO:0035249] | chloride channel complex [GO:0034707]; excitatory synapse [GO:0060076]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | chloride channel activity [GO:0005254]; L-glutamate transmembrane transporter activity [GO:0005313]; L-glutamate uniporter activity [GO:0140788]; neurotransmitter transmembrane transporter activity [GO:0005326]; potassium:proton antiporter activity [GO:0015386]; sodium:phosphate symporter activity [GO:0005436] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family, VGLUT subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q8BLE7}. Cell membrane {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q9JI12}; CATALYTIC ACTIVITY: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q9JI12}; CATALYTIC ACTIVITY: Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q9JI12}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q9JI12}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9JI12}; | null | null | null | null | FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane therefore affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, functions as a vesicular K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular L-glutamate uptake. The vesicular H(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Also involved in the regulation of retinal hyaloid vessel regression during postnatal development (By similarity). May also play a role in the endocrine L-glutamatergic system of other tissues such as pineal gland and pancreas (By similarity). {ECO:0000250|UniProtKB:Q8BLE7, ECO:0000250|UniProtKB:Q9JI12}. | Bos taurus (Bovine) |
A6QLJ0 | ERCC2_BOVIN | MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQRDSSLPHCRFYEEFDVHGRQVPLPTGIYNLDDLKAVGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQANLETLQKTVLRIKETDEQRLREEYRRLVEGLREASAARETDAHLANPVLPDEVLKEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLYTLEISDLTDFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLRRIEQIAQQL | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; | chromosome segregation [GO:0007059]; hair cell differentiation [GO:0035315]; nucleotide-excision repair [GO:0006289]; positive regulation of mitotic recombination [GO:0045951]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to oxidative stress [GO:0006979]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367] | CAK-ERCC2 complex [GO:0070516]; cytoplasm [GO:0005737]; MMXD complex [GO:0071817]; nucleus [GO:0005634]; spindle [GO:0005819]; transcription factor TFIIH holo complex [GO:0005675] | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872] | PF06733;PF06777;PF13307; | 3.40.50.300; | Helicase family, RAD3/XPD subfamily | PTM: ISGylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000250|UniProtKB:P18074}. | Bos taurus (Bovine) |
A6QLP2 | SAHH3_BOVIN | MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSTAAVSAMAPPAGGGDPEAPAPAAERPPAPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGNSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIILLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY | 3.13.2.1 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Note=Binds 1 NAD(+) per subunit.; | one-carbon metabolic process [GO:0006730]; S-adenosylmethionine cycle [GO:0033353] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | hydrolase activity [GO:0016787] | PF05221;PF00670; | 3.40.50.1480;3.40.50.720; | Adenosylhomocysteinase family | PTM: Phosphorylated during neuronal differentiation at the LISN domain. {ECO:0000250|UniProtKB:Q68FL4}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24472682}. Microsome {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000250|UniProtKB:Q68FL4}. | CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; | null | PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. | null | null | FUNCTION: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96HN2, ECO:0000269|PubMed:24472682}. | Bos taurus (Bovine) |
A6QLT2 | MTMR2_BOVIN | MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADRVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPRRTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYVRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERAGSPAQCVTPVQTVV | 3.1.3.64; 3.1.3.95 | null | myelin assembly [GO:0032288]; negative regulation of myelination [GO:0031642]; neuron development [GO:0048666]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of phosphatidylinositol dephosphorylation [GO:0060304] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; vacuolar membrane [GO:0005774] | identical protein binding [GO:0042802]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438] | PF02893;PF06602; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures. {ECO:0000250|UniProtKB:Q13614}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000250|UniProtKB:Q13614}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000250|UniProtKB:Q13614}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000250|UniProtKB:Q13614}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911, ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13614}; | null | null | null | null | FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}. | Bos taurus (Bovine) |
A6QLT4 | MTM1_BOVIN | MASAPTSKYNSHSLENESIKRTSRDGVNRDVGETLPRLPGEIRITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDLRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPIFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYKLCDTYPALLVVPYRASDEDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKEDERYLDVIRETNRQVNKLTIYDARPNVNAVANKATGGGYESDDVYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADRVSSGKSSVVVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNERFLITILDHLYSCRFGTFLYNCESAREKQKVTERTVSLWSLINSNKDKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLDELQLANSAKLSDPSASPSSPSQMMPHVQTHF | 3.1.3.64; 3.1.3.95 | null | endosome to lysosome transport [GO:0008333]; intermediate filament organization [GO:0045109]; mitochondrion distribution [GO:0048311]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of autophagosome assembly [GO:1902902]; phosphatidylinositol dephosphorylation [GO:0046856]; protein dephosphorylation [GO:0006470]; protein transport [GO:0015031]; regulation of vacuole organization [GO:0044088] | cytoplasm [GO:0005737]; filopodium [GO:0030175]; late endosome [GO:0005770]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; sarcomere [GO:0030017] | intermediate filament binding [GO:0019215]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721] | PF02893;PF06602; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13496}. Cell membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q13496}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q13496}. Late endosome {ECO:0000250|UniProtKB:Q13496}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q9Z2C5}. Note=Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation (By similarity). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (By similarity). {ECO:0000250|UniProtKB:Q13496, ECO:0000250|UniProtKB:Q9Z2C5}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000250|UniProtKB:Q13496}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000250|UniProtKB:Q13496}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000250|UniProtKB:Q13496}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911, ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13496}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994, ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:Q13496}; | null | null | null | null | FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. In skeletal muscles, stabilizes MTMR12 protein levels. {ECO:0000250|UniProtKB:Q13496}. | Bos taurus (Bovine) |
A6QLW8 | S22A7_BOVIN | MGFEELLDKVGGFGPFQLRNVALLALPRVLLPMHFLLPIFLAAVPAHRCALPGVPDNFSNEDAWLEAHLPREPDGRLSACLRFTHPQALPNSTLWGEGQNSGEQPEGEPSTVPCPQGWEYNHSEFSSTIATEWDLVCEQKGLNKAISTFFFAGVLVGAEVYGYLSDRFGRRRLLLVAYVSSLALGLASAASVSYIMFAITRTLTGMALAGFTIIVMPLELEWLDVRHRTVAGVLSSTFWTGGVMLLALIGYLIRDWRWLLLTVTLPCVPGILTLWWVPESARWLLTQGRVEEAHRYLLRCARLNGPPVGEDSLSREALNKVAAAERMVRRPSYLDLFRTPRLRYISLCCMVVWFGVNFSYYGVSLDLSGLGLNVYLTQLVFGAVELPSKLLVYLSVRHAGRRLTMAGTLLGAALAVGLRILVSPEMKSWSTALAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLAPLAALLDGVWLSLPKLAYGGIALLAACTALLLPETKQAQLPETIQDVERKSAPSSLQEEEMPMKQVQD | null | null | alpha-ketoglutarate transport [GO:0015742]; monoatomic ion transport [GO:0006811]; prostaglandin transport [GO:0015732] | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | alpha-ketoglutarate transmembrane transporter activity [GO:0015139]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; transmembrane transporter activity [GO:0022857] | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-glutamate(in) + orotate(out) = L-glutamate(out) + orotate(in); Xref=Rhea:RHEA:72043, ChEBI:CHEBI:29985, ChEBI:CHEBI:30839; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) = 3',5'-cyclic GMP(out); Xref=Rhea:RHEA:76207, ChEBI:CHEBI:57746; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=GMP(in) = GMP(out); Xref=Rhea:RHEA:76211, ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=2'-deoxyguanosine(in) = 2'-deoxyguanosine(out); Xref=Rhea:RHEA:76215, ChEBI:CHEBI:17172; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=GDP(in) = GDP(out); Xref=Rhea:RHEA:76219, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=GTP(in) = GTP(out); Xref=Rhea:RHEA:75787, ChEBI:CHEBI:37565; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP(in) = 3',5'-cyclic AMP(out); Xref=Rhea:RHEA:76223, ChEBI:CHEBI:58165; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=creatinine(in) = creatinine(out); Xref=Rhea:RHEA:74539, ChEBI:CHEBI:16737; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate(in) = 2-oxoglutarate(out); Xref=Rhea:RHEA:76231, ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=glutarate(in) = glutarate(out); Xref=Rhea:RHEA:76251, ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q91WU2}; CATALYTIC ACTIVITY: Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368, ChEBI:CHEBI:17775; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q9Y694}; | null | null | null | null | FUNCTION: Functions as a Na(+)-independent bidirectional multispecific transporter. Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively. Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides and nucleotides, with cGMP, 2'deoxyguanosine and GMP being the preferred substrates. Functions as a pH- and chloride-independent cGMP bidirectional facilitative transporter that can regulate both intracellular and extracellular levels of cGMP and may be involved in cGMP signaling pathways. Mediates orotate/glutamate bidirectional exchange and most likely display a physiological role in hepatic release of glutamate into the blood. Involved in renal secretion and possible reabsorption of creatinine. Able to uptake prostaglandin E2 (PGE2) and may contribute to PGE2 renal excretion. Also transports alpha-ketoglutarate and urate. Apart from the orotate/glutamate exchange, the counterions for the uptake of other SLC22A7/OAT2 substrates remain to be identified. {ECO:0000250|UniProtKB:Q9Y694}. | Bos taurus (Bovine) |
A6QNM7 | UBP33_BOVIN | MSSFRSHCPHLDSVGEITKEDLIQKSHGSCQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVKPLHQIQENGVQDFKIPSNTTLKTPLVAVFDDLDIEVEEEDELKARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTIMTEETMEEDKSQSDVDFQSCESCSSSDKAENENGSRSFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVHSEGELDKDRDSVSETADLNNQETVKVQIHSRASEYITDVHLNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLPPTHKKVQSALSPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVILRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDAVQAEEKIEVETRSL | 3.4.19.12 | null | axon guidance [GO:0007411]; cell migration [GO:0016477]; centrosome duplication [GO:0051298]; endocytosis [GO:0006897]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of G protein-coupled receptor signaling pathway [GO:0008277] | centrosome [GO:0005813]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; zinc ion binding [GO:0008270] | PF06337;PF00443;PF02148; | 3.90.70.10;3.30.2230.10;3.30.40.10; | Peptidase C19 family, USP20/USP33 subfamily | PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A6QP16 | ZRAN1_BOVIN | MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSICTYENWAKAKKCVVCDHPRPNNIEAIEFAETEEASSIINEQDRARWRGSCSSGNSQRRSPPTMKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE | 3.4.19.12 | null | cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; positive regulation of Wnt signaling pathway [GO:0030177]; protein K29-linked deubiquitination [GO:0035523]; protein K33-linked deubiquitination [GO:1990168]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of cell morphogenesis [GO:0022604]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872] | PF18418;PF02338;PF00641; | 1.25.40.560;4.10.1060.10; | Peptidase C64 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9UGI0}; | null | null | null | null | FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity). {ECO:0000250|UniProtKB:Q9UGI0}. | Bos taurus (Bovine) |
A6QP84 | SOAT_BOVIN | MRANCSSGLACPANSSEEELPEGLKAFGNLDLVFTVVSALMIGLLMFSLGCSVEVQKLWGHIRRPWGIAVGMLCQFGLMPLIAYLLIISFSLKPLQAIAVLIMGCCPGGTVSNIFTFWVDGDMDLSISMTTCSTMAALGMMPLCLYLYTLSWNLEQNLTIPYQNIGITLVCLIIPVAFGIYVNYRWPKQSKIILKIGAIAGGLLFLVVTGAGMVLMKEFWSSDIILLMISFIFPLIGHATGFLLALLTHQSWQRCRTISLETGTQNVQMCFTMLQLSFTAEQLVQIFGFVLAYGLFQMLNGFFMVAAYKMYKRRLKNKHGNEKPSCQEARHRKKSTSPKETTAFLEVNEEATLSPGPSGPVDPHGAPTPTGDIARAK | null | null | bile acid and bile salt transport [GO:0015721] | membrane [GO:0016020] | bile acid:sodium symporter activity [GO:0008508] | PF01758; | 1.20.1530.20; | Bile acid:sodium symporter (BASS) (TC 2.A.28) family | PTM: Glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71083, ChEBI:CHEBI:29101, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-sulfate(out) + 2 Na(+)(out) = 17beta-estradiol 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71087, ChEBI:CHEBI:29101, ChEBI:CHEBI:136582; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) + 2 Na(+)(out) = dehydroepiandrosterone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71091, ChEBI:CHEBI:29101, ChEBI:CHEBI:57905; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=androst-5-ene-diol 3-sulfate(out) + 2 Na(+)(out) = androst-5-ene-diol 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71099, ChEBI:CHEBI:29101, ChEBI:CHEBI:190287; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + pregnenolone sulfate(out) = 2 Na(+)(in) + pregnenolone sulfate(in); Xref=Rhea:RHEA:71095, ChEBI:CHEBI:29101, ChEBI:CHEBI:133000; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + taurolithocholate 3-sulfate(out) = 2 Na(+)(in) + taurolithocholate 3-sulfate(in); Xref=Rhea:RHEA:71275, ChEBI:CHEBI:29101, ChEBI:CHEBI:58301; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=androsterone 3alpha-sulfate(out) + 2 Na(+)(out) = androsterone 3alpha-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71351, ChEBI:CHEBI:29101, ChEBI:CHEBI:133003; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=5alpha-dihydrotestosterone sulfate(out) + 2 Na(+)(out) = 5alpha-dihydrotestosterone sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71355, ChEBI:CHEBI:29101, ChEBI:CHEBI:136982; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-sulfate(out) + 2 Na(+)(out) = 17beta-estradiol 17-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71359, ChEBI:CHEBI:29101, ChEBI:CHEBI:190469; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=17alpha-hydroxypregnenolone 3-sulfate(out) + 2 Na(+)(out) = 17alpha-hydroxypregnenolone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71363, ChEBI:CHEBI:29101, ChEBI:CHEBI:133742; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=epiandrosterone 3-sulfate(out) + 2 Na(+)(out) = epiandrosterone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71367, ChEBI:CHEBI:29101, ChEBI:CHEBI:133729; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=epitestosterone 17-sulfate(out) + 2 Na(+)(out) = epitestosterone 17-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71371, ChEBI:CHEBI:29101, ChEBI:CHEBI:190485; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + testosterone 17-sulfate(out) = 2 Na(+)(in) + testosterone 17-sulfate(in); Xref=Rhea:RHEA:71375, ChEBI:CHEBI:29101, ChEBI:CHEBI:190489; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=16alpha-hydroxydehydroepiandrosterone 3-sulfate(out) + 2 Na(+)(out) = 16alpha-hydroxydehydroepiandrosterone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71391, ChEBI:CHEBI:29101, ChEBI:CHEBI:87538; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; | null | null | null | null | FUNCTION: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similarity). May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs (By similarity). May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium (By similarity). Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes (By similarity). {ECO:0000250|UniProtKB:Q3KNW5, ECO:0000250|UniProtKB:Q9CXB2}. | Bos taurus (Bovine) |
A6QPB3 | COHA1_BOVIN | MDITQKNKRDGTEVTERIITETVTTRLTSLPPKGGTSNGYAKTGSLGGGSRLEKQSLTHGSSGYINSSGSLRGNASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHGTYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKVVTASSQSVSGTYDTTILDANLPSHVWSSTLPAGSSMGTYHNNITTQSSSLLNTNAYSAGSVFGVPNNMASCSATLQPGISTSSSVFGMQNNLAPSSSTLSHGMAATSTAYGVKKNMPQSPTAVSTGVSTSAASTTNVQNDDLLHKDCKFLILEKDNTPAKKEMELLIMTKDSGKVFTASPASVAATSFSEDTLKKEKQAAYTDTYLVSEANGDVKTVTAKGNGASADIHGYDHRRGGGGGGGSGGALGSGAAGGGGKGSWGAAPTWCPCGSWCSWWKWLLGLLLTWLLLLGLLFGLIALAEEVRKLKARVEELEKMRGRLSYNEKMERSSQDSVQGVAPRLGEGLGKSELDDYNLEDVWQFMKVRLMTEQENGNLRGSPGPKGDMGVQGPKGDRGFPGTPGIPGPLGHQGPEGPKGQKGNVGEPGMEGPMGQRGREGPMGPRGEPGPPGFGEKGDRGDAGKPGIPGPPGVPGSVGPKGSIGPQGLRGEVGLPGIKGDKGPMGPPGPKGDQGEKGPRGLTGEPGLKGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLPGMPGTRGLPGPSGDPGKPGLTGPQGPQGIPGTPGRPGVKGEPGAPGKIMTSEGSSTITVPGPPGPPGAMGPPGPPGAPGPVGPAGLPGQQGPRGEPGLAGESFMGSSSSFSEVLSTQGIDLRGPPGPPGPPGPPGEGLPGPPGPPGSLLTSSETFFSGPPGPPGPPGPKGDQGPPGPRGHQGERGFPGLSGSGSSSLGLNLQGPPGPPGPQGPKGDKGDPGVPGAPGIPGGPSRGGSSSSTTFMQGPPGPPGPPGPPGSLSSSGLEIQQYISDYMQSDSIRPYLSGVQGPPGPPGPPGPVTTITGETFNYSELASLVVSYLQTSGYNIGTSSTSISSEDILAALRRDDVRQYLQQYLMPQGAGGDWFLQSLDYAELSNRILSYMSSTGVSIGLPGPPGPPGLPGTSYEELLSLLQGSEFRGIVGPPGPPGPPGLPGSSWSSISTEDLSSYLQTAGLSSIPGPPGPPGPPGPRGPPGISGALATYAAENSDSFRSELISYLTSPDVRSFIVGPPGPPGPQGPPGDTRLVSTDSSYSRSGSSSSFSRDTSYSSSMGIGGASGGSLGEAGAFGMDMGRGYGAAAESGMYGGNGRFGTSFAGGLDYNELAVRVSESLQRQGLLQGMAYTVQGPPGRPGPQGPPGISKIFSAYSNVTEDLMDFFRTYGAIPGPPGQKGEMGIPGPKGERGPAGPPGPRGHKGEKGDKGDQFYIGRRRRSIAVKP | null | null | extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581] | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; hemidesmosome [GO:0030056]; membrane [GO:0016020] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201] | PF01391; | 1.20.5.320; | null | PTM: The intracellular/endo domain is disulfide-linked. {ECO:0000250}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen homolog. The shedding is mediated by membrane-bound metalloproteases. | SUBCELLULAR LOCATION: Cell junction, hemidesmosome {ECO:0000269|PubMed:9545306}. Membrane {ECO:0000269|PubMed:9545306}; Single-pass type II membrane protein {ECO:0000269|PubMed:9545306}. Note=Localized along the plasma membrane of the hemidesmosome. {ECO:0000250}.; SUBCELLULAR LOCATION: [120 kDa linear IgA disease antigen homolog]: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. {ECO:0000250}.; FUNCTION: The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion. {ECO:0000269|PubMed:12761182}. | Bos taurus (Bovine) |
A6QQJ8 | ZC12A_BOVIN | MSLWELEDRRSCQGTPRPAQEPTAEEATTAELQMKVDFFRKLGYSSAEIHSVLQKLGIQADTNTVLGELVKHGSAAERERQASPDPCPQLPLVPRGGGTPKAPTVETYPPEEDKEGSDLRPIVIDGSNVAMSHGNKDVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRDLEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTSEHKKQPCPYGRKCTYGIKCRFLHPERPSRPQRSVADELRANALLPPSRAASKDKNSRRPSPSSQPGSLPTEHEQCSPDRKKLGAQASPGTPREGLMQTFAPTGRSLPPSGSSGGSFGPSEWFPQTLDSLPYASQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRGPYAGYCTYGAELPATPAFSAFSRALGAGHFSVPADYAPPPAAFPPREYWSEPYQLPPPTQRLQEPQAPGPGADRGPWGGAGRLAKERASVYTKLCGVFPPHLVEAVMSRFPQLLDPQQLAAEILSYKSQHLSE | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5D1E8}; Note=Mg(2+) is required for RNase activity. {ECO:0000250|UniProtKB:Q5D1E8}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cellular response to chemokine [GO:1990869]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; immune response-activating signaling pathway [GO:0002757]; miRNA catabolic process [GO:0010587]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein complex oligomerization [GO:0051259]; T cell receptor signaling pathway [GO:0050852] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; P-body [GO:0000932]; rough endoplasmic reticulum membrane [GO:0030867] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; nuclease activity [GO:0004518]; RNA endonuclease activity [GO:0004521]; RNA exonuclease activity [GO:0004532]; RNA stem-loop binding [GO:0035613] | PF18561;PF11977;PF18039; | 3.40.50.11980; | ZC3H12 family | PTM: Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinase (IKK) subunits IKBKB/IKKB and CHUK/IKKA at Ser-422 and Ser-426; these phosphorylations promote ubiquitin proteasome-mediated degradation of ZC3H12A and hence facilitates rapid and robust production of IL-6 mRNA in response to toll-like receptor (TLR) or IL-1 receptor stimuli (By similarity). {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.; PTM: Ubiquitinated; ubiquitination is induced in response to interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent manner, leading to proteasome-mediated degradation (By similarity). {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.; PTM: Proteolytically cleaved between Arg-95 and Arg-198 by MALT1 in activated T-cells; cleavage at Arg-95 is critical for promoting ZC3H12A degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling T-cell activation and Th17 cell differentiation. {ECO:0000250|UniProtKB:Q5D1E7}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm {ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q5D1E8}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5D1E7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q5D1E7}. Note=Predominantly localized in the cytoplasm. Colocalizes with GW182 on many granule-like structures, probably corresponding to cytoplasmic GW bodies (GWBs), also called processing bodies (P bodies). Colocalizes with calnexin on the surface of the rough endoplasmic reticulum (RER) membrane and with translationally active polysomes (By similarity). Colocalizes with ZC3H12D in cytoplasmic mRNA processing P-body, also known as GW bodies (GWBs) (By similarity). {ECO:0000250|UniProtKB:Q5D1E8}. | null | null | null | null | null | FUNCTION: Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation. Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity). Self regulates by destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (By similarity). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (By similarity). Also plays a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (By similarity). Affects the overall ubiquitination of cellular proteins. Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (By similarity). Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation. Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state. May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (By similarity). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (By similarity). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-inflammatory cytokine production (By similarity). {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}. | Bos taurus (Bovine) |
A6QQL0 | S15A4_BOVIN | MEGAGDERAPLLGARRTAFAGRRAACAAVLLTELLERAAFYGVTANLVLFLNGTAFGWEGAEASQALLLFMGLTYLVSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPATRSALCGAPGPTNVRNCSAPPCTDTPTRYCAPAVLSALALVGLGVGAVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAIVSLGGIAYIQQNVSFVTGYAIPAVCIGVAFVVFLCGQTFFITKPPDGSAFTDMFRILVYSCRPQKRIREHSPSGEGIGVFQQSSKHSLFDSCKMSRGGPFPEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLKIPEISSITTNPHTFPAAWLTMFDAVLILLLIPLKDKLVDPILKRNGLLPSSLKRIAVGMFFVMCSAFAAGILESKRLDLVKEKTINQTIGNVVYYAADLPIWWQVPQYVLIGVSEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGVGSFVGSGLLALVSLKAIGWMSSHTDFGNINGCYLNYYFFLLAAIQGATLLLFLIVSVKYDRQRSRANGTPASRRT | null | null | dipeptide import across plasma membrane [GO:0140206]; histidine transport [GO:0015817]; innate immune response [GO:0045087]; mast cell homeostasis [GO:0033023]; peptidoglycan transport [GO:0015835]; positive regulation of innate immune response [GO:0045089]; positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070430]; positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070434]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 8 signaling pathway [GO:0034161]; positive regulation of toll-like receptor 9 signaling pathway [GO:0034165]; protein transport [GO:0015031]; regulation of isotype switching to IgG isotypes [GO:0048302]; regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0070424] | early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; lysosomal membrane [GO:0005765]; membrane [GO:0016020] | dipeptide transmembrane transporter activity [GO:0071916]; L-histidine transmembrane transporter activity [GO:0005290]; peptide:proton symporter activity [GO:0015333]; peptidoglycan transmembrane transporter activity [GO:0015647] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91W98}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glycylglycylglycine(out) + n H(+)(out) = glycylglycylglycine(in) + n H(+)(in); Xref=Rhea:RHEA:76391, ChEBI:CHEBI:15378, ChEBI:CHEBI:195214; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76392; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out) = n H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in); Xref=Rhea:RHEA:76371, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76372; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate(out) = n H(+)(in) + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate(in); Xref=Rhea:RHEA:64412, ChEBI:CHEBI:15378, ChEBI:CHEBI:61401; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64413; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=carnosine(out) + n H(+)(out) = carnosine(in) + n H(+)(in); Xref=Rhea:RHEA:76383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76384; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + L-histidine(out) = n H(+)(in) + L-histidine(in); Xref=Rhea:RHEA:76379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76380; Evidence={ECO:0000250|UniProtKB:Q8N697}; | null | null | null | null | FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response. Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (By similarity). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (By similarity). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity). {ECO:0000250|UniProtKB:O09014, ECO:0000250|UniProtKB:Q8N697, ECO:0000250|UniProtKB:Q91W98}. | Bos taurus (Bovine) |
A6QR55 | UBP4_BOVIN | MAEGGGYRERPDAETQKSELGALMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLYPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTQQSKSSTAPSRNFTTSPKSSASPYSSVSASPIANGDSTNTSGMHSSGVSRGGSGFSASYNCQESPLTHVQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEIFLVPADPRCRPTQYRVVVPLMGAVSDLCEALSKLSGIAAENMVVTDVYNHRFHKIFQMDEGLNHIMPRDDIFVYEVCSTSPDGSECVTLPVYFRERKSRPSSTSTGAVLYGQPLLVSVPKHKLTLESLYQAVCERISRYIKQPLPDESGSSPLELGACNGSRSGCAGEDEEEMEHQEEGREQLSETEGSGDDEPGSDHGEATQKKNKGRPCPRRLFTFSLVNSYGTADINSLATDGKLLKLNSRSTLAIDWDSETRSCYYNEQESETYEKHVSMLQPQKKKKTAVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRGLNMSEFVCDPSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLACEDQIVTKAAYVLFYQRRDDEFHKTPSLSFPGSSDGGARPSSSQQGTGDDETYSMDTN | 3.4.19.12 | null | negative regulation of protein ubiquitination [GO:0031397]; positive regulation of TORC1 signaling [GO:1904263]; protein deubiquitination [GO:0016579]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647]; spliceosomal tri-snRNP complex assembly [GO:0000244] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872] | PF06337;PF14836;PF00443; | 3.90.70.10;3.30.2230.10; | Peptidase C19 family, USP4 subfamily | PTM: Phosphorylated at Ser-445 by PKB/AKT1 in response to EGF stimulus, promoting its ability deubiquitinate RHEB. {ECO:0000250|UniProtKB:Q13107}.; PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Nucleus {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type. {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q13107}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. Deubiquitinates RHEB in response to EGF signaling, promoting mTORC1 signaling. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000250|UniProtKB:Q13107}. | Bos taurus (Bovine) |
A6R8Q8 | ARO1_AJECN | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYVLISDTNLTPLYLEGFQKSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECISIGMVKEAELARHLGILNNVSVSRISKCLANYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASSSELYVGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLVGGKPISQPYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQNDFSTRVTGPPGGILSPLPNINMEPMTDAFLTASVLAAVARGKGSNRTTRIFGIANQRVKECNRIKAMKDELAKFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVAHEPTLILEKECVGKTWPGWWDCLSQTFKVKLDGKEVGKRTETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKQNTFFVSLTLPDLGLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRTSVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSTIIASHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNIPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPGFGGASVTIPLKLSIMPLLDEIAPEAMSIGAVNTIVCAPPAPDSKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCKLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARCWKVYDVKLINCERGNAISLLVLEAFTHAFYEHPVLNHSS | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) |
A6RYB8 | ATG1_BOTFB | MASTTTSTSSLSSRRQKTGVGSFTINEQIGKGSFATVYRGTHMPSGNLVAIKSVNLSRLNKKLKDNLYVEIEILKSLYHPHIVALIDCRESASHIHLMMEYCELGDLSYFIKKRDRLADNPTLYDMVQKYPMPVEGGLNQVVVRHFFKQLSSAMEFLRERDFVHRDVKPQNLLLIPSPEWIAKRAKGGPEAMKASKESVVAMVGINSLPMLKLADFGFARSLPSTSLAETLCGSPLYMAPEILRYEKYDARADLWSIGTVLYEMMTGRPPFKAINHVQLLQKIEKNQDEIRFPSRGIYSRDLKDIVRRLLKKKPEDRITFPEYFAHPVVTEPIPGLVGDDRPKEKSPETSIVRQPSLRDRQRESPTVKHIDTAYESLITRDIGEQSPRTPNIESNQPFGTPGRSSGRPDSRDRPSPVSAATAPNVDTLPRQRDRKDRTEPNYAPIVRTGSTKQRYDEQANLQPKNEVQSSNSITEAEQDVRDAREYVLVEKKAVEVNAFADEMAANPRLGRANSAPKQLPRRHTSMGEPNSTTGAVAVPPSRIVQRASGRAQPDTSSARNSYGSYGKTGSSPSTASAIAKALQGASVRVFGVSWSPTLIGKGPSPPQLYNPYPAYPTPNAGLIGDGRPIDEDQRVVNIIEDSATRSDVVYGFAEVKYRQLIPLAPSMNHGLGGPNPERTGDAMDEDDGLTVEAIVNLSEEALVLYVKSLSLLSKSMDIAGAWWSRKQRGGIVSGGHTPGSDSSSAAQAGNRINGAVQWVRTRFNEVLEKAELVRLKLVEAQKRLPEDHPGHPNNRSTASRLVGGSSTTDGVVLSSGITAEKLMYDRALEMSRTAAINELANEDLPGCEISYTTAIRMLEAVLENDEELIPRKRSSSLREDKEKSEGGEVNGINFGDRKDVLKVLQMIRTRLQVLKKKMTAIAKHQSMPPPSSSPRRSYSGGTTPTINNTPPK | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709] | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; 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:P53104}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. {ECO:0000250|UniProtKB:P53104}. | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
A6T7D6 | PYRC_KLEP7 | MTAQSQVLKIRRPDDWHIHLRDDDMLKTVVPYTSEFYGRAIVMPNLVPPVTTVAAAIAYRQRIMDAVPAGHDFTPLMTCYLTDSLDPAELERGFNEGVFTAAKLYPANATTNSSHGVTSTDAIMPVLERMEKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLRQRLPGLKVVFEHITTKDAAEYVRDGNELLAATITPQHLMFNRNHMLVGGIRPHLYCLPVLKRNIHQQALRELVASGFSRAFLGTDSAPHARHRKEASCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSLNGPRFYGLPVNESYVELVREETTVVDSIALPNDTLVPFLAGETVRWTVKK | 3.5.2.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00219}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:20676924}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20676924}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:20676924}; Note=Binds 2 Zn(2+) ions per subunit (By similarity). In vitro, shows higher activity with Co(2+), Mg(2+), Ni(2+) and Mn(2+) than with Zn(2+) (PubMed:20676924). {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205] | cytosol [GO:0005829] | dihydroorotase activity [GO:0004151]; zinc ion binding [GO:0008270] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, DHOase family, Class II DHOase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for dihydroorotate {ECO:0000269|PubMed:20676924}; Vmax=8.87 umol/min/mg enzyme {ECO:0000269|PubMed:20676924}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00219}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:20676924}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 60 degrees Celsius. {ECO:0000269|PubMed:20676924}; | FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6T923 | HPXO_KLEP7 | MKAIVIGAGIGGLSAAVALKQSGIDCDVYEAVKEIKPVGAAISVWPNGVKCMAHLGMGDIMETFGGPLRRMAYRDFRSGENMTQFSLAPLIERTGSRPCPVSRAELQREMLDYWGRDSVQFGKRVTRCEEDADGVTVWFTDGSSASGDLLIAADGSHSALRPWVLGFTPQRRYAGYVNWNGLVEIDEALAPGDQWTTFVGEGKRVSLMPVSAGRFYFFFDVPLPAGLAEDRDTLRADLSRYFAGWAPPVQKLIAALDPQTTNRIEIHDIEPFSRLVRGRVALLGDAGHSTTPDIGQGGCAAMEDAVVLGAVFRQTRDIAAALREYEAQRCDRVRDLVLKARKRCDITHGKDMQLTEAWYQELREETGERIINGMCDTILSGPLG | 1.14.13.113 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19260710}; | purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | null | FAD binding [GO:0071949]; FAD-dependent urate hydroxylase activity [GO:0102099]; 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]; urate oxidase activity [GO:0004846] | PF01494; | 3.50.50.60; | FAD-dependent urate hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+); Xref=Rhea:RHEA:27329, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.113; Evidence={ECO:0000269|PubMed:19260710}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for urate {ECO:0000269|PubMed:19260710}; Note=kcat is 42 sec(-1). {ECO:0000269|PubMed:19260710}; | PATHWAY: Purine metabolism; urate degradation. {ECO:0000269|PubMed:19260710}. | null | null | FUNCTION: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). {ECO:0000269|PubMed:19260710}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TB83 | MTFA_KLEP7 | MFKWPWKADDESGNAEMPWEQALAIPVLAHLSSTEQHKLTQMAARFLQQKRLVALQGLELTPLHQARIAMLFCLPVLELGIEWLDGFHEVLIYPAPFIVDDEWEDDIGLVHNQRVVQSGQSWQQGPVVLNWLDIQDSFDASGFNLVVHEVAHKLDTRNGDRASGVPLIPLREVAGWEHDLHAAMNNIQDEIDLVGESAASIDAYAATDPAECFAVLSEYFFSAPELFAPRFPALWQRFCHFYRQDPLARRRENGLQDEGDRRIVH | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01593, ECO:0000269|PubMed:22467785}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01593, ECO:0000269|PubMed:22467785}; | proteolysis [GO:0006508] | cytosol [GO:0005829] | aminopeptidase activity [GO:0004177]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF06167; | 3.40.390.10;1.10.472.150; | MtfA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01593}. | null | null | null | null | null | FUNCTION: Involved in the modulation of the activity of the glucose-phosphotransferase system (glucose-PTS). Interacts with the transcriptional repressor Mlc, preventing its interaction with DNA and leading to the modulation of expression of genes regulated by Mlc, including ptsG, which encodes the PTS system glucose-specific EIICB component. {ECO:0000255|HAMAP-Rule:MF_01593}.; FUNCTION: Shows zinc-dependent metallopeptidase activity (PubMed:22467785). In vitro, can cleave several artificial substrates (PubMed:22467785). The highest activity is observed for L-alanine fused to 4-nitroanilide (L-alanine-pNA) (PubMed:22467785). Shows lower activity towards proline-pNA and valine-pNA (PubMed:22467785). {ECO:0000269|PubMed:22467785}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TBV3 | NUDI_KLEP7 | MRHRTIVCPLIENKGHYLLCKMAADRGVFPGQWALSGGVEPGERIEEALRREIREELGEKLILTHIAPWCFRDDTRVKTYPDGHQETIYMIYLIFNCVSANRDVTINEEFDDYAWVKAEDLKNYDLNAATRVTLSLKGLL | 3.6.1.-; 3.6.1.12; 3.6.1.23; 3.6.1.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; | DNA repair [GO:0006281] | null | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; dCTP diphosphatase activity [GO:0047840]; dTTP diphosphatase activity [GO:0036218]; dUTP diphosphatase activity [GO:0004170]; magnesium ion binding [GO:0000287] | PF00293; | 3.90.79.10; | Nudix hydrolase family, NudI subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). {ECO:0000255|HAMAP-Rule:MF_01846}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TF07 | CYSG2_KLEP7 | MDHLPIFCQLRQRDCLLVGGGDVAERKARLLLDAGANVTVNALDFTPQFQVWADSQMLTLVQGEFIPSLLDNCWLAIAATDDETVNQQVSEAAEARRIFCNVVDAPRQASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESILPLHLGQLARYAGHLRARVKQQFATVGERRRFWEKLFVNDRLAQSLANDDRQAVADTTEQLLTEPLEHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRSGYHCVPQEEINQILLREAQKGRRVVRLKGGDPFIFGRGGEELETLCEAGIPFSVVPGITAASGCSAYSGIPLTHRDFAQGVRLVTGHLKTGGELDWANLAVEKQTLVFYMGLNQAPAIREKLIAHGMAEDMPAAIVENGTAVTQKVVSGTLGQLDILAQQMASPALIIVGRVVGLRDKLNWFSNH | 1.3.1.76; 2.1.1.107; 4.99.1.4 | null | cobalamin biosynthetic process [GO:0009236]; methylation [GO:0032259]; siroheme biosynthetic process [GO:0019354] | null | NAD binding [GO:0051287]; precorrin-2 dehydrogenase activity [GO:0043115]; sirohydrochlorin ferrochelatase activity [GO:0051266]; uroporphyrin-III C-methyltransferase activity [GO:0004851] | PF10414;PF13241;PF14824;PF00590; | 3.40.50.720;1.10.8.210; | Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family; Precorrin methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856, ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107; Evidence={ECO:0000255|HAMAP-Rule:MF_01646}; CATALYTIC ACTIVITY: Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin; Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76; Evidence={ECO:0000255|HAMAP-Rule:MF_01646}; CATALYTIC ACTIVITY: Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin; Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01646}; | null | PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}. | null | null | FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. {ECO:0000255|HAMAP-Rule:MF_01646}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TGM4 | FADB_KLEP7 | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDVGADQALKIGLVDGVVAAEKLRDGALAILRQAMNGDLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARLGREEALVLENKSFVPLAHTNEARALVGIFLNDQYVKAKAKKLTKDVETPKHAAVLGAGIMGGGIAYQSAWKGVPVVMKDISDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIQPTLEYSGFDRVDVVVEAVVENPKVKKAVLAETESKVRPDTVLASNTSTIPISELASVLQRPENFCGMHFFNPVHRMPLVEVIRGEKTSDNTIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKDDSKGKPKKEEDAAVDSLLADVSQPKRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTIGSAKYLDMAQQYQHLGPLYEVPAGLRDKARHNEAYYPQVEPARPVGALKTA | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TZ28 | HCHA_STAA2 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Staphylococcus aureus (strain JH1) |
A6WE36 | XPB_KINRD | MTDGPLIVQSDKTLLLEVDHPRAGACRAAIAPFAELERAPEHVHTYRLTPLGLWNARAAGHDAEQVVDTLLEFSRYSVPHALLVDVAETMARYGRLQLVKDEEHGLVLRSLDPAVLEEVLRSRKSAPLLGTRIAPDAVLVHPSERGNLKQVLLKLGWPAEDLAGYVDGEAHAIDLAEDGWALRPYQSEAVDNFWNGGSGVVVLPCGAGKTLVGAAAMAKARATTLILVTNTVSARQWRDELLKRTSLTEDEIGEYSGARKEIRPVTIATYQVVTTKRKGVYPHLELFDARDWGLILYDEVHLLPAPIFRMTADLQARRRLGLTATLVREDGREGDVFSLIGPKRYDAPWKDIEAQGYIAPADCVEVRVTLPDAERLAYATAEDDEKYRLCSTSLSKSRVVEKLVAQHAGEPTLVIGQYIDQLDDLAARLDAPVIKGETTVKERQRLFDAFRHGEITTLVVSKVANFSIDLPEAKVAIQVSGSFGSRQEEAQRLGRVLRPKGDHGSARFYTVVSRDTKDQDYAAHRQRFLAEQGYAYRIVDADDIDGGVPDADGVLPG | 5.6.2.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19199647}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19199647}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19199647}; Note=ATPase activity has a small preference for Mn(2+) over Mg(2+) or Ca(2+). Co(2+) and Zn(2+) are inactive. {ECO:0000269|PubMed:19199647}; | transcription initiation at RNA polymerase II promoter [GO:0006367] | transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:19199647}; 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:0000269|PubMed:19199647}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for 21-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; KM=50 uM for 10-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; | null | null | null | FUNCTION: ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs, 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs or 5'-flap substrates (PubMed:19199647). Requires ATP hydrolysis for activity; the ATPase activity is DNA-dependent and requires a minimum of 4 single-stranded nucleotides (nt) with 6-10 nt providing all necessary interactions for full processive unwinding (PubMed:19199647). The ATPase prefers ATP over CTP or GTP, is almost inactive with TTP (PubMed:19199647). {ECO:0000269|PubMed:19199647}. | Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) |
A6X8Z5 | RHG31_MOUSE | MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKENKGNFSRTVTTGGFFIPATKMHASSTGSSCDLSKEGEWGQEGMPAGAEGGCEVGGQIRPLPEQLKVFRPIGDPESEQSAPKLLGMFYTSSDSPGKSVFTSSLFQMEPSPRHQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGTEPLILHEMDEEDLAQALIWPEIQQELKIIESEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDAANQSIQEAAILTDREKLEPVCSLLESESQQELSPDPASLAPLEMLLFEKVSSPARIEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSHWTLEAPFSSSCANLETERNYEPLQPPAARTKIAGLEEKALKAFREFSGLKGLEVLPSQKGPSGIQPKPVETNFMGLAEGKEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLNLDSATPIADLFRLENGAPFSSPGIELSELGDTKVTWMSSSHCKAAPWNSQDTQDLDIVAHTLTGRRNSAPVSVSAVRTSFMVKMCQAKAVPVIPPKIQYTQIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQASITSCMYEGSSCSPEPSASTLASTQDAVVQCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPGRPQSLILFPIMDHLPSSPTVIDSKVLLSPIRSPTQTVSPGLLCGELAENTWITPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE | null | null | small GTPase-mediated signal transduction [GO:0007264] | focal adhesion [GO:0005925]; lamellipodium [GO:0030027] | GTPase activator activity [GO:0005096]; SH3 domain binding [GO:0017124] | PF00620; | 1.10.555.10; | null | PTM: Phosphorylated on Thr-776 by GSK3; which reduces GAP activity. {ECO:0000269|PubMed:16024771, ECO:0000269|PubMed:17158447}. | SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell junction, focal adhesion. | null | null | null | null | null | FUNCTION: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269|PubMed:16860736, ECO:0000269|PubMed:9786927}. | Mus musculus (Mouse) |
A6X935 | ITIH4_MOUSE | MKSPAPAHMWNLVLFLPSLLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQELLQRRLGMYELLLKVRPQQLVKHLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGGSIQIEEGYFVHHFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGTNINNAVLLAVELLDRSNQAELLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMALDNGGLARRIYEDSDSALQLQDFYHEVANPLLSSVAFEYPSDAVEEVTRYKFQHHFKGSEMVVAGKLQDQGPDVLLAKVSGQMHMQNITFQTEASVAQQEKEFKSPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEGQEQFQVAEKPVEVGDGMQRLPLAAQAHPFRPPVRGSKLMTVLKGSRSQIPRLGDAVRASRQYIPPGFPGPPGPPGFPAPPGPPGFPAPPGPPLASGSDFSLQPSYERMLSLPSVAAQYPADPHLVVTEKSKESTIPEESPNPDHPQVPTITLPLPGSSVDQLCVDILHSEKPMKLFVDPSQGLEVTGKYENTGFSWLEVTIQKPHLQVHATPERLVVTRGRKNTEYKWKKTLFSVLPGLKMTMNMMGLLQLSGPDKVTIGLLSLDDPQRGLMLLLNDTQHFSNNVKGELGQFYRDIVWEPPVEPDNTKRTVKVQGVDYLATRELKLSYQEGFPGAEISCWTVEI | null | null | acute-phase response [GO:0006953]; hyaluronan metabolic process [GO:0030212]; response to cytokine [GO:0034097] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF06668;PF08487;PF00092; | 3.40.50.410; | ITIH family | PTM: May be O-glycosylated (By similarity). N-glycosylated. {ECO:0000250, ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. | Mus musculus (Mouse) |
A6XA80 | LTC4S_CAVPO | MKDEVALLATVTLLGVLLQAYFSLQVIRARRAHRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGVYFHEGAAALCGLVYLFTRLRYFWGYARSAQLRLAPLYASARALWLLLALATLGLLAHFLPAAARAALLRLLRALLRTA | 2.5.1.-; 4.4.1.20 | null | leukotriene biosynthetic process [GO:0019370]; leukotriene metabolic process [GO:0006691]; long-chain fatty acid biosynthetic process [GO:0042759] | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640] | enzyme activator activity [GO:0008047]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; leukotriene-C4 synthase activity [GO:0004464] | PF01124; | 1.20.120.550; | MAPEG family | PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity. {ECO:0000250|UniProtKB:Q16873}. | SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. | CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000250|UniProtKB:Q16873}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619; Evidence={ECO:0000250|UniProtKB:Q16873}; CATALYTIC ACTIVITY: Reaction=(13S,14S)-epoxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + glutathione = (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:53508, ChEBI:CHEBI:57925, ChEBI:CHEBI:131958, ChEBI:CHEBI:137407; Evidence={ECO:0000250|UniProtKB:Q16873}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53509; Evidence={ECO:0000250|UniProtKB:Q16873}; | null | PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis. {ECO:0000250|UniProtKB:Q16873}. | null | null | FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions. {ECO:0000250|UniProtKB:Q16873}. | Cavia porcellus (Guinea pig) |
A6XH05 | CINS1_SALFT | MSSLIMQVVIPKPAKFFHNNLFSLSSKRHRFSTTTTTRGGRWARCSLQTGNEIQTERRTGGYQPTLWDFSTIQSFDSEYKEEKHLMRAAGMIDQVKMMLQEEVDSIRRLELIDDLRRLGISCHFEREIVEILNSKYYTNNEIDERDLYSTALRFRLLRQYDFSVSQEVFDCFKNAKGTDFKPSLVDDTRGLLQLYEASFLSAQGEETLRLARDFATKFLQKRVLVDKDINLLSSIERALELPTHWRVQMPNARSFIDAYKRRPDMNPTVLELAKLDFNMVQAQFQQELKEASRWWNSTGLVHELPFVRDRIVECYYWTTGVVERRQHGYERIMLTKINALVTTIDDVFDIYGTLEELQLFTTAIQRWDIESMKQLPPYMQICYLALFNFVNEMAYDTLRDKGFDSTPYLRKVWVGLIESYLIEAKWYYKGHKPSLEEYMKNSWISIGGIPILSHLFFRLTDSIEEEAAESMHKYHDIVRASCTILRLADDMGTSLDEVERGDVPKSVQCYMNEKNASEEEAREHVRSLIDQTWKMMNKEMMTSSFSKYFVEVSANLARMAQWIYQHESDGFGMQHSLVNKMLRDLLFHRYE | 4.2.3.-; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | alpha-pinene biosynthetic process [GO:0046248]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; pinene synthase activity [GO:0050550]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate; Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-pinene + diphosphate; Xref=Rhea:RHEA:25666, ChEBI:CHEBI:33019, ChEBI:CHEBI:50025, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25667; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:17557809}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=65.4 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:17557809}; Note=kcat is 3.18 min(-1) with (2E)-geranyl diphosphate as substrate. {ECO:0000269|PubMed:17557809}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17557809}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole, and, as minor products, alpha-terpineol, beta-pinene, alpha-pinene, sabinene and myrcene (PubMed:17557809). {ECO:0000269|PubMed:17557809}. | Salvia fruticosa (Greek sage) |
A6XH06 | SABS1_SALPM | MPLNSLHNLERKPSKAWSTSCTAPAARLQASFSLQQEEPRQIRRSGDYQPSLWDFNYIQSLNTPYKEQRYVNRQAELIMQVRMLLKVKMEAIQQLELIDDLQYLGLSYFFPDEIKQILSSIHNEHRYFHNNDLYLTALGFRILRQHGFNVSEDVFDCFKTEKCSDFNANLAQDTKGMLQLYEASFLLREGEDTLELARRFSTRSLREKLDEDGDEIDEDLSSWIRHSLDLPLHWRIQGLEARWFLDAYARRPDMNPLIFKLAKLNFNIVQATYQEELKDVSRWWNSSCLAEKLPFVRDRIVECFFWAIGAFEPHQYSYQRKMAAIIITFVTIIDDVYDVYGTLEELELFTDMIRRWDNISISQLPYYMQVCYLALYNFVSERAYDILKDQHFNSIPYLQRSWVSLVEGYLKEAYWYYNGYKPSLEEYLNNAKISISAPTIISQLYFTLANSTDETVIESLYEYHNILYLSGTILRLADDLGTSQHELERGDVPKAIQCYMKDTNASEREAVEHVKFLIRETWKEMNTVTTASDCPFTDDLVAVATNLARAAQFIYLDGDGHGVQHSEIHQQMGGLLFQPYV | 4.2.3.-; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:17557809}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17557809}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into sabinene, and, as minor products, myrcene (PubMed:17557809). {ECO:0000269|PubMed:17557809}. | Salvia pomifera (Apple sage) |
A6XIP3 | GP_HAZVJ | MEGSYWWLSLLALLAWGANGESTSPAETSPAPTTPNPPVVNPSLRRKIVNQRILSAMGMDSDPSNEALNGVCQSIHSNGCNANELKLRLADFFIDTNSSQCYDEILVKKPCSSLTPAHNSHWVPRGLDKSEVDKIFDTKLKLFFSQSRKVTCLSASALNPSQFVKHFQVKIQETSGPAKQSLRSLHCVNLVWSHSHKGEKEVVHVLQSAVPVKLKNCLAMLNFRQCYYNQQSEGPVVVPSYQHNGEKWVTGAYTMTVEVDKHADGPCEISTTCITEGSEIKPGVHSLRGFKTTLVIHGKRNTGRRLLSSSNARQECSSGTFLGEGGSAQVVGPKNDGPGDHITFCNGSVVTKIRLGQEHGCYTVRRIKTYRNCRPEEGSSACEVDDELKPCGAQKCMNVHLSVKGLVKTSRGSNVQVHSCDKDCLIQIPEGFGDIQIDCPGGTQHYLESNVLDVDCPMYNRLGGLMLYFCRMSHRPRTCLALFIWLGAGYGITCIAGYMVYYAILALSMLTRCLKRKYMVKGDFCLKCEQKCVTSLDQTLHDESCSYNICPYCGNRLPEEGLRRHVPSCPKRKQRLEEIDLYLDYLLVPCPLHFALSTAVKLGTLLKRLSWVTVFLCLFLTAIAPVQGQVTTSPVLPSNQSTECTLLPPPVFLIFSAVLMSKTLKRMGPVNKVGAAGHSARRTNSPKNLYKSKQIANTKSGPREPRRRVVVKALLILTASSALQSIHLAQAFDSGSLPEGAWEEEMQLVQGCNQECSLEEDECSCPDGQSMTRKLLFFKGLNSAASKMASSHRLLTSVSIDTPWGAIKVESTYKPRLASSNIQLAWNSIEEQGDKVILSGKSTSIIKLEEKTGMQWSLGSESAAEEKRLLVSILDYTQVYSSTFQYITGDRTVSEWPKATCTGDCPDRCGCSTSSCLYKSWPHSRNWRCNPTWCWGVGTGCTCCGVDILRPFNKYFVTKWTTEYVRTDVLVCVELTDQERHCDVVEAGSQFVIGPVRVVVSDPQNVQTKLPSEILTIQKLEGNQVVDIMHATSIVSAKNACKLQSCTHGSPGDMQILHTDNLIQHSHDGGLNLADLNPLVNSTWMSWEGCDLDYYCTTGSWPSCTYTGINSENTESFDNLLNTESNLCERFHFHSKRISASGSTLQMDLKGRPNSGGGELSVLVDVKGLELHSKKISLKGLSFKTLSCSGCYACSSGLSCTVEVRIERPDEFTVHLRSVSPDIAVAEGSIIARRMTGGPLSRLRAFAVRKVKKICFEIVEKSYCKDCKNEDTTKCIEVELQPPKDILLEHKGTIIKRQNETCVSGLQCWTESASSFVSGVGSFFRNYLGSITLGIVLTLLPVAVVLLFFCYGDKLFKLCSCFRCCRGLSRGKVRKELDEDELRNKLKKFSKEGELFGKEKKDARTIALLLSGKGKNYKELV | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF20682;PF01561;PF20726;PF07948; | 1.10.8.1320; | Nairovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic cleavages by host furin-like protease and MBTPS1/S1P endopeptidase yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}. | SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Note=Interaction between glycoprotein C and glycoprotein N is essential for proper targeting of glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Non-Structural protein M]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Glycoprotein N and glycoprotein C interact with each other and are present at the surface of the virion. Glycoprotein N probably locks the Gn-Gc complex in a prefusion state. Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. {ECO:0000250|UniProtKB:Q8JSZ3}.; FUNCTION: [Glycoprotein C]: Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion (By similarity). The spikes at the surface of the virion are formed by an N-terminal extension of glycoprotein C (By similarity). Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (By similarity). Exposure to potassium is necessary for the conformational change leading to fusion (PubMed:29678879). {ECO:0000250|UniProtKB:H2AM12, ECO:0000250|UniProtKB:Q8JSZ3, ECO:0000269|PubMed:29678879}. | Hazara virus (isolate JC280) |
A6XKM2 | CXA1_URSAM | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLATGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI | null | null | cell-cell signaling [GO:0007267]; establishment of mitotic spindle orientation [GO:0000132]; heart development [GO:0007507]; microtubule-based transport [GO:0099111]; negative regulation of cell growth [GO:0030308]; negative regulation of gonadotropin secretion [GO:0032277]; negative regulation of trophoblast cell migration [GO:1901164]; positive regulation of gene expression [GO:0010628]; positive regulation of mesodermal cell differentiation [GO:1905772]; positive regulation of morphogenesis of an epithelium [GO:1905332]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein localization [GO:0008104]; signal transduction [GO:0007165] | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; connexin complex [GO:0005922]; endoplasmic reticulum [GO:0005783]; intercalated disc [GO:0014704]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | beta-catenin binding [GO:0008013]; gap junction channel activity involved in cell communication by electrical coupling [GO:1903763]; gap junction hemi-channel activity [GO:0055077]; monoatomic ion transmembrane transporter activity [GO:0015075]; tubulin binding [GO:0015631] | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity. Phosphorylation at Ser-368 by PRKCD triggers its internalization into small vesicles leading to proteasome-mediated degradation (By similarity). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302, ECO:0000250|UniProtKB:Q6TYA7}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the level of functional Cx43 gap junctions at the plasma membrane. May be desumoylated by SENP1 or SENP2 (By similarity). {ECO:0000250|UniProtKB:P17302}.; PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial gap junction in arteries, it augments channel permeability and may regulate of smooth muscle cell to endothelial cell communication. {ECO:0000250|UniProtKB:P23242}.; PTM: Acetylated in the developing cortex; leading to delocalization from the cell membrane. {ECO:0000250|UniProtKB:P23242}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}. | null | null | null | null | null | FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P23242}. | Ursus americanus (American black bear) (Euarctos americanus) |
A6XMY0 | ARA1_HYAAR | MERRTLLVVLLVCSCVVAAAAEASPSRWPSPGRPRPFPGRPKPIFRPRPCNCYAPPCPCDRWRH | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; immune system process [GO:0002376]; killing of cells of another organism [GO:0031640] | null | chitin binding [GO:0008061] | null | null | null | PTM: Disulfide bonds are important for activity especially against Gram-negative bacteria, since the linearization of the peptide causes a strong decrease of activity on these bacteria. {ECO:0000269|PubMed:23326415}. | null | null | null | null | null | null | FUNCTION: Antimicrobial peptide that has a large activity spectrum with activity against Gram-positive, Gram-negative bacteria, as well as against fungi (PubMed:17658600, PubMed:23326415). Shows activity at micromolar concentrations (PubMed:17658600, PubMed:23326415). Displays minimal inhibitory concentration (MIC) values lower than minimal bactericidal concentrations (MBC) (PubMed:17658600). Synthetic peptides with similar activities than the full length peptide (composed of the first 23 or 25 amino acids (Arasin 1(26-48) or Arasin 1(26-50))) may have a dual mode of action depending on the peptide concentrations (PubMed:23326415, PubMed:26860543). At MIC concentrations, the peptide penetrates into the cytoplasm of target cells (tested on the Gram-negative E.Coli) (PubMed:26860543). The two inner membrane proteins YgdD and SbmA may be required for this uptake (PubMed:26860543). At concentrations higher than MIC, arasin may act by disrupting membranes (PubMed:23326415). Full-length and N-terminal peptides do not show hemolytic activity (PubMed:23326415). {ECO:0000269|PubMed:17658600, ECO:0000269|PubMed:23326415, ECO:0000269|PubMed:26860543}. | Hyas araneus (Atlantic lyre crab) (Great spider crab) |
A6XNC6 | UGFGT_MEDTR | MSTFKNEMNGNNLLHVAVLAFPFGTHAAPLLSLVKKIATEAPKVTFSFFCTTTTNDTLFSRSNEFLPNIKYYNVHDGLPKGYVSSGNPREPIFLFIKAMQENFKHVIDEAVAETGKNITCLVTDAFFWFGADLAEEMHAKWVPLWTAGPHSLLTHVYTDLIREKTGSKEVHDVKSIDVLPGFPELKASDLPEGVIKDIDVPFATMLHKMGLELPRANAVAINSFATIHPLIENELNSKFKLLLNVGPFNLTTPQRKVSDEHGCLEWLDQHENSSVVYISFGSVVTPPPHELTALAESLEECGFPFIWSFRGDPKEKLPKGFLERTKTKGKIVAWAPQVEILKHSSVGVFLTHSGWNSVLECIVGGVPMISRPFFGDQGLNTILTESVLEIGVGVDNGVLTKESIKKALELTMSSEKGGIMRQKIVKLKESAFKAVEQNGTSAMDFTTLIQIVTS | 2.4.1.- | null | flavonoid biosynthetic process [GO:0009813]; phenylpropanoid metabolic process [GO:0009698] | null | UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89.8 uM for kaempferol {ECO:0000269|PubMed:17437063}; KM=28.7 uM for quercitin {ECO:0000269|PubMed:17437063}; KM=52 uM for pelargonidin {ECO:0000269|PubMed:17437063}; KM=71.8 uM for cyanidin {ECO:0000269|PubMed:17437063}; KM=1.5 uM for apigenin {ECO:0000269|PubMed:17437063}; KM=36.7 uM for genistein {ECO:0000269|PubMed:17437063}; KM=1.6 uM for daidzein {ECO:0000269|PubMed:17437063}; KM=11.7 uM for biochanin A {ECO:0000269|PubMed:17437063}; KM=1.5 uM for formononetin {ECO:0000269|PubMed:17437063}; Vmax=1.583 umol/min/ug enzyme toward kaempferol {ECO:0000269|PubMed:17437063}; Vmax=0.8557 umol/min/ug enzyme toward quercitin {ECO:0000269|PubMed:17437063}; Vmax=0.2025 umol/min/ug enzyme toward pelargonidin {ECO:0000269|PubMed:17437063}; Vmax=0.1698 umol/min/ug enzyme toward cyanidin {ECO:0000269|PubMed:17437063}; Vmax=0.0688 umol/min/ug enzyme toward apigenin {ECO:0000269|PubMed:17437063}; Vmax=1.205 umol/min/ug enzyme toward genistein {ECO:0000269|PubMed:17437063}; Vmax=0.053 umol/min/ug enzyme toward daidzein {ECO:0000269|PubMed:17437063}; Vmax=0.3666 umol/min/ug enzyme toward biochanin A {ECO:0000269|PubMed:17437063}; Vmax=0.0879 umol/min/ug enzyme toward formononetin {ECO:0000269|PubMed:17437063}; | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. | null | null | FUNCTION: Catalyzes the glycosylation of flavonoids at the 3-O-position. Glycosylates the 7-O-position if the 3-O-position is not available. Also able to perform 3-O-glycosylation of anthocyanidins. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A6Y9S5 | LGA1_HYPJE | MAPPSLPCGIYAPTMTFFHPESEDIDIPTIKHHAQRLAKAGLAGLVVMGSNGEAVHCTRDEKIAVLSATREALDAAGFQSVPVLFGATEGSVRGTIELCKLAAAAGAAAALVLPPSYYRAQTDEASIEAYFVAVADASPIPLVLYNYPGAVSGIDMDSDLLIRLAQHKNIVGTKFTCGNTGKLTRVALATDAKTPFRDGSGYMAFGGMCDFTLQTLVSGGSGIIAGGANVMPKLCVKVWDSYSQGNRDEAEKLQKVLSRGDWPLTKAAIAGTKSAIQTYYGYGGYPRRPLKRLEQARVSAIEEGIREAMEIEKTL | 4.1.2.54 | null | D-galacturonate catabolic process [GO:0019698] | null | 4-hydroxy-tetrahydrodipicolinate synthase activity [GO:0008840]; aldehyde-lyase activity [GO:0016832] | PF00701; | 3.20.20.70; | DapA family | null | null | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-L-galactonate = L-glyceraldehyde + pyruvate; Xref=Rhea:RHEA:38107, ChEBI:CHEBI:15361, ChEBI:CHEBI:27975, ChEBI:CHEBI:75545; EC=4.1.2.54; Evidence={ECO:0000269|PubMed:17609199}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for 2-dehydro-3-deoxy-L-galactonate {ECO:0000269|PubMed:17609199}; KM=3.8 mM for D-glycero-3-deoxy-pentulosonate {ECO:0000269|PubMed:17609199}; KM=0.5 mM for pyruvate {ECO:0000269|PubMed:17609199}; KM=1.2 mM for L-glyceraldehyde {ECO:0000269|PubMed:17609199}; KM=6.5 mM for glycolaldehyde {ECO:0000269|PubMed:17609199}; Vmax=20.3 umol/min/mg enzyme with 2-dehydro-3-deoxy-L-galactonate as substrate {ECO:0000269|PubMed:17609199}; Vmax=12.5 umol/min/mg enzyme with D-glycero-3-deoxy-pentulosonate as substrate {ECO:0000269|PubMed:17609199}; Vmax=6.5 umol/min/mg enzyme with pyruvate and L-glyceraldehyde as substrates {ECO:0000269|PubMed:17609199}; Vmax=0.9 umol/min/mg enzyme with glycolaldehyde as substrate {ECO:0000269|PubMed:17609199}; | PATHWAY: Carbohydrate acid metabolism. {ECO:0000269|PubMed:17609199}. | null | null | FUNCTION: Mediates the conversion of 2-dehydro-3-deoxy-L-galactonate to pyruvate and L-glyceraldehyde in D-galacturonate catabolic process. {ECO:0000269|PubMed:17609199, ECO:0000269|PubMed:18768163}. | Hypocrea jecorina (Trichoderma reesei) |
A6YFB5 | HTRA1_XENLA | MTMLWLAVLLTCGAPAALLPTSGVGCPARCDPSSCSPAPTNCQSGETALRCGCCSVCAAAENERCGEGPEDPLCASGLRCVRNGGVTRCQCPSNQPVCGSDGKTYSSLCRLQAESKAVQGRGVAAIIPIQRGDCQQGQKDPDSPRYKYNFIADVVEKIAPAVVHIELFRILPFFKREVPAASGSGFIVSEDGLILTNAHVVTNKHRLKVERSDGSTYDAQIIDVDEKADIALIKIKAKGKLPVLLLGRSEELRPGEFVVAIGSPFSLQNTVTTGIVSTAQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVVGINTLKVTAGISFAIPSDKIRKFMAESHNRQSTGQGTKKKKYLGIRMMSLSQGKLKELKEQVKDFPENTSGAYIVEVLPDTPAEEAGLKEGDIIISISGKTVTSSSEVSEAIKKEGTLQMVIRRGNEDIPISVTPKEIEF | 3.4.21.- | null | positive regulation of apoptotic process [GO:0043065]; programmed cell death [GO:0012501]; proteolysis [GO:0006508] | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | growth factor binding [GO:0019838]; serine-type endopeptidase activity [GO:0004252] | PF00219;PF07648;PF17820;PF13365; | 2.30.42.10;2.40.10.120;3.30.60.30;4.10.40.20; | Peptidase S1C family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000269|PubMed:17681134}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}. | null | null | null | null | null | FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans such as biglycan, syndecan-4 and glypican-4. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Consequently, facilitates inductive processes in the developing embryo, such as posteriorization, mesoderm induction and neuronal differentiation. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. Consequently, may regulate many physiological processes. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. {ECO:0000269|PubMed:17681134}. | Xenopus laevis (African clawed frog) |
A6YP92 | ARX_RAT | MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRTDQEKAMQGSPKGSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELGGPGGVAHPEERLSAASGPGSAPAAGGGTGTEEDEEELLEDEEDEDEEEELLEDDEEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAGSDSEEGLLKRKQRRYRTTFTSYQLEELERAFQKTHYPDVFTREELAMRLDLTEARVQVWFQNRRAKWRKREKAGAQTHPPGLPFPGPLSATHPLSPYLDASPFPPHHPALDSAWTAAAAAAAAAFPSLPPPPGSASLPPSGAPLGLSTFLGAAVFRHPAFISPAFGRLFSTMAPLTSASTAAALLRQPTPAVEGAVASGALADPATAAADRRASSIAALRLKAKEHAAQLTQLNILPGTSTGKEVC | null | null | axon guidance [GO:0007411]; cell proliferation in forebrain [GO:0021846]; cerebral cortex GABAergic interneuron migration [GO:0021853]; cerebral cortex tangential migration [GO:0021800]; embryonic olfactory bulb interneuron precursor migration [GO:0021831]; epithelial cell fate commitment [GO:0072148]; forebrain development [GO:0030900]; globus pallidus development [GO:0021759]; interneuron migration [GO:1904936]; lipid digestion [GO:0044241]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron development [GO:0048666]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; organ growth [GO:0035265]; positive regulation of gene expression [GO:0010628]; positive regulation of organ growth [GO:0046622]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of epithelial cell proliferation [GO:0050678]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35137, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. | null | null | null | null | null | FUNCTION: Transcription factor. Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C. Positively modulates transcription of KDM5C. Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcription regulator ZNF711; synergy may be related to enrichment of histone H3K4me3 in regulatory elements. Required for normal brain development (By similarity). Plays a role in neuronal proliferation, interneuronal migration and differentiation in the embryonic forebrain. May also be involved in axonal guidance in the floor plate (By similarity). {ECO:0000250|UniProtKB:O35085, ECO:0000250|UniProtKB:Q96QS3}. | Rattus norvegicus (Rat) |
A6YQT5 | RPOA_PRRSV | MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVPELGVLGLFYRPEEPLRWTLPRAFPTVECSPAGACWLSAIFPIARMTSGNLNFQQRMVRVAAEIYRAGQLTPTVLKTLQVYERGCRWYPIVGPVPGVGVYANSLHVSDKPFPGATHVLTNLPLPQRPKPEDFCPFECAMADVYDIGRGAVMYVAGGKVSWAPRGGNEVKFEPIPKELKLVANRLHTSFPPHHVVDMSRFTFMTPGSGVSMRVEYQHGCLPADTVPEGNCWWRLFDSLPPEVQYKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTDTHGPIVIQYFSVKESWIRHLKLVEEPSLPGFEDLLRIRVEPNTSPLAGKDEKIFRFGSHKWYGAGKRARKPRSGATTMVAHHASSAHETRQATKHEGAGANKAEHLKRYSPPAEGNCGWHCISAIANRMVNSNFETTLPERVRPSDDWATDEDLVNTIQILRLPAALDRNGACGSAKYVLKLEGEHWTVSVIPGMSPTLLPLECVQGCCEHKGGLVSPDAVEISGFDPACLDRLAKVMHLPSSTIPAALAELSDDSNRPVSPAATTWTVSQFYARHRGGDHHDQVCLGKIISLCQVIEDCCCHQNKTNRATPEEVAAKIDQYLRGATSLEECLAKLERVSPPSAADTSFDWNVVLPGVEAANQTTEQPHVNSCCTLVPPVTQEPLGKDSVPLTAFSLSNCYYPAQGDEVHHRERLNSVLSKLEEVVLEEYGLMSTGLGPRPVLPSGLDELKDQMEEDLLKLANTQATSEMMAWAAEQVDLKAWVKSYPRWTPPPPPPRVQPRRTKSVKSLPEGKPVPAPRRKVRSDCGSPVLMGDNVPNGSEETVGGPLNFPTPSEPMTPMSEPVLVPASRRVPKLMTPLSGSAPVPAPRRTVTTTLTHQDEPLDLSASSQTEYEAFPLAPSQNMGILEAGGQEVEEVLSEISDILNDTNPAPVSSSSSLSSVKITRPKYSAQAIIDSGGPCSGHLQKEKEACLSIMREACDASKLGDPATQEWLSRMWDRVDMLTWRNTSAYQAFRILNGRFEFLPKMILETPPPHPCGFVMLPRTPAPSVSAESDLTIGSVATEDVPRILGKIGDTDELLDRGPSAPSKGEPVCDQPAKDPRMSPRESDESMIAPPADTGGVGSFTDLPSSDGVDVDGGGPLRTVKTKAGRLLDQLSCQVFSLVSHLPIFFSHLFKSDSGYSPGDWGFAAFTLFCLFLCYSYPFFGFAPLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGTACEFDSPECRNVLHSFELLKPWDPVRSLVVGPVGLGLAILGRLLGGARYIWHFLLRLGIVADCILAGAYVLSQGRCKKCWGSCVRTAPNEIAFNVFPFTRATRSSLIDLCDRFCAPKGMDPIFLATGWRGCWTGRSPIEQPSEKPIAFAQLDEKRITARTVVAQPYDPNQAVKCLRVLQAGGAMVAEAVPKVVKVSAIPFRAPFFPAGVKVDPECRIVVDPDTFTTALRSGYSTANLVLGTGDFAQLNGLKIRQISKPSGGGPHLIAALHVACSMALHMLAGVYVTAVGSCGTGTNDPWCTNPFAVPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGLQEIALVVLIFVSIGGMAHRLSCKADMLCILLAIASYVWVPLTWLLCVFPCWLRWFSLHPLTILWLVFFLISVNIPSGILAVVLLVSLWLLGRYTNIAGLVTPYDIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTQKPSLNTVNVVGSSMGSGGVFTIDGKIKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGVAPKAQFCEDGWTGRAYWLTSSGVEPGVIGNGFAFCFTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVKPIKLSELSEFFAGPKVPLGDVKIGSHIIKDTCEVPSDLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVGFFILNEILPAVLVRSVFSFGMFVLSWLTPWSAQVLMIRLLTAALNRNRWSLGFYSLGAVTSFVADLAVTQGHPLQVVMNLSTYAFLPRMMVVTSPVPVIACGVVHLLAIILYLFKYRCLHNVLVGDGVFSSAFFLRYFAEGKLREGVSQSCGMSHESLTGALAMRLTDEDLDFLTKWTDFKCFVSASNMRNAAGQFIEAAYAKALRIELAQLVQVDKVRGTMAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSKMTVARVVDPTPAPPPVPVPIPLPPKVLENGPNAWGDEDRLSKKKRRRMEAVGIFVMDGKKYQKFWDKNSGDVFYEEVHISTDEWECLRTGDPVDFDPETGIQCGHITIEDKVYNVFTSPSGRRFLVPANPENRRAQWEAAKLSVEQALGMMNVDGELTAKELEKLKRIIDKLQGLTKEQCLNCLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPVARPVDGGVVLLRSAVPSLIDVLISGADASPKLLARHGPGNTGIDGTLWDFEAEATKEEVALSAQIIQACDIRRGDAPEIGLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPSGFELYVPTIPASVLDYLDSRPDCPKQLTEHGCEDAALRDLSKYDLSTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFPTKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAALSGVTQGFMKKAFNSPIALGKNKFKELQAPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSVSNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPSMPNYHWWVEHLNLMLGFQTDPKKTTITDSPSFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCARKDGYSFPGPPFFLSMWEKLRSNHEGKKSRMCGYCGAPAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCSECEPPLGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVDLPDGDYASTALLPTCKEINMVAVASNVLRSRFIIGPPGAGKTHWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPAPSRTGPWVRILAGGWCPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLMSMVNTTRVTYVEKPVRYGQVLTPYHRDREDGAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQLQSMFDLPAKGTPVNLAVHRDEQLIVLDRNNREITVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGFYFSPDLTQFAKLPVELAPHWPVVTTQNNERWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVRGEAQVLPETVFSTGRIEVDCREYLDDREREVAESLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGKAAKAVCTLTDVYLPDLEAYLHPETQSRCWKVMLDFKEVRLMVWKDKTAYFQLEGRHFTWYQLASYASYIRVPVNSTVYLDPCMGPALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGEDWEDYNDAFRARQKGKIYKANATSMRFHFPPGPVIEPTLGLN | 2.7.7.48; 3.4.19.12; 3.4.21.-; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | null | induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:0039579]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral protein processing [GO:0019082]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA helicase activity [GO:0003724]; RNA nuclease activity [GO:0004540]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252] | PF16749;PF19215;PF14757;PF14756;PF05410;PF05411;PF05412;PF05579;PF00680;PF01443; | 3.90.70.160;4.10.80.390;3.30.1330.220;2.30.31.30;3.90.70.70;3.40.50.300;3.90.70.60;2.40.10.10; | Arteriviridae polyprotein family | PTM: [Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and Nsp1-beta. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are processed, which represents the minor pathway. The major pathway occurs when nsp2 acts as a cofactor for nsp4. {ECO:0000250|UniProtKB:Q9WJB2}. | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:35858300}. Host cytoplasm {ECO:0000269|PubMed:35858300}. Note=Accumulates mainly in the host cytoplasm in early infection and then mostly in the host nucleus. {ECO:0000269|PubMed:35858300}.; SUBCELLULAR LOCATION: [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Non-structural protein 5-6-7]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q04561}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Serine protease nsp4]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Helicase nsp10]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp11]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host nucleus {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Non-structural protein 12]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Helicase nsp10]: 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; CATALYTIC ACTIVITY: [Helicase nsp10]: 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=3.6.4.13; CATALYTIC ACTIVITY: [Nsp2 cysteine proteinase]: 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; CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp11]: Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284, ChEBI:CHEBI:173079, ChEBI:CHEBI:173080; Evidence={ECO:0000250|UniProtKB:P19811}; | null | null | null | null | FUNCTION: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis (By similarity). Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1 (By similarity). Repurposes the host antiviral stress granules into a proviral platform to counteract the EIF2AK2/PKR restriction, thereby regulating the host inflammatory response (PubMed:35858300). {ECO:0000250|UniProtKB:Q04561, ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:35858300}.; FUNCTION: [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28}.; FUNCTION: [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF-kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250|UniProtKB:Q04561}.; FUNCTION: [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). Also plays a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811, ECO:0000250|UniProtKB:Q04561}. | Porcine reproductive and respiratory syndrome virus (PRRSV) |
A6YRY8 | RSSA_SHEEP | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSARPFTEDWSAAPTAQATEWVGTTSELS | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; structural constituent of ribosome [GO:0003735] | PF16122;PF00318; | null | Universal ribosomal protein uS2 family | PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions. {ECO:0000255|HAMAP-Rule:MF_03016}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03016}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03016}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Co-localizes with PPP1R16B in the cell membrane. {ECO:0000255|HAMAP-Rule:MF_03016}. | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA. {ECO:0000255|HAMAP-Rule:MF_03016}. | Ovis aries (Sheep) |
A6YSL1 | RNC1_MAIZE | MGPPAMAFQALTLTPLPFSLHSSSRRVRVLAVAADQTPPPAPPSEPANSPSRLLRELAQRKKAVSPKKKHPPRRFILKPPLDDERLTRRFLSSPQLSLKALPLLSSCLPSAPLSTADRTWMDEYLLEAKQALGYPLAPSETLGEGDDCPARHFDVLFYLAFQHLDPSSERTRMRHVRNGHSRLWFLGQYVLELAFCEFFLQRYPRESPGPMRERVFALIGKKVLPRWLKAASLHNLVFPYDDLDKMIRKDREPPSKAVFWAIFGAIYLCFGMPEVYRVLFEAFGMDPDDESCQPKLRRQLEDVDYVSVEFEKRQLTWQDVAAYRPPPDALFAHPRLFRACVPPGMHRFRGNIWDFDSRPKVMTTLGYPLPMNDRIPEITEARNIELGLGLQLCFLHPSKHKFEHPRFCYERLEYVGQKIQDLVMAERLLMKHLDAPGRWLAEKHRRTLMNKYCGRYLRDKHLQHYIIYGETVQDRFEHNRRLRNPSTTSVQQALHGLAYCVYGKPDVRRLMFEVFDFEQVQPKAV | null | null | Group II intron splicing [GO:0000373]; mRNA processing [GO:0006397]; regulation of gene expression [GO:0010468]; ribosome biogenesis [GO:0042254]; RNA processing [GO:0006396] | chloroplast stroma [GO:0009570]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | double-stranded RNA binding [GO:0003725]; ribonuclease III activity [GO:0004525]; single-stranded RNA binding [GO:0003727] | PF00636; | 1.10.1520.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:17693527}. | null | null | null | null | null | FUNCTION: Binds specific group II introns in chloroplasts and facilitates their splicing. Acts on both subgroup IIA and subgroup IIB introns. The substrates of the subgroup II also require the CRM domain proteins CAF1 or CAF2. Binds both single-stranded and double-stranded RNA non-specifically, but lacks endonuclease activity. Required for plastid ribosome biogenesis. {ECO:0000269|PubMed:17693527}. | Zea mays (Maize) |
A6ZM04 | PIF1_YEAS7 | MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNSSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYKKVRRSRKHLRRWENIGALVVDEISMLDAELLDKLDFIARKIRKNHQPFGGIQLIFCGDFFQLPPVSKDPNRPTKFAFESKAWKEGVKMTIMLQKVFRQRGDVKFIDMLNRMRLGNIDDETEREFKKLSRPLPDDEIIPAELYSTRMEVERANNSRLSKLPGQVHIFNAIDGGALEDEELKERLLQNFLAPKELHLKVGAQVMMVKNLDATLVNGSLGKVIEFMDPETYFCYEALTNDPSMPPEKLETWAENPSKLKAAMEREQSDGEESAVASRKSSVKEGFAKSDIGEPVSPLDSSVFDFMKRVKTDDEVVLENIKRKEQLMQTIHQNSAGKRRLPLVRFKASDMSTRMVLVEPEDWAIEDENEKPLVSRVQLPLMLAWSLSIHKSQGQTLPKVKVDLRRVFEKGQAYVALSRAVSREGLQVLNFDRTRIKAHQKVIDFYLTLSSAESAYKQLEADEQVKKRKLDYAPGPKYKAKSKSKSNSPAPISATTQSNSGIAAMLQRHSRKRFQLKKESNSNQVHSLVSDEPRGQDTEDHILE | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03176}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03176}; Note=Mg(2+). To a lesser extent, can also use Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03176}; | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; mitochondrial genome maintenance [GO:0000002]; negative regulation of telomere maintenance via telomerase [GO:0032211]; telomere maintenance [GO:0000723] | mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; G-quadruplex DNA binding [GO:0051880]; telomerase inhibitor activity [GO:0010521] | PF05970;PF21530; | 3.40.50.300; | Helicase family, PIF1 subfamily | PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus {ECO:0000250}. Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03176}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. Note=Bound to the mitochondrial inner membrane either directly or indirectly via a protein complex. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03176}; | null | null | null | null | FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing (By similarity). {ECO:0000255|HAMAP-Rule:MF_03176}. | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZU07 | ATG1_YEAS7 | MGDIKNKDHTTSVNHNLMASAGNYTAEKEIGKGSFATVYRGHLTSDKSQHVAIKEVSRAKLKNKKLLENLEIEIAILKKIKHPHIVGLIDCERTSTDFYLIMEYCALGDLTFLLKRRKELMENHPLLRTVFEKYPPPSENHNGLHRAFVLSYLQQLASALKFLRSKNLVHRDIKPQNLLLSTPLIGYHDSKSFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVVFEMCCGTPPFRASNHLELFKKIKRANDVITFPSYCNIEPELKELICSLLTFDPAQRIGFEEFFANKVVNEDLSSYELEDDLPELESKSKGIVESNMFVSEYLSKQPKSPNSNLAGHQSMADNPAELSDALKNSNILTAPAVKTDHTQAVDKKASNNKYHNSLVSDRSFEREYVVVEKKSVEVNSLADEVAQAGFNPNPIKHPTSTQNQNVLLNEQFSPNNQQYFQNQGENPRLLRATSSSSGGSDGSRRPSLVDRRLSISSLNPSNALSRALGIASTRLFGGANQQQQQQQITSSPPYSQTLLNSQLFHELTENIILRIDHLQHPETLKLDNTNIVSILESLAAKAFVVYSYAEVKFSQIVPLSTTLKGMANFENRRSMDSNAIAEEQDSDDAEEEDETLKKYKEDCLSTKTFGKGRTLSATSQLSATFNKLPRSEMILLCNEAIVLYMKALSILSKSMQVTSNWWYESQEKSCSLRVNVLVQWLREKFNECLEKADFLRLKINDLRFKHASEVAENQTLEEKGSSEEPVYLEKLLYDRALEISKMAAHMELKGENLYNCELAYATSLWMLETSLDDDDFTNAYGDYPFKTNIHLKSNDVEDKEKYHSVLDENDRIIIRKYIDSIANRLKILRQKMNHQN | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709] | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | PTM: Autophosphorylated at Thr-226 and Ser-390. The phosphorylation state may play a role in the induction of protein degradation upon starvation. Phosphorylation at Thr-226 within the activation loop is required for protein kinase activity whereas phosphorylation at Ser-34 leads to inhibition of kinase activity. Phosphorylation of Ser-508 and Ser-515 by PKA is required to induce autophagy but not for kinase activity. {ECO:0000250|UniProtKB:P53104}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. Note=Formes punctate structures in starvation conditions only when ATG13 and ATG17 were both present. Localizes to both the isolation membrane (IM) and the vacuole-isolation membrane contact site (VICS) during IM expansion. The IM is a membrane sac generated from the pre-autophagosomal structure that ultimately expands to become a mature autophagosome. {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; 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:P53104}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. Finally, ATG1 is also required for the maintenance of cell viability under starvation and for glycogen storage during stationary phase. Plays a role in genome stability through suppression of abnormal mitosis under starvation, and in regulation of filamentous growth. {ECO:0000250|UniProtKB:P53104}. | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZXH8 | ATG9_YEAS7 | MERDEYQLPNSHGKNTFLSRIFGLQSDEVNPSLNSQEMSNFPLPDIERGSSLLHSTNDSREDVDENDLRVPESDQGTSTEEEDEVDEEQVQAYAPQISDGLNGDHQLNSVTSKENVLETEKSNLERLVEGSTDDSVPKVGQLSSEEEEDNEFINNDGFDDDTPLFQKSKIHEFSSKKSNTIEDGKRPLFFRHIYQNNRPQRDTQKLFTSSNAIHHDKDKSANNGPRNINGNQKHGTKYFGSATQPRFTGSPLNNTNRFTKLFPLRKPNLLSNISVLNNTPEDRINTLSVKERALWKWANVENLDIFLQDVYNYYLGNGFYCIILEKILNICTLLFVVFVSTYMGHCVDYSKLPTSHRVSDIIIDKCYSNSITGFTKFFLWMFYFFVILKIVQLYFDVQKLSELQNFYKYLLNISDDELQTLPWQNVIQQLMYLKDQNAMTANVVEVKAKNRIDAHDVANRIMRRENYLIALYNSDILNLSLPIPLFRTNVLTKTLEWNINLCVMGFVFNESGFIKQSILKPSQREFTREELQKRFMLAGFLNIILAPFLVTYFVLLYFFRYFNEYKTSPGSIGARQYTPIAEWKFREYNELYHIFKKRISLSTTLANKYVDQFPKEKTNLFLKFVSFICGSFVAILAFLTVFDPENFLNFEITSDRSVIFYITILGAIWSVSRNTITQEYHVFDPEETLKELYEYTHYLPKEWEGRYHKEEIKLEFCKLYNLRIVILLRELTSLMITPFVLWFSLPSSAGRIVDFFRENSEYVDGLGYVCKYAMFNMKNIDGEDTHSMDEDSLTKKIAVNGSHTLNSKRRSKFTAEDHSDKDLANNKMLQSYVYFMDDYSNSENLTGKYQLPAKKGYPNNEGDSFLNNKYSWRKQFQPGQKPELFRIGKHALGPGHNISPAIYSTRNPGKNWDNNNNGDDIKNGTNNATAKNDDNNGNNDHEYVLTESFLDSGAFPNHDVIDHNKMLNSNYNGNGILNKGGVLGLVKEYYKKSDVGR | null | null | lipid transport [GO:0006869]; protein localization to phagophore assembly site [GO:0034497] | autophagosome [GO:0005776]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; phagophore assembly site membrane [GO:0034045] | null | PF04109; | null | ATG9 family | PTM: Phosphorylated by ATG1; phosphorylation is required for autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Phosphorylation by ATG1 regulates ATG18 interaction and preautophagosome elongation. Phosphorylation at Ser-122 is required for selective autophagy by regulating anterograde trafficking and interaction with ATG23 and ATG27. Phosphorylation at Ser-122 prevents ubiquitination by the SCF(MET30) complex. {ECO:0000250|UniProtKB:Q12142}.; PTM: Ubiquitinated by the SCF(MET30) complex in normal conditions, leading to its degradation by the proteasome, thereby preventing inappropriate induction of autophagy. Ubiquitination by the SCF(MET30) complex is prevented by phosphorylation at Ser-122. {ECO:0000250|UniProtKB:Q12142}. | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Note=The vast majority of ATG9 exists on cytoplasmic mobile vesicles (designated ATG9 vesicles) that were derived from the Golgi apparatus in a process involving ATG23 and ATG27. The peripheral pool of ATG9 partially colocalizes within tubulovesicular clusters adjacent to mitochondria. It appears that membrane that contains ATG9 is delivered to the autophagosome from the Golgi-endosomal system rather than from the ER or mitochondria. Within the PAS, localizes at the edge of the isolation membrane. ATG9 cycling is regulated by at least the conserved oligomeric Golgi (COG) complex, ARP2, HOG1, PIK1, SEC2, SEC9, SSO1 and SSO2. {ECO:0000250|UniProtKB:Q12142}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088; Evidence={ECO:0000250|UniProtKB:Q12142}; | null | null | null | null | FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. Recruits vesicle-tethering proteins TRS85 and YPT1 to the autophagosome formation site. Recruits also ATG23 and ATG8 to the PAS. {ECO:0000250|UniProtKB:Q12142}. | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZY89 | ARO1_YEAS7 | MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVATPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAETEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTKKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKIIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKAPFKAIFDAVTKE | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A7B558 | NANY_MEDG7 | MKTVGYAIVGTGYFGAELGRIMKEQEGARIVAVLDPENGQTIAEELDCDVETDLDTLYSREDVEAVIVATPNYLHKEPVIKAAEHGVNVFCEKPIALSYQDCDEMVRTCQEHGVIFMAGHVMNFFHGVRYAKKLINDGVIGKVLYCHSARNGWEEQQPTISWKKIREKSGGHLYHHIHELDCVQFLMGGMPEEVTMTGGNVAHQGEAFGDEDDMLFVNMQFSDNRYAVLEWGSAFHWPEHYVLIQGTKGAIKIDMCDCGGTLKVDGREEHFLVHESQEEDDDRTRIYHGTEMDGAIMYGKPGKKPPMWLHSIMKNEMKYLNGILHGKEVDDEFRPLLTGEAARAAIATADACTKSRFEDRKVKLSEIIGEGSTI | 4.2.1.- | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:32669363}; Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:32669363}; | null | null | biliverdin reductase (NAD(P)+) activity [GO:0004074]; lyase activity [GO:0016829]; nucleotide binding [GO:0000166] | PF01408;PF02894; | 3.40.50.720; | Gfo/Idh/MocA family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-2,7-anhydro-alpha-neuraminate = N-acetyl-alpha-neuraminate; Xref=Rhea:RHEA:78519, ChEBI:CHEBI:15377, ChEBI:CHEBI:58770, ChEBI:CHEBI:229228; Evidence={ECO:0000269|PubMed:32669363}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.074 mM for 2,7-AN {ECO:0000269|PubMed:31636419}; Note=kcat is 0.0824 sec(-1). {ECO:0000269|PubMed:31636419}; | null | null | null | FUNCTION: Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota (PubMed:31636419, PubMed:32669363). Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7-anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH (PubMed:31636419, PubMed:32669363). Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+) (PubMed:32669363). {ECO:0000269|PubMed:31636419, ECO:0000269|PubMed:32669363}. | Mediterraneibacter gnavus (strain ATCC 29149 / DSM 114966 / JCM 6515 / VPI C7-9) (Ruminococcus gnavus) |
A7BFV8 | SPT_BACTC | MKHNLQDNLQGEQMANTNSNGGKKPFSDAKIIERANLLRDNDLYFFFRAIEETEASTVTVKGKKQIMIGSNNYLGLTHHPAVKEAAIKAVEKYGTGCTGSRFLNGNLNIHEELDEKLAAYLGHEKAIVFSTGMQANLGALSAICGPKDLMLFDSENHASIIDASRLSLGTTFKYKHNDMASLEELLESNMSRFNRVIIVADGVFSMTGDILRLPEVVKLAKKYGAYVYVDDAHGLGVMGPQGRGTMAHFDVTKDVDFNMGTFSKSFASIGGVISGSKDAIDYVRHSARSFMFSASMPPAAVATVSACIDVVQNDETILNNLWSNVEFMRNGFKELGFFTYGSQTPIIPLFIGDDMKALKMTKWLESKGVFCTPVLPPAVPKGETLIRTSYMASHNREDLSTVLEVFAEAKKIFDIPNHLH | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17557831}; | ceramide biosynthetic process [GO:0046513]; sphingosine biosynthetic process [GO:0046512] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17557831}. Cell inner membrane {ECO:0000269|PubMed:17557831}; Peripheral membrane protein {ECO:0000269|PubMed:17557831}. Note=Predominantly concentrated in a limited region near the inner membrane or organelle-like multilayered membrane structure. {ECO:0000269|PubMed:17557831}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000269|PubMed:17557831}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762; Evidence={ECO:0000269|PubMed:17557831}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 mM for L-serine {ECO:0000269|PubMed:17557831}; Note=kcat is 0.03 sec(-1) (in the presence of 100 uM of palmitoyl-CoA). {ECO:0000269|PubMed:17557831}; | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305|PubMed:17557831}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 to 8.0. {ECO:0000269|PubMed:17557831}; | null | FUNCTION: Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine. {ECO:0000269|PubMed:17557831}. | Bacteriovorax stolpii (Bdellovibrio stolpii) |
A7BHQ9 | TYRO_PHONA | MSRVVITGVSGTIANRLEINDFVKNDKFFSLYIQALQVMSSVPPQENVRSFFQIGGIHGLPYTPWDGITGDQPFDPNTQWGGYCTHGSVLFPTWHRPYVLLYEQILHKHVQDIAATYTTSDKAAWVQAAANLRQPYWDWAANAVPPDQVIVSKKVTITGSNGHKVEVDNPLYHYKFHPIDSSFPRPYSEWPTTLRQPNSSRPNATDNVAKLRNVLRASQENITSNTYSMLTRVHTWKAFSNHTVGDGGSTSNSLEAIHDGIHVDVGGGGHMGDPAVAAFDPIFFLHHCNVDRLLSLWAAINPGVWVSPGDSEDGTFILPPEAPVDVSTPLTPFSNTETTFWASGGITDTTKLGYTYPEFNGLDLGNAQAVKAAIGNIVNRLYGASVFSGFAAATSAIGAGSVASLAADVPLEKAPAPAPEAAAQPPVPAPAHVEPAVRAVSVHAAAAQPHAEPPVHVSAGGHPSPHGFYDWTARIEFKKYEFGSSFSVLLFLGPVPEDPEQWLVSPNFVGAHHAFVNSAAGHCANCRSQGNVVVEGFVHLTKYISEHAGLRSLNPEVVEPYLTNELHWRVLKADGSVGQLESLEVSVYGTPMNLPVGAMFPVPGNRRHFHGITHGRVGGSRHAIV | 1.14.18.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:17617709}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:17617709}; | melanin biosynthetic process [GO:0042438] | null | copper ion binding [GO:0005507]; tyrosinase activity [GO:0004503] | PF18132;PF00264; | 2.60.310.20;1.10.1280.10; | Tyrosinase family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17617709}. | null | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:17617709}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:17617709}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1930 uM for L-dopa {ECO:0000269|PubMed:17617709}; KM=119 uM for t-butylphenol {ECO:0000269|PubMed:17617709}; KM=30.6 uM for p-cresol {ECO:0000269|PubMed:17617709}; KM=163 uM for t-butylcatechol {ECO:0000269|PubMed:17617709}; KM=1240 uM for 3-(3,4-dihydroxyphenyl) propionic acid {ECO:0000269|PubMed:17617709}; KM=122 uM for dopamine {ECO:0000269|PubMed:17617709}; | null | null | null | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. {ECO:0000250|UniProtKB:Q92396}. | Pholiota nameko |
A7DTF0 | MRG1_CAEEL | MSSKKNFEVGENVACIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGEEKDRIFKGTASEYAEKHNAELPTTALKPKKKSLAAEAPRDDRDDTPGTSKGKKAKSVTIAPVMTADDMKVELPKPLRKILIDDYDLVCRYFINIVPHEYSVDQIIEDYIKTIPVSNEQMRTVDDLLIEYEEADIKITNLALICTARGLVDYFNVTLGSSYQLLYKFERPQYNDLVKKRAMEKGIDITNPTALQDSGFRPSQEYGIVHFLRMLAKLPDYLKLTQWNDHVINRIMIGVHDLIVFLNKNHGKYYRGSSDYQGASNDYYRRSLAADDGVGANQ | null | null | chromosome attachment to the nuclear envelope [GO:0097240]; chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA repair [GO:0006281]; embryo development ending in birth or egg hatching [GO:0009792]; germ cell development [GO:0007281]; heterochromatin formation [GO:0031507]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to euchromatin [GO:1905632] | autosome [GO:0030849]; chromatin [GO:0000785]; euchromatin [GO:0000791]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634] | null | PF05712;PF11717; | 2.30.30.140;1.10.274.30; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:22172672}. Chromosome {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}. Note=Concentrated on euchromatic regions marked by H3K36me2/me3 and probably enriched on autosomes. {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}. | null | null | null | null | null | FUNCTION: Protein involved in the remodeling of chromatin thereby regulating various processes including transcription, chromosome synapsis and genome integrity (PubMed:17215300, PubMed:22172672, PubMed:22212480, PubMed:30929290). Mainly binds genomic loci carrying trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4' (H3K4me3), and acetylated histone H3 'Lys-9' (H3K9ac), 'Lys-27' (H3K27ac) (PubMed:30425042, PubMed:31118512). During meiosis, required for the presynaptic pairing of homologous chromosomal regions outside of the pairing center and for the progression of chromosome synapsis (PubMed:22172672, PubMed:22212480). Essential maternal factor required in postembryonic germline development and in maintaining germ cell identity (PubMed:12175490, PubMed:30425042). Plays an important role in maintaining genomic integrity in primordial germ cells (PGCs) during meiosis by regulating DNA double-strand break (DSB) repair and synapsis (PubMed:22212480, PubMed:30929290). Also, required for chromatin-based transcriptional silencing in PGCs and for silencing of X-linked genes in the maternal germ line (PubMed:17215300, PubMed:30929290). By retaining histone acetyltransferase, cbp-1, in euchromatin, promotes the anchoring of heterochromatin at the inner nuclear membrane in intestinal and hypodermal cells (PubMed:31118512). {ECO:0000269|PubMed:12175490, ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:22172672, ECO:0000269|PubMed:22212480, ECO:0000269|PubMed:30425042, ECO:0000269|PubMed:30929290, ECO:0000269|PubMed:31118512}. | Caenorhabditis elegans |
A7DY56 | TRN1_COCOF | MANLRESSRDKSRWSLEGMTALVTGGSKGIGEAVVEELAMLGARVHTCARDETQLQESLREWQAKGFQVTTSVCDVSSRDQREKLMETVSSLFQGKLNILVNNAGTCITKPTIDYTSEDFSFLMSTNLESSFHLSQLAHPLLKSSGLGSIVLISSVASVVHVNVGSIYGATKGAMNQLARNLACEWASDSIKVNSVCPGFISTPLASNYFRNEEFKKEVENIIPTGRVGEANEVSSLVAYLCLPAASYVTGQTICVDGGFSVNGFTFKSLPLR | 1.1.1.206; 1.1.1.236 | null | null | null | tropine dehydrogenase activity [GO:0050356]; tropinone reductase activity [GO:0050358] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family, SDR65C subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + tropine = H(+) + NADPH + tropinone; Xref=Rhea:RHEA:18357, ChEBI:CHEBI:15378, ChEBI:CHEBI:57554, ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349; EC=1.1.1.206; Evidence={ECO:0000269|PubMed:18221363}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pseudotropine = H(+) + NADPH + tropinone; Xref=Rhea:RHEA:24244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57493, ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349; EC=1.1.1.236; Evidence={ECO:0000269|PubMed:18221363}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3290 uM for tropinone {ECO:0000269|PubMed:18221363}; KM=2002 uM for nortropinone {ECO:0000269|PubMed:18221363}; KM=42 uM for 8-thiabicyclo[3.2.1]octan-3-one {ECO:0000269|PubMed:18221363}; KM=2636 uM for quinuclidinone {ECO:0000269|PubMed:18221363}; KM=1342 uM for N-propylpiperidin-4-one {ECO:0000269|PubMed:18221363}; KM=7583 uM for N-methylpiperidin-4-one {ECO:0000269|PubMed:18221363}; KM=13 uM for 3-methylcyclohexanone {ECO:0000269|PubMed:18221363}; KM=15 uM for 4-methylcyclohexanone {ECO:0000269|PubMed:18221363}; Vmax=0.79 nmol/sec/mg enzyme with tropinone as substrate {ECO:0000269|PubMed:18221363}; Vmax=0.59 nmol/sec/mg enzyme with nortropinone as substrate {ECO:0000269|PubMed:18221363}; Vmax=1.5 nmol/sec/mg enzyme with 8-thiabicyclo[3.2.1]octan-3-one as substrate {ECO:0000269|PubMed:18221363}; Vmax=2.73 nmol/sec/mg enzyme with quinuclidinone as substrate {ECO:0000269|PubMed:18221363}; Vmax=22.24 nmol/sec/mg enzyme with N-propylpiperidin-4-one as substrate {ECO:0000269|PubMed:18221363}; Vmax=29.53 nmol/sec/mg enzyme with N-methylpiperidin-4-one as substrate {ECO:0000269|PubMed:18221363}; Vmax=21.67 nmol/sec/mg enzyme with 3-methylcyclohexanone as substrate {ECO:0000269|PubMed:18221363}; Vmax=47.23 nmol/sec/mg enzyme with 4-methylcyclohexanone as substrate {ECO:0000269|PubMed:18221363}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. The pH has no influence on the tropine to pseudotropine product ratio. {ECO:0000269|PubMed:18221363}; | null | FUNCTION: Oxidoreductase having both tropinone reductase I and II activities. Involved in the tropane alkaloids calystegines and cochlearine biosynthesis. Can use tropinone and nortropinone as substrates and produces both tropine and pseudotropine. Able to oxidize pseudotropine in the reverse reaction. {ECO:0000269|PubMed:18221363}. | Cochlearia officinalis (Common scurvygrass) |
A7E2V4 | ZSWM8_HUMAN | MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTDQCLTYEQITGWWYSVRTSASHSSASGHTGRSNGQSEVAAHACASMCDEMVTLWRLAVLDPALSPQRRRELCTQLRQWQLKVIENVKRGQHKKTLERLFPGFRPAVEACYFNWEEAYPLPGVTYSGTDRKLALCWARALPSRPGASRSGGLEESRDRPRPLPTEPAVRPKEPGTKRKGLGEGVPSSQRGPRRLSAEGGDKALHKMGPGGGKAKALGGAGSGSKGSAGGGSKRRLSSEDSSLEPDLAEMSLDDSSLALGAEASTFGGFPESPPPCPLHGGSRGPSTFLPEPPDTYEEDGGVYFSEGPEPPTASVGPPGLLPGDVCTQDDLPSTDESGNGLPKTKEAAPAVGEEDDDYQAYYLNAQDGAGGEEEKAEGGAGEEHDLFAGLKPLEQESRMEVLFACAEALHAHGYSSEASRLTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLSKAAFLLTVLSERPEHHNLAFRVGMFALELQRPPASTKALEVKLAYQESEVAALLKKIPLGPSEMSTMRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPGSRPPSRNWNSETPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQAKLKKILDKLLDRESQTHKPQTLSSFYSSSRPTTASQRSPSKHGGPSAPGALQPLTSGSAGPAQPGSVAGAGPGPTEGFTEKNVPESSPHSPCEGLPSEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVEVGRYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEQTAGGSSTAREGATSCSASGIRAGGEAGRGMPEGRGGPGTEPVTVAAAAVTAAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVPSSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVACELWGQGTVSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEMATFSP | null | null | positive regulation of miRNA catabolic process [GO:2000627]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; target-directed miRNA degradation [GO:0140958] | Cul2-RING ubiquitin ligase complex [GO:0031462]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytosol [GO:0005829] | ubiquitin ligase-substrate adaptor activity [GO:1990756]; zinc ion binding [GO:0008270] | PF21055; | null | ZSWIM8 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3UHH1}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:33184234, ECO:0000269|PubMed:33184237}. | null | null | FUNCTION: Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237). Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target (PubMed:33184234). May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation (PubMed:24012004). {ECO:0000269|PubMed:24012004, ECO:0000269|PubMed:33184234, ECO:0000269|PubMed:33184237}. | Homo sapiens (Human) |
A7E2Y1 | MYH7B_HUMAN | MSGNKRGSRASCPHRGAECLLPWAALNLQGFQLLLLHPSATAMMDVSELGESARYLRQGYQEMTKVHTIPWDGKKRVWVPDEQDAYVEAEVKSEATGGRVTVETKDQKVLMVREAELQPMNPPRFDLLEDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSRGRLMRLEYQRLLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKHKE | null | null | null | cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15755502}; Peripheral membrane protein {ECO:0000269|PubMed:15755502}. | null | null | null | null | null | FUNCTION: Involved in muscle contraction. {ECO:0000269|PubMed:11919279}. | Homo sapiens (Human) |
A7E320 | UHRF1_BOVIN | MWIQVRTMDGKVAHTVDSLSRLTKVEELRKKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYDVRLNDTIQLLVRQSLVLPVPVPSSSGGSKERDSELSDTDSGCGLAQSESDKSSNSGEAANEPEGKADEDECDETELGLYKVGEYVDARDTNMGAWFEAKVIRVTRKAPAHDQPSSSSSKPEDDIIYHVTYDDYPENGVVQMTSQNVRARARHTIKWEDLQVGQVVMVNYNPDLPKDRGFWYDAEILRKRETRTARELHANVRIGGDSLNDCRIVFVDEVFKIERPGEGNPMVENPMRRKSGPSCKHCKDDERKLCRMCACHVCGGKQDPDKQLMCDECDMAFHIYCLRPPLSSVPPEEEWYCPDCRIDSSEVVQAGEKLKESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHFGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNHGAYSLVLAGGYEDDVDHGNSFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDLKGAEAKDWRSGKPVRVVRNVKGRKHSKYAPIEGNRYDGIYKVVRYWPEKGKSGFLVWRFLLRRDDVEPGPWTKEGKDRIKKLGLTMQYPEGYLEALARKEKENSKQAALDKEEEDGEEGFTSPRKGKRKSKSAGGDGSSRGTPKKTKVEPYSLTTQQSSLIKEDKSNMKLWTEILKSLKDGPKFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFKAQVFSCPACRYDLGRSYAMTVNQPLQAVLSQLFPGYGSGR | 2.3.2.27 | null | cell cycle [GO:0007049]; DNA repair [GO:0006281]; heterochromatin formation [GO:0031507]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | chromatin [GO:0000785]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; replication fork [GO:0005657] | hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00628;PF02182;PF12148;PF00240; | 2.30.30.1150;2.30.30.140;2.30.280.10;3.30.40.10; | null | PTM: Phosphorylation at Ser-302 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-645 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-645 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VDF2, ECO:0000255|PROSITE-ProRule:PRU00358}. Note=Associated, through the YDG domain (also called SRA domain), with replicating DNA from early to late S phase, including at replicating pericentric heterochromatin (By similarity). Also localizes to euchromatic regions. In non-S-phase cells, homogenously distributed through the nucleus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8VDF2}. | 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:Q96T88}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF2 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation. Plays a pivotal role in the establishment of correct spindle architecture by catalyzing the 'Lys-63'-linked ubiquitination of KIF11, thereby controlling KIF11 localization on the spindle. {ECO:0000250|UniProtKB:Q96T88}. | Bos taurus (Bovine) |
A7E3N2 | NCF2_RAT | MSLAEAIRLWNEGVQAADKKDWKGALEAFSEVQDPHSRICFNIGCMYTILDNLQEAEQAFTKSINRDKHLAVAYFQRGMLYYSMEKYRPASVGRKAALLFLGSYNLVARIIVGYPLSPGKVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKRCPTSHLPLDPPQVTMALWFEEGGVGKRSVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSLESDIPPPPNSSPPERLQLSPGWCQQLGPLRCPPFLLHQEVKRSVPMPYMLKVHYKYTVVMETQLGLPYSQLRNMVSKKLELLPEHTKLSYQRRDSPELLLLSEESMKDAWAQVKNYCLTLWCEHTVGDQGFVDEPKEKENSDADNRTTEPQPKEGTQVVAIFSYDATQPEDLEFVEGDVILVLSHVNEEWLEGECKGKIGIFPKAFVEGCAAKNLEGTPREV | null | null | cellular response to hormone stimulus [GO:0032870]; phagocytosis [GO:0006909]; positive regulation of blood pressure [GO:0045777]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; respiratory burst [GO:0045730]; response to activity [GO:0014823]; response to glucose [GO:0009749]; response to hyperoxia [GO:0055093]; response to laminar fluid shear stress [GO:0034616]; response to lipid [GO:0033993]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to progesterone [GO:0032570]; response to xenobiotic stimulus [GO:0009410]; superoxide anion generation [GO:0042554] | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; NADPH oxidase complex [GO:0043020] | small GTPase binding [GO:0031267]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00564;PF00018;PF13181; | 2.30.30.40;1.25.40.10; | NCF2/NOXA1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}. | 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:P19878}. | Rattus norvegicus (Rat) |
A7E3S4 | RAF1_BOVIN | MEHIQGAWKTISNGFGFKDTVFDGTSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTVGDGGVPALPSLTMRRMRESVSRIPPGSQHRYSTPHAFTFSASSPSSEGSLSQRQRSTSTPNVHMVSATLPVDSRMIEDAIRSHSESGSPSALSSSPNNLSPTGWSQPKTPAPAQRERAPGSSTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P04049}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P04049}; | death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; insulin receptor signaling pathway [GO:0008286]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intermediate filament cytoskeleton organization [GO:0045104]; myelination [GO:0042552]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of protein-containing complex assembly [GO:0031333]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphorylation [GO:0016310]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; Ras protein signal transduction [GO:0007265]; response to muscle stretch [GO:0035994]; Schwann cell development [GO:0014044]; somatic stem cell population maintenance [GO:0035019]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; type B pancreatic cell proliferation [GO:0044342] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; small GTPase binding [GO:0031267] | PF00130;PF00069;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphorylation of Ser-259 by the complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading to stimulate RAF1 activity. Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization (By similarity). Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation. Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells. Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338. Dephosphorylation at Ser-338 by PPP5C results in a decreased of activity (By similarity). {ECO:0000250}.; PTM: Methylated at Arg-563 in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its mitochondrial localization. Retinoic acid-induced Ser-621 phosphorylated form of RAF1 is predominantly localized at the nucleus (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P04049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P04049}; 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:P04049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:P04049}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation (By similarity). {ECO:0000250|UniProtKB:P04049}. | Bos taurus (Bovine) |
A7EK16 | MYO1_SCLS1 | MGISRRPKADKNASAADSAPGGKPNIQKAQFDTTKKKEVGVSDLTLISKVSNEAINENLKKRFDNREIYTYIGHVLVSVNPFRDLGIYTDAVLESYKGKNRLEMPPHVFAVAESAYYNMNAYKDNQCVIISGESGAGKTEAAKRIMQYIANVSGGSNSSIQETKEMVLATNPLLESFGNAKTLRNNNSSRFGKYLQLQFNAQGEPVGADITNYLLEKTRVVTQIKDERNFHIFYQFTKGASQAYRESYGIQQPSQYLYTSKAGCFDVDGIDDLAEYQDTLQAMKVIGLSQAEQDEIFRMLAAILWTGNIQFREGDDGYATVVDQSVVDFLAYLLDVDAAHVIQAITIRILTPRNGEVIESPANVPQAMATRDALAKAIYNNLFDWIVERVNKSLTARAETSNSIGILDIYGFEIFEQNSFEQLCINYVNEKLQQIFIQLTLKTEQEEYAREQIKWTPIKYFDNKIVCDLIEAIRPPGVFSAMKDATKTAHADPAACDRTFMQAISGMSNPHLTPRQGNFIIKHYAGDVSYTVEGITDKNKDQLLKGLLNLFGQSRNHFIHELFPHQVDQDNRKQPPSAGDKIKASANDLVTTLMKATPSYIRTIKPNENKSPTEYNEKNVLHQVKYLGLQENVRIRRAGFAYRQTFDKFVERFYLLSPKTSYAGDYIWTGDSKTGAMQILKDTNIPVEEYQMGVTKAFIKAPETLFALEHMRDRYWHNMAARIQRVWRAFLQIRIEAATRIQRMFRKKREGKEFLELREKGHQILQGRKERRRYSLLGSRRFMGDYLGIAATTGPGSKIRGSINLPASEVTLFSCRGEILETKFGRSSKLSPRIFIMTRTKFYIVSQLLVNKQVQIAVEKAIPLGAIKFVSISTCRDDWFSLGVGSPQEADPLLTCVFKTELFTHMQAAMPGGGFNLKIGDSIEYAKKPNKMQLIKVVKDSQQAQDHYKSATIHTQAGEPPNSRSKPLPKGKPVAAKPFTSGRLIKPGGPGGRPSRLTNGNRPTPKPVPTPAPAAARPVPAVNPVAASIPVHTRNTSVQSTQSTRAVPPPPPPAPPAPPPAPVSKEPQYRVLYEFAGQSANEFSLKQGEIVTVLQKETNGWWLTKNVRGQGWAPTAYLEEVTPPPPPPVATRPAPPPAPGPPKMNGTNGAAIRSKPTPPAPPAKRPAAGRKPAPPPAPRDSGMSISSNGSGNNSGRSTPTPSLAGGLAEALRARQSAMQGNAKREDEDDW | null | null | actin cortical patch assembly [GO:0000147]; actin cortical patch localization [GO:0051666]; actin filament organization [GO:0007015]; endocytosis [GO:0006897]; mitotic cytokinesis [GO:0000281]; vesicle transport along actin filament [GO:0030050] | actin cortical patch [GO:0030479]; actin cytoskeleton [GO:0015629]; cell cortex of cell tip [GO:0051285]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; myosin I complex [GO:0045160]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; prospore membrane [GO:0005628]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; microfilament motor activity [GO:0000146] | PF00063;PF06017;PF00018; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex (By similarity). {ECO:0000250}. | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
A7F0W2 | ATG1_SCLS1 | MASKTPSSSSSRRPRNVGVGSFTINEEIGKGSFATVYRGTHVPSGSLVAIKSVNLGRLNKKLKDNLYVEIEILKSLHHPHIVALMDCRESTSHIHLMMEYCELGDLSYFIKKRDKLADNPSLFDMIRKYPMPVDGGLNQVVVRHFFKQLSSAMEFLRDRDFVHRDVKPQNLLLIPSPDWMAKSKNGPEAMKASKESIVPMVGINSLPMLKLADFGFARSLPSTSLAETLCGSPLYMAPEILRYEKYDARADLWSIGTVLYEMMTGKPPFRAANHVELLRKIEQNEDEIRFPSKTVFSRDLKDIARRFLKKRPEDRITFPEYFAHPVVTGPIPGLVGEDLPKEIITPSRSPEASVARHPSLRERQRENPTPKPVETTYESLIARDIGEQAPRSPHIEANQPVEIPGHKSGRPGSRDRPSAISAATAPNVDTLPRQRDRTERHYAPIGRPVSRKPSYDEQANLPVQEEIRSSDSITEAEQDVRDAREYVLVEKKAVEVNAFADEMAASPRLAHANHIPKQPTRRHTSMGAPNSTSGAVAVPPSRAVQKAQGNTRPDTSSARNSYGSYGKTGSSPSTASAIAKALQGASVRVFGVSWSPTLIGKGPSPQQLYNPYPAYPTPNTGFIGDARPIDEDQRVVNVIEDSATRSDVVYGFAEVKYRQLIPLAPSMNHGLGGPNNEKVGDAMDEDDGLTVEAIVNLSEEALVLYVKSLSLLSKSMDIAGAWWLRKNRGGVISGGHTPGSDSSSAVQAGNRINGAVQWVRTRFNEVLEKAELVRLKLVEAQKRLPEDHPGHPSNHATASKIVGGSSTTDGVVLSSGITAEKLMYDRALEMSRTAAINELANEDLPGCEISYTTAIRMLEAVLENDEELIPRKRSPSLREDKEKCDGGEVNGINFGDRKDVLKVLQMIRTRLHVLKKKMAVIARHQSMPPPSSPRHSHSGGTTPTIANTPPH | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; regulation of autophagy [GO:0010506]; response to starvation [GO:0042594]; reticulophagy [GO:0061709] | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; 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:P53104}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. {ECO:0000250|UniProtKB:P53104}. | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
A7F7H0 | ARO1_SCLS1 | MGSTTFENPTRIEILGKEDIIVDFDIWRNFVAEDLLSDLPSSTYVLITDTNLSPLYVPAFQQSFEALAAKSSSTPRLLTYEIPPGENSKSRETKAEIEDWMLSHQCTRDSVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAFWQPQRIYIDLRFLETLPVREFINGMAEVVKTAAIWDEAEFSALEDNANLIMTTIRAKNTDCSTRLGPIRDILKRIVLGSAKTKADVVSADEREGGLRNILNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARHLGVLKPGAVARLVKCIASYGLPTSLADKRIQKLTAGKLCPVDVLLEKMGVDKKNDGRKKKIVLLSAIGKTYEPKASVVEDRSIRVVLSDSVEVRPSVPETLNVEVTPPGSKSISNRALVLAALGTGPCRIKNLLHSDDVEFMLTSIGKLGGATYAWEDAGEVLCVQGKGGDLHASPTELYIGNAGTASRFLTTVVSLCKPSASTKSTILTGNARMKVRPIGPLVDSLRANGVDIEYLEKEHSLPLNVAASGGFTGGDINLAATVSSQYVSSLLMCAPYAKNPVTLRLVGGKPISQLYIDMTTAMMAAFGIHVVRSQTEEHTYHIPQGVYKNPEEYVVESDASSATYPLAVAAISGTTCTIPNIGCKSIQGDARFAIDVLKPMGCKVVQTDYSTTVTGPPIGSLQAIEEVDMEPMTDAFLTASVLGAVAKGTTKIRGIANQRVKECNRIKAMKDELAKFGVTCRELEDGIEVDGVPIKDLKHPAEGIHCYDDHRVAMSFSVLSVAASQPVLIEERECVGKTWPGWWDILSKSFQVELAGKEVKATHSKKIGIPALPDKSIFIIGMRGAGKTTAGAWAAKILGRPYKDLDVELERISGMSIPDMVRSKGWDFFRAAELDLLKHCLTDQPEKHVFACGGGVVEMPEARELLINFHKSGGIVLLVHRDTEQVMDYLRIDKTRPAYVEDMMGVYSRRKPWFNECSNFQYHSKGSGASALSVAEQDFARFLHHISGKSLHFDEMRNKPQSFFVSLTMPDISGAAYILPSVAVGSDAVEVRVDLLEDPSSTNGIPGTDFLSVQIAHLRSVVHLPVIFTVRTVSQGGRFPDAAHEEALKLYKLAVKMGIEYIDLEIAFPDELLQEVTEAKGFSRIIASHHDPQGTLSWKNGGWFQHYNRALQYGDIIKLVGSAKSIEDNFALAKFKKTMAAAHDTPLIAINMGVTGKLSRVLNGFMTPVSHPSLPFKAAPGQLSAAEIRSTLSTLGEIEPKSFYLFGTPISQSRSPALHNTLFKQTGLPHRYSRLETDRVADVQDVIRAPDFGGASVTIPLKLDIIPLLDSVTDAVKVIGAVNTIIPTPDNPPRLVGENTDWLGMTHSLMSASHTPSPVDSPSPALVIGAGGTARAAIYALHSLGHSPIYMVARTPSKLDTLINSFPSSFNIIPLPSTTSATELTTPPAVAISTIPADRPIESNMRETLAVLLRHEKKDEGKQRTLLEMAYKPSQTPLMRMAEDAGWVAIPGLEVLSAQGWYQFQKWTSIQPLYVDARAAVMGDSTA | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
Subsets and Splits