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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A7GBG3 | BXF_CLOBL | MPVVINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTDPSDFDPPASLENGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGEVLLQEISYAKPYLGNEHTPINEFHPVTRTTSVNIKSSTNVKSSIILNLLVLGAGPDIFENSSYPVRKLMDSGGVYDPSNDGFGSINIVTFSPEYEYTFNDISGGYNSSTESFIADPAISLAHELIHALHGLYGARGVTYKETIKVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSRVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTEIDLANKFKVKCRNTYFIKYGFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQNIKLNPKIIDSIPDKGLVEKIVKFCKSVIPRKGTKAPPRLCIRVNNRELFFVASESSYNENDINTPKEIDDTTNLNNNYRNNLDEVILDYNSETIPQISNQTLNTLVQDDSYVPRYDSNGTSEIEEHNVVDLNVFFYLHAQKVPEGETNISLTSSIDTALSEESQVYTFFSSEFINTINKPVHAALFISWINQVIRDFTTEATQKSTFDKIADISLVVPYVGLALNIGNEVQKENFKEAFELLGAGILLEFVPELLIPTILVFTIKSFIGSSENKNKIIKAINNSLMERETKWKEIYSWIVSNWLTRINTQFNKRKEQMYQALQNQVDAIKTVIEYKYNNYTSDERNRLESEYNINNIREELNKKVSLAMENIERFITESSIFYLMKLINEAKVSKLREYDEGVKEYLLDYISEHRSILGNSVQELNDLVTSTLNNSIPFELSSYTNDKILILYFNKLYKKIKDNSILDMRYENNKFIDISGYGSNISINGDVYIYSTNRNQFGIYSSKPSEVNIAQNNDIIYNGRYQNFSISFWVRIPKYFNKVNLNNEYTIIDCIRNNNSGWKISLNYNKIIWTLQDTAGNNQKLVFNYTQMISISDYINKWIFVTITNNRLGNSRIYINGNLIDEKSISNLGDIHVSDNILFKIVGCNDTRYVGIRYFKVFDTELGKTEIETLYSDEPDPSILKDFWGNYLLYNKRYYLLNLLRTDKSITQNSNFLNINQQRGVYQKPNIFSNTRLYTGVEVIIRKNGSTDISNTDNFVRKNDLAYINVVDRDVEYRLYADISIAKPEKIIKLIRTSNSNNSLGQIIVMDSIGNNCTMNFQNNNGGNIGLLGFHSNNLVASSWYYNNIRKNTSSNGCFWSFISKEHGWQEN | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19543288}; Note=Binds 1 zinc ion per subunit (PubMed:19543288). {ECO:0000269|PubMed:19543288}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | lipid binding [GO:0008289]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | SUBCELLULAR LOCATION: [Botulinum neurotoxin type F]: Secreted {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin F light chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:19476346, ECO:0000305|PubMed:19543288}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin F heavy chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host synapse, host presynaptic cell membrane {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane {ECO:0000305|PubMed:19476346}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000305|PubMed:19476346}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for over-expressed human VAMP1 {ECO:0000269|PubMed:22289120}; KM=24.5 uM for over-expressed human VAMP2 {ECO:0000269|PubMed:22289120}; KM=15 uM for over-expressed human VAMP3 {ECO:0000269|PubMed:22289120}; Note=kcat is 16.12, 34.37 and 28.57 sec(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively. {ECO:0000269|PubMed:22289120}; | null | null | null | FUNCTION: [Botulinum neurotoxin type F]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:14423425). Precursor of botulinum neurotoxin F which may have 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:19476346, PubMed:19650874). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). Requires complex gangliosides for full neurotoxicity (PubMed:19650874, PubMed:21483489). Electrical stimulation increases uptake of toxin, presumably by transiently exposing a receptor usually found in eukaryotic target synaptic vesicles (PubMed:19476346, PubMed:19650874). Blocks neurotransmitter release by cleaving synaptobrevin-2/VAMP2 (PubMed:19476346). It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function (PubMed:19476346, PubMed:19650874, PubMed:21483489). {ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:14423425, ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:21483489}.; FUNCTION: [Botulinum neurotoxin F light chain]: Has protease activity (PubMed:19476346, PubMed:19543288). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '58-Gln-|-Lys-59' bond of synaptobrevin-2/VAMP2 and probably also the equivalent 'Gln-|-Lys' sites in VAMP1 and VAMP3 (PubMed:19476346, PubMed:19543288). Substrate specificity is conferred by multiple interactions of LC with substrate (PubMed:19543288). {ECO:0000250|UniProtKB:P30996, ECO:0000269|PubMed:19543288, ECO:0000305|PubMed:19476346}.; FUNCTION: [Botulinum neurotoxin F heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface (PubMed:19476346, PubMed:19650874). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity). Isolated HC binds to host synaptosomes and neurons, significantly decreases uptake and toxicity of whole BoNT/F (PubMed:19476346, PubMed:19650874). Interferes with uptake of BoNT/E and to a lesser extent BoNT/C (PubMed:19650874). in vitro binds gangliosides GT1b, GD1b and GD1a (PubMed:19476346, PubMed:19650874, PubMed:21849494). Binds to synaptic vesicle glycoproteins SV2A, SV2B and SV2C which may serve as coreceptors with gangliosides (PubMed:19476346, PubMed:19650874). Interaction with SV2 proteins requires SV2 glycosylation (PubMed:19476346). However knockout SV2A/SV2B mice still cleave synaptobrevin, leaving the identification of its receptor unclear (PubMed:21483489). {ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:21483489}. | Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) |
A7HD43 | GCHK_ANADF | MTGVPETVFEELKRYVGWGDGDERALRSLHGAAAPHFPRLAEEFYDRILGHEGARTALVGGESQVGHLKVTMIAWLDELLGGPWDEAYWDRRYRIGRVHVRIGLPQHYMFGAMNVHRTGLARLAYERFHGDPPELERVRNALGKVLDLELAVMLHTYREDLLAQQARVERLSTFGQLVGSIGHDLRNPLGVIETSLYILRTRTGEDERARKHLDRIGEQLGVANGIITNLLDMIRDRPLAREPVELAAVVGGAAESVRRPTGVSLALEGLDALPPVEGDPGQLRQVFVNLLENAVFAASPEGVVAVRASRADGLVALDVEDSGPGVDPATRRRLFEPLITTKDKGIGLGLALVKRIAERHGGTVEYSDRPGGGARFTVRLPA | 2.7.13.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:21852234}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:21852234}; | peptidyl-histidine phosphorylation [GO:0018106]; phosphorelay signal transduction system [GO:0000160] | null | ATP binding [GO:0005524]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803] | PF02518;PF00512;PF11563; | 1.10.287.130;1.10.490.10;3.30.565.10; | null | PTM: Autophosphorylated. {ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}. | null | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.9 uM for ATP (with the Fe(III)-OH(-) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=35.4 uM for ATP (with the Fe(III)-CN(-) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=23.8 uM for ATP (with the Fe(III)-imidazole bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=23 uM for ATP (with the Fe(II)-O(2) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=357 uM for ATP (with the Fe(II)-CO bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=78 uM for ATP (with the Fe(II) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=33.6 uM for ATP (with the heme-free form of the enzyme) {ECO:0000269|PubMed:26212354}; Note=kcat is 1.1 min(-1) for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. kcat is 1.2 min(-1) with the Fe(III)-CN(-) bound form of the enzyme. kcat is 1.1 min(-1) with the Fe(III)-imidazole bound form of the enzyme. kcat is 1.0 min(-1) with the Fe(II)-O(2) bound form of the enzyme. kcat is 1.0 min(-1) with the Fe(II)-CO bound form of the enzyme. kcat is 0.4 min(-1) with the Fe(II) bound form of the enzyme. kcat is 0.3 min(-1) with the heme-free form of the enzyme. The presence of the cognate response regulator (RR) protein significantly reduces the enzyme affinity for ATP. {ECO:0000269|PubMed:26212354}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 11.0 for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. At pH 8.0, displays 75% of the optimal rate. Is inactive below pH 5.5 and above pH 12.7. {ECO:0000269|PubMed:26212354}; | null | FUNCTION: Member of the two-component regulatory system GcHK/Anae109_2439. Autophosphorylates in response to oxygen availability, and then transfers the phosphate group to a conserved Asp residue in the receiver domains of the cognate response regulator Anae109_2439, resulting in its activation. {ECO:0000269|PubMed:21852234}. | Anaeromyxobacter sp. (strain Fw109-5) |
A7IQH5 | HCDS3_XANP2 | MSNRLKNEVIAITGGGAGIGLAIASAALREGAKVALIDLDQGLAERSAAMLSTGGAVAKGFGADVTKAADITAAITSAEQTIGSLTGLVNNAGIAGFGSVHDADAAAWDRIMAVNVTGTFLASKAALAGMLERHKGTIVNFGSVAGLVGIPTMAAYCAAKGAIVNLTRQMAADYSGRGVRVNAVCPGTVTSTGMGQQLLGSDTSPEVQARRLAKYPIGRFGTPEDIAEAVIFLLSDQAAFVTGAAFAVDGGMTAI | 1.1.1.269 | null | null | null | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH; Xref=Rhea:RHEA:21052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57552, ChEBI:CHEBI:57945, ChEBI:CHEBI:58430; EC=1.1.1.269; Evidence={ECO:0000269|PubMed:20302306}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21053; Evidence={ECO:0000269|PubMed:20302306}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for S-HPC {ECO:0000269|PubMed:20302306}; KM=270 uM for 2-KPC {ECO:0000269|PubMed:20302306}; KM=9100 uM for R-HPC {ECO:0000269|PubMed:20302306}; KM=120 mM for 2-butanone {ECO:0000269|PubMed:20302306}; KM=1400 mM for 2-propanol {ECO:0000269|PubMed:20302306}; KM=68 mM for (R)-2-butanol {ECO:0000269|PubMed:20302306}; KM=28 mM for (S)-2-butanol {ECO:0000269|PubMed:20302306}; KM=191 uM for NAD(+) {ECO:0000269|PubMed:20302306}; KM=8.42 uM for NADH {ECO:0000269|PubMed:20302306}; Note=kcat is 5.5 sec(-1) with R-HPC as substrate. kcat is 25 sec(-1) with S-HPC as substrate. kcat is 11 sec(-1) with 2-KPC as substrate. kcat is 0.044 sec(-1) with 2-butanone as substrate. kcat is 2.0 sec(-1) with 2-propanol as substrate. kcat is 1.0 sec(-1) with (R)-2-butanol as substrate. kcat is 2.6 sec(-1) with (S)-2-butanol as substrate. {ECO:0000269|PubMed:20302306}; | null | null | null | FUNCTION: Involved in aliphatic epoxide carboxylation (PubMed:20302306). Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:20302306). The enzyme is highly specific for the S enantiomers (PubMed:20302306). In vitro can also use the aliphatic ketone 2-butanone and the aliphatic alcohol 2-propanol, and shows an inherent stereoselectivity for 2-butanone reduction (PubMed:20302306). {ECO:0000269|PubMed:20302306}. | Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) |
A7IZE9 | ALL21_BLOTA | MKFIIALAALIAVACALPVSNDNFRHEFDHMIVNTATQRFHEIEKFLLHITHEVDDLEKTGNKDEKARLLRELTVSEAFIEGSRGYFQRELKRTDLDLLEKFNFEAALATGDLLLKDLKALQKRVQDSE | null | null | null | null | IgE binding [GO:0019863]; protein homodimerization activity [GO:0042803] | PF11642; | 1.20.58.970; | Mite group 5 allergen family | null | null | null | null | null | null | null | null | Blomia tropicalis (Mite) |
A7KAL2 | ATG1_PENRW | MASQHSRRSREAPRPEMSIGRYTRLDEIGRGSFATVYQGVHTKSKTYVAIKSVNLSKLNKKLKENLSSEIDILKGLHHPHIVALIDCHESTSHIHLVMEYCALGDLSLFIKRRDTLGSHKYTRDMIAKYPNPPGGSLNEVVTRHFLKQLSSALKFLRDRNLIHRDIKPQNLLLCPSPSSYRSGHAQVMPYKGSDDSYEPTTGLESLPMLKIADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGRPPFRATNHVELLRKIEKGEDRIRFPEDNPASDDIKKLIRGLLKRNPVERLNFPEFFSNNVINDPIPGLLADDAPGPPQSPRPRQLVGKAEESPYDTGPEDKLAYPPGQRPVTTHPKSGTPPTATDMRRMGSADRPAPAISKEQQPGGTPPQRPGPVSLATAPGRQELIDRNATTAAMDRQRHRNTYAGAPKASDSTIRAQEARDRAAQEVAFERDYVVVEKRAVEVNAFADELAHSPRLQGGLSRPGQTGAGSRRTTTQGLPTVSPSSPHANAAKAMQVVSGRARADSTHQRQHSYERRYGQSPTSATSAISKALNMASGRLFGMGFSPPLAITKGGRSPPLAYNPFPAYPPVHASLLITGDGSKPNATGDEDCKAVQEIEECATRSDVVFGFAEVKYKQLIPLAPSASTDPSARPMDTNVEPDSADSDDGLTVDAIVTLSEEALVLYVKALSLLAKSMDIAGAWWSRKNREEVYGESPTKDSMSAVAGTRINYVVQWVRSRFNEVIEKAEFVRLKLIEGQRRLPPDHPSHPDNHSISSTAGSSSTADVVVSPGVTAERLMYDRALEMSRAAAINELTGEDLANCEITYVTAIRMLEAVLEDDGMRSMPGSNIERQSSSQGGEKVVLDELQVEDRQVVVKLVSSMRGRLASVRKKVAVLAKRSSAPTPTAGSAGKTPTSNISPVTYATGVTPPR | 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] | 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 | 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 (PubMed:17204848). 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 (By similarity). {ECO:0000250|UniProtKB:P53104, ECO:0000269|PubMed:17204848}. | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
A7KAU2 | S47A1_RABIT | MEAPVELGPGGRQASPERRHWLRCLVLSDFREELRALLVLACPAFLAQLMVFLISFVSSVFCGHLSKLELNAVTLAIAVINVMGVSVGFGLSSACDTLISQTYGSRNLKHVGVILQRGSLILLLCCLPCWALFLNTQHILLLFRQDPAVSRLTQTYVTIFIPALPATFLYTLQVKYLLNQGIVLPQVVTGVAANLVNALANYLFVYQLHLGVMGSALANTVAQFTLALLLFLYILRSKVYQATWGGWSLECLQDWASFFRLAIPSMLMLCMEWWAYEIGSFLSGILGMVELGAQSVTYELAVIVYMIPMGLSVAVNVRVGNALGAGNIEQAKKSSAVALLVTELIAVVFCVMLLSCKDLVGYIFTSDRDIIALVAQVTPIYAVSHLFESLAGTSGGILRGSGNQKFGAIVNAIGYYVVGLPIGIALMFAAKLGVIGLWLGIVVCAVSQAVCFLGFIARLNWTKACQQARVHANLTVNTASNGNSAVLPDQPHPVGPDSHGGIVLRDADRKEGAELNEQVHPELPLPVRPEDSAHLSGKQLALRRGLLLLGVILVLLAGILVKVYVRTQ | null | null | organic cation transport [GO:0015695]; putrescine transport [GO:0015847]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; organic cation transmembrane transporter activity [GO:0015101]; polyspecific organic cation:proton antiporter activity [GO:0140968]; putrescine transmembrane transporter activity [GO:0015489]; thiamine transmembrane transporter activity [GO:0015234]; xenobiotic transmembrane transporter activity [GO:0042910] | PF01554; | null | Multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17442726}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q96FL8}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane; at the brush border membranes of the proximal tubules (kidney) and at the bile caniculi (liver). {ECO:0000250|UniProtKB:Q96FL8}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in); Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:Q96FL8}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(in) + H(+)(out) = estrone 3-sulfate(out) + H(+)(in); Xref=Rhea:RHEA:72139, ChEBI:CHEBI:15378, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q96FL8}; CATALYTIC ACTIVITY: Reaction=creatinine(in) + H(+)(out) = creatinine(out) + H(+)(in); Xref=Rhea:RHEA:72183, ChEBI:CHEBI:15378, ChEBI:CHEBI:16737; Evidence={ECO:0000250|UniProtKB:Q96FL8}; CATALYTIC ACTIVITY: Reaction=agmatine(in) + H(+)(out) = agmatine(out) + H(+)(in); Xref=Rhea:RHEA:72127, ChEBI:CHEBI:15378, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:Q96FL8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72128; Evidence={ECO:0000250|UniProtKB:Q96FL8}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72129; Evidence={ECO:0000250|UniProtKB:Q96FL8}; | null | null | null | null | FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation antiporter (PubMed:17442726). Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively. Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate. May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:Q96FL8, ECO:0000269|PubMed:17442726}. | Oryctolagus cuniculus (Rabbit) |
A7KAX9 | RHG32_HUMAN | METESESSTLGDDSVFWLESEVIIQVTDCEEEEREEKFRKMKSSVHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKTCGSTASMKVKHVKKLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEVMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDTLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYRTLEFLMRHLSLLADYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGRISMAMQEGAASLSRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEMLGNRCNSYDNLPHDNESEEEGGLLHIPALMSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSPGYSKDKPSANKKDAETGSSQCQTPGSTASSEPVSPLQEKLSPFFTLDLSPTEDKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMSISEPISVTLPPRVSEVIGTVSNTTAQNASSSTWDKCVEERDATNRSPTQIVKMKTNETVAQEAYESEVQPLDQVAAEEVELPGKEDQSVSSSQSKAVASGQTQTGAVTHDPPQDSVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQSLKRPGTSQAGYTNYGDIAVATTEDNLSSSYSAVALDKAYFQTDRPAEQFHLQNNAPGNCDHPLPETTATGDPTHSNTTESGEQHHQVDLTGNQPHQAYLSGDPEKARITSVPLDSEKSDDHVSFPEDQSGKNSMPTVSFLDQDQSPPRFYSGDQPPSYLGASVDKLHHPLEFADKSPTPPNLPSDKIYPPSGSPEENTSTATMTYMTTTPATAQMSTKEASWDVAEQPTTADFAAATLQRTHRTNRPLPPPPSQRSAEQPPVVGQVQAATNIGLNNSHKVQGVVPVPERPPEPRAMDDPASAFISDSGAAAAQCPMATAVQPGLPEKVRDGARVPLLHLRAESVPAHPCGFPAPLPPTRMMESKMIAAIHSSSADATSSSNYHSFVTASSTSVDDALPLPLPVPQPKHASQKTVYSSFARPDVTTEPFGPDNCLHFNMTPNCQYRPQSVPPHHNKLEQHQVYGARSEPPASMGLRYNTYVAPGRNASGHHSKPCSRVEYVSSLSSSVRNTCYPEDIPPYPTIRRVQSLHAPPSSMIRSVPISRTEVPPDDEPAYCPRPLYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLPNRDFAFYNPRLQGKSLYSYAGLAPRPRANVTGYFSPNDHNVVSMPPAADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPVMSQYDNMTPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKESRHAAKAISPEGEDRFYRRHPEAEMDRAHHHGGHGSTQPEKPSLPQKQSSLRSRKLPDMGCSLPEHRAHQEASHRQFCESKNGPPYPQGAGQLDYGSKGIPDTSEPVSYHNSGVKYAASGQESLRLNHKEVRLSKEMERPWVRQPSAPEKHSRDCYKEEEHLTQSIVPPPKPERSHSLKLHHTQNVERDPSVLYQYQPHGKRQSSVTVVSQYDNLEDYHSLPQHQRGVFGGGGMGTYVPPGFPHPQSRTYATALGQGAFLPAELSLQHPETQIHAE | null | null | regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase-mediated signal transduction [GO:0007264] | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; fibrillar center [GO:0001650]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; postsynaptic density [GO:0014069] | GTPase activator activity [GO:0005096]; phosphatidylinositol phosphate binding [GO:1901981] | PF00620;PF14604; | 3.30.1520.10;1.10.555.10;2.30.30.40; | PX domain-containing GAP family | PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN. Phosphorylated tyrosine residues undergo dephosphorylation after stimulation of NMDA receptors (By similarity). Phosphorylated in vitro by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q811P8}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q811P8}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12446789}. Endosome membrane {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane {ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q811P8}. Membrane {ECO:0000269|PubMed:17663722}. Note=Association to membrane via PX domain (PubMed:17663722). Associated with cortical actin in undifferentiated neuroblastoma cells, but localized to dendritic spine and postsynaptic density after differentiation (By similarity). Colocalizes with EGFR at the cell membrane upon EGF treatment (PubMed:12446789). Colocalizes with GAB2 at the cell membrane (PubMed:12819203). {ECO:0000250|UniProtKB:Q811P8, ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:17663722}. | null | null | null | null | null | FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722}. | Homo sapiens (Human) |
A7L9Z8 | AT2C2_MOUSE | MGRRLKFLQKLAFLGQNHRYKALERDEVETLIDEQCELKAIEREKTVAALPPGEACKCSREELARAFHVDLDSGLSEFAVAQRRLVHGWNEFVTDNAEPVWKKYLDQFRNPLILLLLGSSVVSVLTKEYEDAVSIALAVLIVVTVGFIQEYRSEKSLEELTKLVPPECNCLRDGKLRHMLARDLVPGDIVSLSMGDRIPADIRLTEVTDLLVDESSFTGEVEPCGKTDSPLADGGDLSTLSNVVFMGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTIFSFGIIGLLMLVGWVQGKPFLSMFTVGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVSGVGYSGEGTVCLLPSKEVIKGFDNVSVGKLVEAGCVANNAVIRKNAVMGQPTEGALVVLAMKMNLGSIKDSYVRKKEIPFSSEQKWMAVRCGPKSEDGEDIYFMKGAFEEVIHHCSMYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRAGVKEAVQVLSESGVSVKMVTGDALETALAIGRTIGLCNEKLKAMSGEEVEGTEQGALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAANMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPSPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALRRPPRSVGDTILNRALILRVLMSAAVIIGGTLFIFWREIPANGTSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSVLGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKLWEKFLSRARPTQMLPEAV | 7.2.2.10 | null | calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mammary gland epithelium development [GO:0061180]; manganese ion transport [GO:0006828]; positive regulation of calcium ion import [GO:0090280]; protein localization to plasma membrane [GO:0072659] | basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; P-type manganese transporter activity [GO:0140613] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15677451}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O75185}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:23840669}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:O75185}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000250|UniProtKB:O75185}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate; Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75185}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821; Evidence={ECO:0000250|UniProtKB:O75185}; | null | null | null | null | FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity). Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus (By similarity) (PubMed:23840669). {ECO:0000250|UniProtKB:O75185, ECO:0000269|PubMed:23840669}. | Mus musculus (Mouse) |
A7LCJ3 | SN_PIG | MDFLLLLLLLASSALAGLASWTVSRPETVQGIKGSCLIIPCTFGFPANVEVPHGITAIWYYDYSGKRLVVSHSRNPKVVENHFQGRALLLGQAEQRTCSLLLKDLQPQDSGSYNFRFEISEGNRWSDVKGTVVTVTEVPSVPTIALPAKLHEGMEVDFNCSTPYVCPTEPVNLQWQGQDPTRSVTSHLQKLEPSGTSHMETLHMALSWQDHGRILSCQVSAAERRMQKEIHLQVQHAPKGVEILFSHSGRNVLPGDLVTLSCQVNSSNPQVSSVQWVKDGTKLKDQKRVLQLRRAAWADAGVYTCQAGNAVGSSVSPPVSLHVFMAEVQVSPVGSILENQTVTLACNTPKEAPSELRYSWCKNHALLEGSHSRTLRLHSVTRADSGFYFCEVQNARGRERSPPVSVVVSHPPLTPDLTAFPETQAGLVGILQCSVVSEPPATLVLSHGGLISASTSGEGDHSPRFSVASAPNSLRLEIQDLGPTDSGEYMCSASSSLGNASSTLDFHANAARLLISPAAEVVEGQAVTLSCRSSLSLMPDTRFSWYLNGALILEGPSSSLLLPAASSTDAGSYHCRAQNSHSTSGPSPPAVLTVLRAPRQPVFTAQLDPDTAGAGAGRQGLLLCRVDSDPPAQLQLLHRGRVVASSLSWGGGCCTCGGCFQRMKVTKAPNLLRVEIRDPALEDEGVYLCEASSALGNASASATLDAQATVLVITPSHTLQEGIEANLTCNVSREASGPANFSWFRDGALWAQGPLDTVTLLPVSRTDAALYACRIVTEAGAGLSTPVALNVLYPPDPPKLSALLDVDQGHTAVFVCTVDSHPLAQLALFRGEHLLAASSALRLPPRGRLQAKASANSLQLEVRDLSLGDSGSYHCEATNILGSANTSLTFQVRGAWVRVSPSPELQEGQAVVLSCQVPIGVLEGTSYRWYRDGQPLQESTSATLRFAAITLSQAGAYHCQAQASGSATTDLAAPVSLHVTYAPRQATLTTLMDSGLGRLGLLLCRVNSDPPAQLRLLHGSRLVASTLQGVEELAGSSPRLQVATAPNTLRLEIHNAVLEDEGVYTCEATNTLGQTLASAALDAQAMRVQVWPNATVQEGQLVNLTRLVWTTHLAQLTYTWYRDQQQLPGAAHSILLPNVTVTDAASYRCGILIPGQALRLSRPVALDVLYAPRRLRLTHLLESRGGQLAVVLCTVDSRPAAQLTLSHAGRLLASSTAASVPNTLRLELWEPRPSDEGLYSCSARSPLGQANTSLELRLEGVQVALAPSATVPEGAPVTVTCEDPAARPPTLYVWYHNSRWLQEGSAASLSFPAATRAHAGAYTCQVQDAQGTRISQPAALHILYAPRDAVLSSFWDSRASPMAVVQCTVDSEPPAEMTLSHDGKVLATSQGVHGLAVGTGHVQVARNALQLRVQNVPSRDKDTYVCMDRNSLGSVSTMGQLQPEGVHVVAEPGLDVPEGTALNLSCRLPSGPGHIGNSTFAWFRNGRQLHTESVPTFTFTHVARAQAGLYHCQAELPAGAATSAPVLLRVLYPPKTPTMTVFVEPEGGIQGILDCRVDSEPLASLTLHLGSRLVASSQPQAAPAKPHIRVSASPNALRVDMEELKPSDQGEYVCSASNALGSASAATYFGTRALHRLHLFQHLLWFLGLLASLLFLLLGLGVWYAWRRGNFHKLRMGEYSVEMVSRKETTQMSTDQEEVTGIGDDAGSVNQAAFDPAHLCENTQSVKSTV | null | null | cell adhesion [GO:0007155]; clathrin-dependent endocytosis [GO:0072583]; clathrin-dependent endocytosis of virus by host cell [GO:0075512]; negative regulation of phagocytosis [GO:0050765]; symbiont entry into host cell [GO:0046718] | early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; late endosome [GO:0005770]; plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; virion binding [GO:0046790]; virus receptor activity [GO:0001618] | PF08205;PF07679;PF00047;PF13895;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32093750}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response. Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs). In turn, enhances macrophage-to-T-cell transmission of several viruses including reproductive and respiratory syndrome virus or porcine arterivirus (PubMed:10073688, PubMed:17567703). Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid (By similarity). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q9BZZ2, ECO:0000269|PubMed:10073688, ECO:0000269|PubMed:17567703}.; FUNCTION: (Microbial infection) Facilitates porcine reproductive and respiratory syndrome virus (PRRSV) infection via inhibition of type I IFN transcription. {ECO:0000269|PubMed:32093750}. | Sus scrofa (Pig) |
A7LFZ6 | DCL4_ORYSJ | MGDAAAAAPAAAAAGPSSTRGEPKDPRTIARKYQLDLCKRAVEENIIVYLGTGCGKTHIAVLLIYELGHLIRKPSREVCIFLAPTIPLVRQQAVVIASSTDFKVQCYYGNGKNSRDHQEWENDMREFEVLVMTPQILLQSLRHCFIKMNSIALLILDECHHAQPQKRHPYAQIMKEFYNSNSVEKFPRVFGMTASPIIGKGVMPSHSFTEKGGRSPCQPLIFFLPKGGSNKLNYTKCINSLEELLHAKVCSVDNEELESVVASPDMEVYFYGPVNHSNLTTICIKELDSLKLQSERMLRASLCDFKDSQKKLKSLWRLHENIIFCLQELGSFGALQAARTFLSFDGDKLDRREVDLNGSTSSFAHHYLNGATSILSRNKTDGSHAGSFDLEKLEEPFFSNKFSVLINVLSRYGLQENMKCIVFVKRITVARAISNILQNLKCLEFWKCEFLVGCHSGSKNMSRNKMDAIVQRFSSGEVNLLVATSVGEEGLDIQTCCLVVRFDLPETVASFIQSRGRARMTKSKYVVLLERENQSHEKLLNGYIAGESIMNEEIDSRTSNDMFDCLEENIYQVDNTGASISTACSVSLLHCYCDNLPRDMFFTPSPVFFYIDGIEGIICRLILPPNAAFRQADGQPCLSKDEAKRDACLKACVKLHKLGALTDFLLPGPGSRKNKVSVTNNSSNNKVEDDSLREELHEMLIPAVLKPSGLKLDSLSNLHFYYVKFIPIPEDRRYQMFGLFVINPLPVEAETLQVDLHLARGRIVKAGIKHLGKIAFEKEKMMLAHKFQEMCLKILLDRSEFTSPHVKLGNDVTLEINSTFYLLLPIKQKCYGDRFMIDWPAVERCLSSPIFKDPIDVSVHASYSSNESLRLLDGIFSKTDVVGSVVFSPHNNIFFFVDGILDEINAWSEHSGATYAEHFKERFRIELSHPEQPLLKAKQIFNLRNLLHNRLPETTESEGRELLEHFVELPPELCSLKVIGFSKDMGSSLSLLPSLMYRLENLLVAIELKDVMLSSFPEASQISASGILEALTTEKCLERISLERFEVLGDAFLKYVVGRHKFITYEGLDEGQLTRRRSDVVNNSHLYELSIRKKLQVYIRDQQFEPTQFFAPGRPCKVVCNTDVEVRLHQMDIHPDNRENCNLRCTRSHHWLHRKVIADVVESLIGAFLVEGGFKAAFAFLHWIGIDVDFNNPALYRVLDSSSINLSLMDYTDIAGLEELIGYKFKHKGLLLQAFVHPSFSQHSGGCYQRLEFLGDAVLEYVITSYLYSTYPDIKPGQITDLRSLAVGNDSLAYAAVEKSIHKHLIKDSNHLTSAISKFEMYVKLSNSEKDLLEEPACPKALGDIVESCIGAVLLDSGFNLNYVWKVMLMLLKPVLTFANMHTNPMRELRELCQCHGFELGLPKPMKADGEYHVKVEVNIKSKIIICTAANRNSKAARKFAAQETLSKLKNYGYKHRNKSLEEILIVARKRESELIGYNEDPIDVEADISVKMKSPHIHEENIPFQNTETSFTRSSKFHNQIIAGSGKHDVNNGRNNQPKLATQSGRLPSEATEKSNKKVYHGDMVHKTARSFLFELCAANYWKPPEFKLCKEEGPSHLRKFTYKVVVEIKGASATLLECHSDGKLQKKAAQEHAAQGALWCLKQLGHLPKEEDVRV | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | DNA-templated transcription termination [GO:0006353]; lsiRNA processing [GO:0010599]; maintenance of shoot apical meristem identity [GO:0010492]; polarity specification of adaxial/abaxial axis [GO:0009944]; reproductive structure development [GO:0048608]; RNAi-mediated antiviral immunity against RNA virus [GO:0051214]; siRNA processing [GO:0030422]; ta-siRNA processing [GO:0010267]; vegetative phase change [GO:0010050] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]; RNA binding [GO:0003723] | PF00270;PF03368;PF14709;PF00271;PF02170;PF00636; | 3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10; | Helicase family, Dicer subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the RNA silencing pathway. Cleaves double-stranded RNA to produce small interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. Required for the production of 21 nucleotide siRNAs. Regulates shoot apical meristem (SAM) initiation and maintenance, leaf polarization and lemma polarity through the trans-acting siRNAS (ta-siRNAs) pathway, which probably modulate the expression of the ARF2, ARF3, ARF4, ARF14 and ARF15 genes. Can process endogenous 21 nucleotide siRNAs derived from an imperfect inverted repeat. May not be involved in microRNAs (miRNAs) production. {ECO:0000269|PubMed:17804793, ECO:0000269|PubMed:17905898}. | Oryza sativa subsp. japonica (Rice) |
A7LXT0 | GH31A_BACO1 | MIMNMKNIFYCLLPGLLLGACSNKVYEKTGDSVIVKVQHKETGGPRLVRLQVMGDKLIHVSATADSKFADPQSLIVVPQKKQTSFAVVQNGDTITVSTEEVKASVLASTGEVWFTDKNGELILQENKGGGKTFTPIEVEGTKGYTVCQVFESPEDEAFYGLGQHQADEFNYKGKNEELFQYNTKVSVPFVVSNKNYGILLDSYSFCRFGNPNDYSQLNRIFKLYDKTGQEGALTGTYVPKKGETLVRREDSIYFENLKTIENLPKKLPLMGAKVTYEGEIEPAQTGEFKFILYYAGYVKVYLNNEPVVPERWRTAWNPNSYKFAAHLEAGKRVPLKIEWQPDGGQSYCGLRALTPVNPEEQGKQSWWSEMTKQLDYYFMAGENMDDVISGYRSLTGKSPVMPKWAMGFWQSREKYNTQEEMLGALKGFRDRKIPLDNIVLDWNHWPENAWGSHEFDKARFPDPKAMVDSIHAMHARMMISVWPKFYVTTEHFKEFDENGWMYQQSVKDSLKDWVGPGYHYGFYDAYDPDARKLFWKQMYEHYYPLGIDAWWMDASEPNVRDCTDLEYRKALCGPTALGSSTEFFNAYALMNAEAIYDGQRGVDNNKRVFLLTRSGFAGLQRYSTATWSGDIGTRWEDMKAQISAGLNFAMSGIPYWTMDIGGFCVENRYVAGQKQWNATKTENADYKEWRELNTRWYQFGAFVPLYRAHGQYPFREIWEIAPEGHPAYQSVVYYTKLRYNMMPYIYSLAGMTWFDDYTIMRPLVMDFTADAEVNDIGDQFMFGPSFMVSPVYRYGDRSREIYFPQAEGWYDFYSGKFQAGGERKVIEAPYERIPLYVRAGAIIPFGDDIQYTDEKPAEHIRLYIYQGADGEFTLYEDEGVNYNYEQGMYAMIPMKYDEATKTLVIGERQGEFPGMLKERTFTVVTVNKEKAQPFDLNAKGVTVKYNGSEQTLKL | 3.2.1.177 | null | symbiotic process benefiting host [GO:0085030]; xyloglucan catabolic process [GO:2000899] | plasma membrane [GO:0005886] | alpha-D-xyloside xylohydrolase [GO:0061634]; carbohydrate binding [GO:0030246]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553] | PF17137;PF13802;PF01055;PF21365; | 2.60.120.380;3.20.20.80;2.60.40.1760;2.60.40.1180; | Glycosyl hydrolase 31 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell inner membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.; EC=3.2.1.177; Evidence={ECO:0000269|PubMed:24463512}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.7 mM for Xyl-alpha-PNP {ECO:0000269|PubMed:24463512}; KM=31.8 mM for Glc-alpha-PNP {ECO:0000269|PubMed:24463512}; KM=0.223 mM for XXXG {ECO:0000269|PubMed:24463512}; KM=0.378 mM for XLLG {ECO:0000269|PubMed:24463512}; KM=38.1 mM for isoprimeverose {ECO:0000269|PubMed:24463512}; Note=kcat is 1.6 sec(-1) for Xyl-alpha-PNP. kcat is 0.071 sec(-1) for Glc-alpha-PNP. kcat is 32.6 sec(-1) for XXXG. kcat is 31.0 sec(-1) for XLLG. kcat is 1.78 sec(-1) for isoprimeverose.; | PATHWAY: Glucan metabolism; xyloglucan degradation. {ECO:0000269|PubMed:24463512}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512}; | null | FUNCTION: Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides in xyloglucan degradation, converting the 'X' to 'G' units. {ECO:0000269|PubMed:24463512}. | Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
A7LXT7 | BGH5A_BACO1 | MEKQSFSDGLFSPLGIKRVIFMLVLLTTSFISCSNSDEKGGSLEVAQEYRNLEFDARGSRQTIQIDGPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQSLYSVPAYDEYIAPDNTGMRDLTSMQLSALMKAGVNVGNTFEAVIVGNDGSLSGDETCWGNPTPNKVLFEGIKAAGFDVVRIPVAYSHQFEDAATYKIKSAWMDKVEAAVKAALDAGLYVIINIHWEGGWLNHPVDANKEALDERLEAMWKQIALRFRDYDDRLLFAGTNEVNNDDANGAQPTEENYRVQNGFNQVFVNTVRATGGRNHYRHLIVQAYNTDVAKAVAHFTMPLDIVQNRIFLECHYYDPYDFTIMPNDENFKSQWGAAFAGGDVSATGQEGDIEATLSSLNVFINNNVPVIIGEYGPTLRDQLTGEALENHLKSRNDYIEYVVKTCVKNKLVPLYWDAGYTEKLFDRTTGQPHNAASIAAIMKGLN | 3.2.1.151 | null | symbiotic process benefiting host [GO:0085030]; xyloglucan catabolic process [GO:2000899] | cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576] | beta-glucosidase activity [GO:0008422]; xyloglucan-specific endo-beta-1,4-glucanase activity [GO:0033946] | PF13004;PF00150; | 3.20.20.80;2.60.40.10; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}. | CATALYTIC ACTIVITY: Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151; Evidence={ECO:0000269|PubMed:24463512}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.036 mM for XXXG-beta-CNP {ECO:0000269|PubMed:24463512}; KM=0.145 mM for XLLG-beta-CNP {ECO:0000269|PubMed:24463512}; KM=3.59 mM for GGGG-beta-CNP {ECO:0000269|PubMed:24463512}; Note=kcat is 10.5 sec(-1) for XXXG-beta-CNP. kcat is 11.1 sec(-1) for XLLG-beta-CNP. kcat is 0.12 sec(-1) for GGGG-beta-CNP.; | PATHWAY: Glucan metabolism; xyloglucan degradation. {ECO:0000269|PubMed:24463512}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512}; | null | FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. {ECO:0000269|PubMed:24463512}. | Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
A7M7C7 | SKOR2_MOUSE | MASSPLPGPNDILLASPSSAFQPDALSQPRPGHANLKPNQVGQVILYGIPIVSLVIDGQERLCLAQISNTLLKNFSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAERLCKSFLGENRPPKLPDNFAFDVSHECAWGCRGSFIPARYNSSRAKCIKCSYCNMYFSPNKFIFHSHRTPDAKYTQPDAANFNSWRRHLKLTDKSPQDELVFAWEDVKAMFNGGSRKRALPQPSAHPACHPLSSVKAAAVAAAAAVAGGGGLLGPHLLGAPPPPPPPPPLAELAGAPHAHHKRPRFDDDDDSLQEAAVVAAASLSAAAASLSVAAATGGAGPGAGGPGGGCVAGVGVGASAGAGAAAGTKGPRSYPVIPVPSKGSFGGVLQKFPGCGGLFPHPYTFPAAAAAFGLCHKKEDAGTAAEALGGAGAGSAGAAPKAGLSGLFWPAGRKDAFYPPFCMFWPPRTPGGLPVPTYLQPPPQPPSALGCALGDSPALLRQAFLDLAEPGGAGGSAEAAPPPGQPPPVVANGPGSGPPATGGTGARDTLFESPPGGSGGDCSAGSTPPAEQGVTSGTGSASSGAGSVGTRVPAPHHPHLLEGRKAGGGSYHHSSAFRPVGGKDDAESLAKLHGASAGTPHSAPAHHHHHHHHPHHHHHHPPQPPSPLLLLQPQPDEPGSERHHPAPPPPPPPPPLAPQPHHRGLLSPEGTSCSYPSEDSSEDEEDEEEEQEVDVEGHKPLEGEEEEDGRDPEDEEEEDEETRVLLGDSLVGGGRFLQGRGLSEKGSGRDRTTPAVGAFPLALNSSRLLQEDGKLGDSGGSDLPAPPPPPLAPQKASSSGGSRPGSPVHHPSLEEEPSYKDNQKPKENNQVIISTKDDNFSDKNKGHGFFITDSDSSGDFWRERSGEHTQETNSPHSLKKDVENMGKEELQKVLFEQIDLRRRLEQEFQVLKGNTSFPVFNNFQDQMKRELAYREEMVQQLQIIPYAASLIRKEKLGAHLSKS | null | null | cell development [GO:0048468]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellum morphogenesis [GO:0021587]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of smoothened signaling pathway [GO:0045880]; regulation of cerebellar granule cell precursor proliferation [GO:0021936]; regulation of dendrite morphogenesis [GO:0048814]; regulation of neuroblast proliferation [GO:1902692]; smoothened signaling pathway [GO:0007224] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SMAD binding [GO:0046332] | PF08782;PF02437; | 3.10.390.10;3.10.260.20; | SKI family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18522874}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a TGF-beta antagonist in the nervous system (By similarity). Exhibits transcriptional repressor activity. {ECO:0000250, ECO:0000269|PubMed:18522874}. | Mus musculus (Mouse) |
A7MAQ2 | DIOA3_DIOJA | MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI | 1.6.5.4; 4.2.1.1 | null | carbon utilization [GO:0015976]; cellular oxidant detoxification [GO:0098869]; cellular response to carbon dioxide [GO:0071244]; negative regulation of endopeptidase activity [GO:0010951]; one-carbon metabolic process [GO:0006730]; positive regulation of gene expression [GO:0010628]; positive regulation of phagocytosis [GO:0050766]; response to oxygen radical [GO:0000305] | null | antioxidant activity [GO:0016209]; carbonate dehydratase activity [GO:0004089]; L-ascorbic acid binding [GO:0031418]; monodehydroascorbate reductase (NADH) activity [GO:0016656]; nutrient reservoir activity [GO:0045735]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q75N34}. | null | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:22195572, ECO:0000269|PubMed:25747844}; CATALYTIC ACTIVITY: Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378, ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59513; EC=1.6.5.4; Evidence={ECO:0000269|PubMed:22195572}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.49 mM for dehydroascorbate (DHA) (at ph 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:25747844}; KM=10.2 mM for sodium bicarbonate (at ph 7.1 and 4 degrees Celsius) {ECO:0000269|PubMed:25747844}; Note=kcat is 0.0152 min(-1) for DHA. kcat is 30500 min(-1) for sodium bicarbonate. {ECO:0000269|PubMed:25747844}; | null | null | null | FUNCTION: Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities (PubMed:22195572). Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2) (PubMed:25747844). Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages (PubMed:22796748). {ECO:0000269|PubMed:22195572, ECO:0000269|PubMed:22796748, ECO:0000269|PubMed:25747844, ECO:0000305}. | Dioscorea japonica (Japanese yam) |
A7MB74 | SGK1_BOVIN | MTVKTEAARDTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISPPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHVLEGLLQKDRTKRLGAKDDFMEIKNHVFFSLINWEDLINKKITPPFNPNVSGPSDLRHFDPEFTEEPVPNSIGRSPDSLLLTASVKEAAEAFLGFSYAPPMDSFL | 2.7.11.1 | null | apoptotic process [GO:0006915]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00433; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Regulated by phosphorylation. Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401 are also essential for its activity. Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell cycle progression (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by NEDD4L; which promotes proteasomal degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum; which promotes rapid proteasomal degradation and maintains a high turnover rate in resting cells (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A7MBB4 | M3K13_BOVIN | MANPQEHLSCSSSPRLPLSENKTFNGLQDDLAPMGSHASPKLLKDQQEKGMVQTELAEGTNSPITTTVLTSISEDSRDQFENSVLQLREQDESEMAMSHGNSNTVDGEGTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSTCPDGFKILMKQTWQSKTRNRPSFRQTLMHLDIASADVLATPQETYFKSQAEWREEVKKHFEKIKSEGTCIHRLDEELIRRRREELRHALDIREHYERKLERANNLYMELSAIMLQLEMREKELIKREQAVEKKYPGTYKRHPVRPIIHPNAMEKLMKRKGMPHRPGMQAKRPDLLRSEGIPSVEVAPTASPLSGSPKLSSSSSKSRYRSKPRHRRGNSRGSHGDFAAILKNQPAQEDSPHPTSLHQAEPQYPSSQHHNLLQQQYQQPPPAMSQSHHPRLNMHGQDIATCPNNLRYFGPAAALRSPLSNHSQRQMPGSSPDLISTAMAADCWRSSEPDKGQAGPWGCCQADPYDPCLQCRPEQHGSLDVPSAKPVGRSPSLFKPPAHNPLLENAQGSEKMEENEFSGYRSASSLGASHHITPPVLPRKTRPLQKSGDDSSEEEEGEVDSEVEFPRRQRPHRCISSCQSYSTFSSENFSVSDGEEGNTSDHSNSPDELADKLEDHLAEKLDDLLSQTPEIPIEISSHSDGLSDKECAVRRVKTQMSLGKLCAEERGYENPMQFEESDCDSSDGECSDATVRTNKHYSSATW | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | JNK cascade [GO:0007254]; phosphorylation [GO:0016310]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; membrane [GO:0016020] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated on serine and threonine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; | null | null | null | null | FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A7MBE0 | S22A1_BOVIN | MLTVDDVLEQVGEFGWFQKQTFLILCLLSAAFAPIYVGIVFLAFTPDHRCRSPGVAELSRRCGWSLAEELNYTVPGPGPESQCLRYEVDWNQSTLGCLDPLASLATNGSPLPLGPCEQGWVYDTPGSSIVTEFNLVCDDSWKVDLFQSCVNLGFFLGSLGVGYIADRFGRKVCLLATTLTCASLGVLTAVAPDYTSLLIFRLLQGLVSKGSWTAGYTLITEFVGLGYRRTVAILYQMAFTVGLVLLSGLAYILPHWRWLQLAVSLPIFLLLFRFWFVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFIDLFRTPNLRKYTFILMYLWFTSSVVYQGLIMHVGATGGNLYLDFLYSALVEFPAGFIILVTIDRFGRRYPLATSNLAAGLACFLMIFIPHDLPWLNIMVACVGRMGITIVFQMVCLVNAELFPTFIRNLGMMVCSSLCDLGGVLTPFLVFRLMEVWQGSPLILFAALGLVAGGMTLLLPETKGVTLPETIEDAENLQRKAKPKENKIYLQVQTSELNTQAAERDASQGTAQQK | null | null | (R)-carnitine transmembrane transport [GO:1902270]; acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; dopamine transport [GO:0015872]; monoamine transport [GO:0015844]; monoatomic ion transport [GO:0006811]; norepinephrine transport [GO:0015874]; organic cation transport [GO:0015695]; prostaglandin transport [GO:0015732]; putrescine transport [GO:0015847]; serotonin transport [GO:0006837]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934]; thiamine transport [GO:0015888]; xenobiotic transport [GO:0042908] | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328] | (R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; xenobiotic transmembrane transporter activity [GO:0042910] | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of hepatocytes. Mainly localized to the basolateral membrane of renal proximal tubular cells (By similarity). However, also identified at the apical side of proximal tubular cells. Mainly expressed at the lateral membrane of enterocytes. Also observed at the apical side of enterocytes. Localized to the basal membrane of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089}. | CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959, ChEBI:CHEBI:16347; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-isobutanoyl-(R)-carnitine(in) = O-isobutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74315, ChEBI:CHEBI:84838; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-acetyl-(R)-carnitine(in) = O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:74319, ChEBI:CHEBI:57589; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-3-hydroxybutanoyl-(R)-carnitine(in) = O-3-hydroxybutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74323, ChEBI:CHEBI:84842; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-propanoyl-(R)-carnitine(in) = O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74327, ChEBI:CHEBI:53210; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-butanoyl-(R)-carnitine(in) = O-butanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74331, ChEBI:CHEBI:21949; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-2-methylbutanoyl-(R)-carnitine(in) = O-2-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74335, ChEBI:CHEBI:84840; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-3-methylbutanoyl-(R)-carnitine(in) = O-3-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74339, ChEBI:CHEBI:70819; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-hexanoyl-(R)-carnitine(in) = O-hexanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74343, ChEBI:CHEBI:84834; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15245}; | null | null | null | null | FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (By similarity). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation. Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline. Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover. Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism. Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (By similarity). {ECO:0000250|UniProtKB:O08966, ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089}. | Bos taurus (Bovine) |
A7MBI0 | PACN1_BOVIN | MSGSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMSCVQERAKIEKAYAQQLTDWAKRWRQLLEKGPQYGSLERAWGAIMTEADKVSELHQEMKNSLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAVTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMEGMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAESSSYVQVYRELEQAIRGADAQDDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTAAKKEKQPKKAEGAALTNAAGVVESTSQAGDRGSVSSYDRGQTYATEWSDDESGNPFGGSEANGGSNPFDEDAKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEVV | null | null | actin filament organization [GO:0007015]; cytoskeleton organization [GO:0007010]; negative regulation of endocytosis [GO:0045806]; neuron projection morphogenesis [GO:0048812]; plasma membrane tubulation [GO:0097320]; positive regulation of dendrite development [GO:1900006]; protein localization to membrane [GO:0072657]; regulation of endocytosis [GO:0030100]; synaptic vesicle endocytosis [GO:0048488] | axon terminus [GO:0043679]; COPI-coated vesicle [GO:0030137]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endosome [GO:0005768]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; presynaptic endocytic zone [GO:0098833]; ruffle membrane [GO:0032587] | cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543] | PF00611;PF14604; | 1.20.1270.60;2.30.30.40; | PACSIN family | PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC). {ECO:0000305}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with MAPT in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites. Associates with membranes via its F-BAR domain (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A7MBI7 | COMT_BOVIN | MLEAPPLLLVAGGVGLALLALRWLATTDLQFFGRAFIVWNEFIMKPIRNLLMGSSKEQRILQHVLQHAVAGDPQSVVAAIDSYSLEKEWAMHVGEKKGQIVDRVLREQQPSVLLELGAYCGYSAVRMARLLLPGARLLTIEFNPDYAAITQRMVEFAGLQDKVTVVLGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDMLLLEECGLLREGTVLLADNVIYPGAPDFLEYVRGNSRFECSHFSSYLEYSKVVDGLEKVVYKGLSGPARP | 2.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P22734}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P22734}; | catecholamine catabolic process [GO:0042424]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; lipid metabolic process [GO:0006629]; methylation [GO:0032259] | axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; plasma membrane [GO:0005886] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: [Isoform Soluble]: Cytoplasm {ECO:0000250|UniProtKB:P22734}.; SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane {ECO:0000250|UniProtKB:P22734}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:P22734}. | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87602, ChEBI:CHEBI:136972; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100, ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089; Evidence={ECO:0000250|UniProtKB:P21964}; | null | null | null | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000250|UniProtKB:P21964}. | Bos taurus (Bovine) |
A7MBL8 | PKN2_DANRE | MAADSVQNDARGPMVSGRLDFDQNLDFSDTMVQKNLDEIKDQIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNMLKKSNKKVEELHQELQELNAHIVVKDPEEVEEYPLTPDTPKSETRMSTNSNRLAALKKQADIELKVKQGAEDMIQMYSNGSSKDRKLLAAAQQMLQDSKTKIEFIRMQILKASQTSEINYENNDVTTSKPIISPLDLRIEELRHHYRIESAVADGAKNVMKLLGTGKVTEKKAHSEAQARLNESSQKLDLLKFSLEQRLSELPKNHPKGTLIMEELAMVASPPNSPRQSIMSTSNQYSTVAKPAALTGTLDVRLMGCQDLLENVPGRSKTASVSLPGWSPSEARSSFMSRGNKNKSGSSRTLSKSDDLSNEISAVLKLDNTVVGQTHWKPVSNQSWDQKFTLELDRSRELEIAVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPSVNTSFSPQAADLGSAMSHETAPMGHPDAHSLPSDPTVTKLDFDKAVTPPSKRNSIEVEIEETAPPDKISDGKEVQDALATFDFLNNTVAKPDYDSLVEHEQPGLELTEIQRKTEIREEEEVQFSLSDFKCVAVLGRGHFGKVLLADYKTTGEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHADVFSETRSVFYAACVVLGLQFLHDHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFKDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPKYLSTEAISIMRRLLRRNPERRLGAGERDAEEVKRHPFFRDMDWPGLLAKKIRPPFVPTITSREDVSNFDDEFTSEAPILTPPREPRILTLGEQDLFADFDYIADWC | 2.7.11.13 | null | cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | anchoring junction [GO:0070161]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylated. Phosphorylated. {ECO:0000250}.; PTM: Proteolytically cleaved. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell junction {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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; | null | null | null | null | FUNCTION: Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling processes (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7MBS7 | THS7A_DANRE | MGLASRAPGKGGTSAGALASLFRVALLFFGLWDVQTQTVANTRPTYIWQTGPWGRCMGSECGPGGSQSRAVWCAHSEGWTTLHTNCQQSERPSNQQSCFRVCDWHKELYDWQLGAWNQCVPVSMRNAGVPRPAVCTRGEEGIQTREVGCVHKSDGVPAEDAICEYFEPKPRLEQACLIPCPRDCVVSEFSPWTSCSKSCGMGLQNRLRSVLAPPLFGGSACPNLTEFRTCQPGKCEGVESLHSLRVGPWGQCMASPIRQARDTGEARVPKAERKAKRDRQARQERQGKRRKNKEKKELRESKGERVRERVKEKKRMRDPETRELIKKKRTRNRQNRQGLKFWDLQVGYQTREVTCVHRSGSTASISQCTQQTLPVTYQACVISKDCEVSEWSDWSVCSKECYDLNGRKGQRTRTRQVQQFPVGGGAECPELEESEPCSPQGEGIPPCVVYNWRSTEWSDCRVDVLLSQQDRRRSNQTGLCGGGVQTREVYCVQAPSETSSNLGSLKSKDALRPVNSDLCLGVPHNTTQLCHIPCPVECEVSAWSAWGPCTFENCQDQSTKKGFKLRKRKIMNEPTGGTGNCPHLTEAIPCEEPSCYDWLLVKLEECVPDNDKVCGPGTQNPQVQCINSDGEFVDRQLCRDAILPMPVLCEVSCPKDCVLSPWTSWSLCSNTCSGKNSEGKQTRARSILAYNAGDGGVQCPNSSALQEVRSCNDHPCTVYHWQTGPWGQCIEDTSVPSANSSISRAVPGTAVNDAFCSVGMQTRKVICVRVNVGQVPPKKCPESLRPETVRPCLLPCKRDCVVTPYSDWTPCPSICQTGGSVKKKQSRKRIIIQLPANGGQDCPEVLFQEKDCDASSVCPGYRWKTHKWRRCQLVPWSIRQDSPGAQETCGPGLQARAVSCKKLDSGPADVAACLKFAGPMPQLTQSCQLPCQDDCQLTAWSKFSTCAADCVGVRTRKRTLVGKSKKREQCKNTQMYPLSETQYCPCNKYNAQPVGNWSDCILPEGRVEGLLGMKVQGDIKECGQGYRYQAMVCYDQDNRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCLSDCSQYVWVAEPWSVWKVSNVDLKENCGEGVQTRKVRCMQNTVDGPSDPVEDYLCDPEEMPLGARESKLPCPEDCVLTDWGSWSRCPLPCNVNSTRQRSASPIRQPSERKQCPSTTEKEICTLNSNCFHYSYNITDWSTCQLSERAVCGVGFKTRMLDCVRSDSKSVDLKFCEELGLEKKWQMNASCVVECPVNCQLSDWSSWSECSHTCGLAGKLWRRRTVIQASQGDGRPCSSQLEQWKPCPVKPCFSWRYSVWSPCKSEGARCGEGLRFRNVSCFVSDGSGKDAGSMVDEELCGDLEQTVDGDKQIILQESCTVPCPGECYLTDWTMWSPCQLSCIGGDDLGFGSVQVRSRAVLAQEPENLLQCPEQEWEARPCTEGQCYDYKWMTGAWRGSSRQVWCQRSDGLNVTGGCQSTTEPVSDRSCDPACDKPRSICTEAGICGCEEGYTEVMTSDGVLDQCTVIPVLEIPTAGDSKADVKTIRALNPTEPTANMPGRAGRTWFLQPFGPDGKLKTWVYGVAAGAFVLLVFIVSMTYLACKKPKKPQRRQMNNRLKPLTLAYDGDADM | null | null | angiogenesis [GO:0001525]; axon extension [GO:0048675]; blood vessel endothelial cell migration [GO:0043534]; glomerular filtration [GO:0003094]; glomerulus development [GO:0032835]; podocyte development [GO:0072015]; regulation of Notch signaling pathway [GO:0008593]; sprouting angiogenesis [GO:0002040] | cell projection [GO:0042995]; plasma membrane [GO:0005886] | null | PF19030;PF19028;PF00090; | 2.20.100.10; | null | PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q69ZU6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q69ZU6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q69ZU6}. Cell projection {ECO:0000250|UniProtKB:Q69ZU6}. Note=Detected on podocyte foot processes. {ECO:0000250|UniProtKB:Q69ZU6}. | null | null | null | null | null | FUNCTION: Required for normal sprouting angiogenesis and normal embryonic development of intersegmental vessels (ISV) (PubMed:21520329, PubMed:27484901). Required for normal function of the glomerular filtration barrier (PubMed:28814510). Required for normal axon outgrowth on embryonic motor neurons at the level of the horizontal myoseptum. Required for normal expression of notch1b, suggesting that its functions in angiogenesis and neuron outgrowth are due to decreased expression of notch1b (PubMed:27484901). Plays a role in actin cytoskeleton rearrangement (By similarity). {ECO:0000250|UniProtKB:Q69ZU6, ECO:0000269|PubMed:21520329, ECO:0000269|PubMed:27484901, ECO:0000269|PubMed:28814510}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7MCT6 | EKI2_MOUSE | MAVPPSAPVPCSPFYLRRQEPCPQCSWSMEEKAVASAGCWEPPGPPRAAVPCFSVTVEQDDILPGALRLIRELRPHWKPEQVRTKRFKDGITNKLLACYVEEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTIHANGSLPKPTLWHKMHRYFTLVKDEISPSLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNVVDYSRYPARETQVQWLRYYLEAQKGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKVKPQVSALEMPK | 2.7.1.82 | null | in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphorylation [GO:0016310]; placenta development [GO:0001890]; post-embryonic development [GO:0009791] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ethanolamine kinase activity [GO:0004305] | PF01633; | 3.90.1200.10; | Choline/ethanolamine kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine; Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216; EC=2.7.1.82; Evidence={ECO:0000269|PubMed:16861741}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. | null | null | FUNCTION: Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity. {ECO:0000269|PubMed:16861741}. | Mus musculus (Mouse) |
A7MCY6 | TBKB1_HUMAN | MESMFEDDISILTQEALGPSEVWLDSPGDPSLGGDMCSASHFALITAYGDIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEIKDGSLLEVEKVSLQQRLNQFQHELQKNKEQEEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQICGLEQQLRQQQGLQDAAFSNLSPPPAPAPPCTDLDLHYLALRGGSGLSHAGWPGSTPSVSDLERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSERDMAWVKRVGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGGQRHSPLSQRHSPAPQCPSPSPPARAAPPCPPCQSPVPQRRSPVPPCPSPQQRRSPASPSCPSPVPQRRSPVPPSCQSPSPQRRSPVPPSCPAPQPRPPPPPPPGERTLAERAYAKPPSHHVKAGFQGRRSYSELAEGAAYAGASPPWLQAEAATLPKPRAYGSELYGPGRPLSPRRAFEGIRLRFEKQPSEEDEWAVPTSPPSPEVGTIRCASFCAGFPIPESPAATAYAHAEHAQSWPSINLLMETVGSDIRSCPLCQLGFPVGYPDDALIKHIDSHLENSKI | null | null | canonical NF-kappaB signal transduction [GO:0007249]; defense response to virus [GO:0051607]; type I interferon-mediated signaling pathway [GO:0060337] | cytoplasm [GO:0005737]; serine/threonine protein kinase complex [GO:1902554] | metal ion binding [GO:0046872] | PF12845; | null | null | null | null | null | null | null | null | null | FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. {ECO:0000269|PubMed:21931631}. | Homo sapiens (Human) |
A7MD48 | SRRM4_HUMAN | MASVQQGEKQLFEKFWRGTFKAVATPRPESIIVASITARKPLPRTEPQNNPVVPAQDGPSEKLGQHLATEPLGTNSWERDKTCRELGATRGHSASHDKDLTPPPSSRGKKKKKKSTRKKRRRSSSYSPSPVKKKKKKSSKKHKRRRSFSKKRRHSSSSPKSKRRDEKRHKKQSRSRPRKSHRHRHHRCPSRSQSSESRPSSCESRHRGRSPEEGQKSRRRHSRRCSKTLCKDSPEAQSSRPPSQPLQMLGYLSARGVITGSGSAADLFTKTASPLTTSRGRSQEYDSGNDTSSPPSTQTSSARSRGQEKGSPSGGLSKSRELNSGNTSDSGNSFTTSSPQNKGAMLENLSPTSRGRESRGFQSPCLECAEVKKSSLVPSTARSSPMKGCSRSSSYASTRSSSHSSRSPNPRASPRYTQSRSTSSEKRSYSRSPSYSSKSGKRSPPSRSSRSRRSPSYSRYSPSRERDPKYSEKDSQQRERERARRRRRSYSPMRKRRRDSPSHLEARRITSARKRPIPYYRPSPSSSGSLSSTSSWYSSSSSRSASRSYSRSRSRSRSRRRSRTRTSSSSSSRSPSPGSRSRSRSRSRSRSRSRSQSRSYSSADSYSSTRR | null | null | cell differentiation [GO:0030154]; mRNA processing [GO:0006397]; nervous system development [GO:0007399]; neuron maturation [GO:0042551]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]; sensory perception of sound [GO:0007605] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; mRNA binding [GO:0003729] | PF15230; | null | NSR100 family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q8BKA3}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BKA3}. | null | null | null | null | null | FUNCTION: Splicing factor specifically required for neural cell differentiation. Acts in conjunction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural-specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural-specific exon 10 in nPTB/PTBP2, leading to increased expression of neural-specific nPTB/PTBP2. Also promotes the inclusion of exon 16 in DAAM1 in neuron extracts (By similarity). Promotes alternative splicing of REST transcripts to produce REST isoform 3 (REST4) with greatly reduced repressive activity, thereby activating expression of REST targets in neural cells (PubMed:30684677). Plays an important role during embryonic development as well as in the proper functioning of the adult nervous system. Regulates alternative splicing events in genes with important neuronal functions (By similarity). {ECO:0000250|UniProtKB:Q8BKA3, ECO:0000269|PubMed:30684677}. | Homo sapiens (Human) |
A7MRY4 | LUXN_VIBC1 | MFDFSLEAIVYAKAITLLATVAVVMMWLFYYCYRLKQKNEVIFGTHHAAYIAYSVCIIAWISSNAYFHTDLLPELGASAGMFMAKFANLASFFAFAFAYYFSCQLAAEQRKGKVHRWQQGIFVSLTVYSLFINLRPGLTVEHVDIVGPSQFIIEFGPHTSYFFIGLVSFVVLTLVNLVAMRTNSSKLTLAKTNYMIAGILVFMLSTAVIHLGMTYFMGDFSLTWLPPALSISEMLFVGYALLTSRFYSVKYIAYLALSVLLVCAIFVLPLGAIFIPLTESNQWLIAIPICALIGITWQLLYKKTSRYASFLIYGDKKTPVQQILSLEEDFKLSIDDAMRRLGKLLQIPNDKLRLVTSNYNETFYEEYLSSNRSVLVFDELSEELEYKVSAKRSMKALYDKMSSNNTALVMPLFGQGKSVTHLLISPHKSNNQMFSNEEISAVQTLLTRVQSTIEADRRIRQSRALANSIAHEMRNPLAQVQLQFEALKQHIENHAPVEQITLDIENGQAAIQRGRQLIDIILREVSDSSPEHEPIAMTSIHKAVDQAVSHYGFENEKIIERIRLPQHTDFVAKLNETLFNFVIFNLIRNAIYYFDSYPDSQIEISTKTGPYENTLIFRDTGPGIDETISHKIFDDFFSYQKSGGSGLGLGYCQRVMRSFGGRIECKSKLGTFTEFHLYFPVVPNAPKADTLRTPYFNDWKQNKRSNEHKVAPNVQINNQSPTVLIVDDKEVQRALVQMYLNQLGVNSLQANNGENAVEVFKANHVDLILMDVQMPVMNGFDASQRIKELSPQTPIVALSGESGERELDMINKLMDGRLEKPTTLNALRHVLGNWLNKNTASSACEAERE | 2.7.13.3; 3.1.3.- | null | null | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: At low cell density, in the absence of AI-1 (autoinducer 1), LuxN has a kinase activity and autophosphorylates on His-471. The phosphoryl group is then transferred on Asp-771 of the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-1, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity. LuxN phosphatase acts on itself. As LuxU could function to establish an equilibrium between the aspartyl-phosphate of LuxN and the aspartyl-phosphate of LuxO, LuxU transfers phosphate from LuxO to LuxN and finally phosphate is drained from the system. {ECO:0000269|PubMed:10632884}. | Vibrio campbellii (strain ATCC BAA-1116) |
A7N805 | MPAA_VIBC1 | MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; | cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | amidase activity [GO:0004040]; hydrolase activity, acting on ester bonds [GO:0016788]; murein tripeptide carboxypeptidase activity [GO:0061473]; zinc ion binding [GO:0008270] | PF04952; | 3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}. | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; | null | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}. | null | null | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide. {ECO:0000269|PubMed:22970852}. | Vibrio campbellii (strain ATCC BAA-1116) |
A7RDN6 | RNLS_MOUSE | MSRVLVVGAGLTGSLCAALLRKEITAPLYLGLWDKGGDIGGRMITASSPHNPRCTADLGAQYITCSPHYVKEHQNFYEELLAHGILKPLTSPIEGMKGKEGDCNFVAPQGFSSVIKYYLKKSGAEVSLKHCVTQIHLKDNKWEVSTDTGSAEQFDLVILTMPAPQILELQGDIVNLISERQREQLKSVSYSSRYALGLFYEVGMKIGVPWSCRYLSSHPCICFISIDNKKRNIESSECGPSVVIQTTVPFGVQHLEASEADVQKLMIQQLETILPGLPQPVATICHKWTYSQVTSSVSDRPGQMTLHLKPFLVCGGDGFTHSNFNGCISSALSVMKVLKRYI | 1.6.3.5 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; | cardiac left ventricle morphogenesis [GO:0003214]; dopamine metabolic process [GO:0042417]; epinephrine metabolic process [GO:0042414]; heart contraction [GO:0060047]; norepinephrine metabolic process [GO:0042415]; phosphate ion homeostasis [GO:0055062]; regulation of systemic arterial blood pressure [GO:0003073]; response to norepinephrine [GO:0071873]; response to salt [GO:1902074] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on NAD(P)H [GO:0016651] | PF01593;PF13450; | 3.90.660.10;3.50.50.60; | Renalase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17846919}. | CATALYTIC ACTIVITY: Reaction=1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:40395, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88138; EC=1.6.3.5; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; CATALYTIC ACTIVITY: Reaction=1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:40399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88137; EC=1.6.3.5; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; CATALYTIC ACTIVITY: Reaction=1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:48000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88139; EC=1.6.3.5; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; CATALYTIC ACTIVITY: Reaction=1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:47996, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88140; EC=1.6.3.5; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; | null | null | null | null | FUNCTION: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis. {ECO:0000250|UniProtKB:Q5VYX0}. | Mus musculus (Mouse) |
A7T1N0 | TMP2L_NEMVE | MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEEWNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFRRGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPGHQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVPAVVIDGSGRAASVVGFAYNHTIKRNVDGQTINVIDPQYEDEVRAKVVEVFGAKGADKTYSMIKDVLEDEKMISVYSLDGEISQDIDLAILKALLKANRSSPVAQLNLALAWNRIDLAKSDIFTEEQQWTTETLSAAMLTALLDDKAEFAELFLQNGLSMREFLSLDILCKLYAEVPGNTTIKPLLQKEMGKRQVKTIDMDVVGEVIEELMGDMFESYYRKDGHYFGELASYAEGLVLKNRKSSKDLLANINRIDPLPTPYLDVFLWAVLCNRRELARVLWEAGREPMAAALMASRLLKRMASRAQEDNTITDISSDLYDHARLFEERAVGVLDECFNENETLSQTLLVRELDHYSRMTALELAVSAESQDFIAHTSCQVLLTRLWMGTMAMNTRWWKVLVCLYLPVLIFPIIYFVPDEQHERQAAEREHQKSLNQKSSKVKSHKEKNDAPVVPVYRSKEEKAVSNDEEARVGTENEEEDFQLEDYIPEIREDDSMEVIMRNKKLGFCDRIMHFYSAPFSKFVGNVVGYLAFIFLYAYVVLFNFPRFDPAKTLGGIHPTEIVLYFWVFTILIEEIRQLAAKPPKYIKDKVSVYFSDTWNFVDIFSLTVFIIAIILRFFTNSRIFTASRIILSLDIIFFIVRSLQIFSVNRLLGPKLVMIQKMMQDLAQFIIILAVFTIAYGIALHAVMFPSPGIYARNNTWVTITSVVQYPYWQMYGELFLDEIQGEKPKEFGEVDPDGRWLSPLLLAIYMVFTNILLLNLLIAIFNYTFERVQEDSDKVWKFQRYDLVQEYHSRPVFAPPLVLLGHILIFIRWVWRMCRCGHPPRGSTMKIGLSPAEMEQMDNWEFQAAEMYIHQQQQKNSGTLEERVRALGDRVDCINSQLNRVLDSMSGTRAHALTDGNGLEGGHDSEGRLARMEVELSSNSESLQKILALLQQQPPVKGQAAVPIQLTLLHYKARSSPYPGSTAKRFAVQDNMVDWQVPFPDYKPVNYTAPVVLANPVWADKDLMAMSPRPELPYNQMDHTCNVNRVSYNGTYVVKDGLPLNPMGRTGMQGRGLLGRFGPNHAADPVVTRWKRTSAGVMLQGGKKVLEFVAIQRKDNNQWAIPGGMVEPGQLVTQALKAEFGEEAMAKLNVSQEEKERIAKQIERLFQQGQEIYKGYVDDPRNTDNAWMETVAVNFHDDKGDLFGDITLQAGDDAAAVRWQRVSGNIPLYASHVSILEKVAKMRDAAF | null | null | calcium ion transmembrane transport [GO:0070588]; sodium ion transmembrane transport [GO:0035725] | plasma membrane [GO:0005886] | ADP-ribose diphosphatase activity [GO:0047631]; ligand-gated calcium channel activity [GO:0099604]; ligand-gated sodium channel activity [GO:0015280]; metal ion binding [GO:0046872] | PF00520;PF18139;PF00293; | 3.90.79.10; | Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27333281, ECO:0000305|PubMed:28775320}; Multi-pass membrane protein {ECO:0000269|PubMed:29745897}. | null | null | null | null | null | FUNCTION: Nonselective, voltage-independent cation channel that mediates Ca(2+) and to a lesser extent Na(+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). Functions as a ligand-gated ion channel (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). Binding of ADP-ribose causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). May have ADP-ribose pyrophosphatase activity which reduces ADP-ribose levels induced by oxidative stress, thus preventing the channel activation by reactive oxygen species (PubMed:25620041, PubMed:27333281). {ECO:0000269|PubMed:25620041, ECO:0000269|PubMed:27333281, ECO:0000269|PubMed:28775320, ECO:0000269|PubMed:29745897}. | Nematostella vectensis (Starlet sea anemone) |
A7TUE1 | CCLOP_MEDTR | MEGRGFSGLYKNSSEELFLKTVMESPIGMPVPTMEMLGFKTVSQSFRTDSEELFKRWLTNDQEGYNSSSMGLNSRLSKRISTEIANMSNQQHIGVASEGRNNDKSCLQNNFLANDVSSDFNFPIRDPVDRELQSSNLFLAKAWFITDQRMTRSRSSELRRRYTEMQNSQAPQGLDSMFMVPEHDTNTIKEELANFNGFDYLSMCELPSQKGTFMSPSNSSSSTFNTHQLVDVDKVSSCVSMLKGTLQRKKLECQVEKEAAEDGLNEIFCIREPLFQSAFNEEESWNQQKLVNVQGDFTDQVNDPGVMQTLEGTTNFVLDGFANQTNQIQGRTASGEPSQSESSAAAPVISSGLDACEGPSNSNQTLGDSSWKQVGESTQNKVRGVREQIMDNLKDDRKRKSLERYGSVTSAVSDGKMDNTKKRRVERSRKMAEAKERNLTPTIPSDMQAILKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEDLADEKERLLEEIERILSETGKI | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877] | nucleus [GO:0005634] | protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | null | null | CYCLOPS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17722695, ECO:0000269|PubMed:21787150}. | null | null | null | null | null | FUNCTION: Involved symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Required for proper induction of early nodulin gene expression. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis. Acts downstream of CCAMK (PubMed:21692638). Required for symbiosome formation (i.e. the release of the bacteria from the ITs) and subsequent symbiosome development. Required for the expression of the nodule-specific RPG gene, which controls proper IT growth and is essential for symbiosome formation (PubMed:21787150). Acts upstream of ERN1, a transcriptional regulator required for nodulation (PubMed:17449807). {ECO:0000269|PubMed:17449807, ECO:0000269|PubMed:21692638, ECO:0000269|PubMed:21787150}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A7TZE6 | SKIT1_MOUSE | MGSTGLCFYGHCIVMFLLQMVTASSEPFIVNGLEGPVLASLGGNLELSCQLSPPQQAQHMEIRWFRNLYTEPVHLYRDGKDMFGEIISKYVERTELLKDGIGEGKVTLRIFNVTVDDDGSYHCVFKDGDFYEEHITEVKITAINLQVQIHVHPPNTKGVIVECHSGGWFPRPLMQWRDRRGEVIPAASKSHSQGRDKLFNMKISLLISESFFQKVICCLQNPLTGQEERTSVILSDAFFSWNRIWKMILGIILSMMVVSIFVFSCLLHHEHKVCKWKWDAPWIKGLLIMTSSMVTVVLVMVYLHMKQRVPVSDVHFELDTLWVEDISVILCSLMVPATMLVSYTYFRLKDWCQHNHAQRVFTSN | null | null | epithelial cell differentiation [GO:0030855]; gamma-delta T cell differentiation [GO:0042492]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive thymic T cell selection [GO:0045059]; regulation of cytokine production [GO:0001817]; T cell differentiation [GO:0030217]; T cell receptor signaling pathway [GO:0050852] | cell periphery [GO:0071944]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020] | signaling receptor binding [GO:0005102] | PF07686; | 2.60.40.10; | SKINT family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. Plays a central role in mediating key epithelial-immune interactions by being involved in the selection of Vgamma5(+)Vdelta1(+) T-cells, which constitute 90% of epidermal gammadelta T-cells. {ECO:0000269|PubMed:18408721}. | Mus musculus (Mouse) |
A7UL74 | CTF7_ARATH | MQAKINSFFKPSSSSSIAASVTTDTDDGLAVWENNRNAIVNTYQRRSAITERSEVLKGCIEKTLKKGSSSVPKNHKKKRNYTQFHLELGQSDFLLRHCAECGAKYAPGDELDEKNHQSFHKDYMYGLPFKGWQNEKAFTSPLFIKNRIVMVSENDSPAHRNKVQEVVKMMEVELGEDWILHQHCKVYLFISSQRISGCLVAEPIKEAFKLIASPDDERQLQKESSSSPSTSIQFGNIVLQREVSKRCRTSDDRLDNGVIVCEEEAKPAVCGIRAIWVSPSNRRKGIATWLLDTTRESFCNNGCMLEKSQLAFSQPSSIGRSFGSKYFGTCSFLLYKAQLIDTHFS | 2.3.1.- | null | anther development [GO:0048653]; cell division [GO:0051301]; developmental vegetative growth [GO:0080186]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in seed dormancy [GO:0009793]; embryo sac development [GO:0009553]; establishment of meiotic sister chromatid cohesion [GO:0034089]; leaf phyllotactic patterning [GO:0060772]; meiotic chromosome segregation [GO:0045132]; meiotic sister chromatid cohesion [GO:0051177]; mitotic sister chromatid cohesion [GO:0007064]; mitotic sister chromatid segregation [GO:0000070]; multicellular organismal reproductive process [GO:0048609]; root development [GO:0048364]; sister chromatid cohesion [GO:0007062] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | acetyltransferase activity [GO:0016407]; metal ion binding [GO:0046872]; peptide-lysine-N-acetyltransferase activity [GO:0061733] | PF13880;PF13878; | null | Acetyltransferase family, ECO subfamily | PTM: Autoacetylated. {ECO:0000269|PubMed:20671110}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20671110}. Cytoplasm {ECO:0000269|PubMed:20671110}. | null | null | null | null | null | FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:20671110). Involved in preservation of genome integrity and meiosis (PubMed:20671110, PubMed:23750584). Required for DNA repair and for the regulation of chromosome segregation during mitotic cell division (PubMed:20671110, PubMed:23750584). Knock-down mutants are extremely dwarf (PubMed:20671110). Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of WAPL1 and WAPL2 (PubMed:26813623). {ECO:0000269|PubMed:20671110, ECO:0000269|PubMed:23750584, ECO:0000269|PubMed:26813623}. | Arabidopsis thaliana (Mouse-ear cress) |
A7VJC2 | ROA2_RAT | MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIFLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY | null | null | G-quadruplex DNA unwinding [GO:0044806]; lung development [GO:0030324]; male gonad development [GO:0008584]; miRNA transport [GO:1990428]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oligodendrocyte differentiation [GO:0048709]; positive regulation of telomerase RNA reverse transcriptase activity [GO:1905663]; positive regulation of telomere maintenance via telomere lengthening [GO:1904358]; primary miRNA processing [GO:0031053]; response to mineralocorticoid [GO:0051385]; RNA transport [GO:0050658]; telomere capping [GO:0016233] | Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681] | DNA polymerase binding [GO:0070182]; G-rich strand telomeric DNA binding [GO:0098505]; miRNA binding [GO:0035198]; molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; pre-mRNA intronic binding [GO:0097157]; regulatory region RNA binding [GO:0001069]; RNA binding [GO:0003723]; single-stranded telomeric DNA binding [GO:0043047] | PF11627;PF00076; | 3.30.70.330; | null | PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (PubMed:24098712). According to a report, methylation affects subcellular location and promotes nuclear localization (PubMed:10772824). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (PubMed:24098712). {ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:24098712}.; PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000250|UniProtKB:P22626}. | SUBCELLULAR LOCATION: [Isoform B1]: Nucleus {ECO:0000269|PubMed:20406423}.; SUBCELLULAR LOCATION: [Isoform A2]: Nucleus {ECO:0000269|PubMed:20406423, ECO:0000269|PubMed:24098712}.; SUBCELLULAR LOCATION: [Isoform A2b]: Cytoplasm {ECO:0000269|PubMed:20406423}. Nucleus {ECO:0000269|PubMed:20406423}. Note=Mainly localizes in the cytoplasm in neural cells. {ECO:0000269|PubMed:20406423}.; SUBCELLULAR LOCATION: [Isoform B1b]: Cytoplasm {ECO:0000269|PubMed:20406423}. Nucleus {ECO:0000269|PubMed:20406423}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22626}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9578590, ECO:0000269|PubMed:9925756}. Cytoplasm {ECO:0000269|PubMed:9925756}. Cytoplasmic granule {ECO:0000250|UniProtKB:P22626}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes following sumoylation. {ECO:0000250|UniProtKB:P22626}. | null | null | null | null | null | FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus (PubMed:19099192). Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417, PubMed:9578590). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (PubMed:15659580). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). Also plays a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (By similarity). {ECO:0000250|UniProtKB:P22626, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:15659580, ECO:0000269|PubMed:9578590, ECO:0000303|PubMed:19099192}. | Rattus norvegicus (Rat) |
A7WLH8 | SUMO1_PIG | MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to heat [GO:0034605]; negative regulation of action potential [GO:0045759]; negative regulation of delayed rectifier potassium channel activity [GO:1902260]; protein sumoylation [GO:0016925]; roof of mouth development [GO:0060021] | nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nuclear stress granule [GO:0097165]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; septin ring [GO:0005940] | potassium channel regulator activity [GO:0015459]; protein tag activity [GO:0031386]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250|UniProtKB:P63165}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250|UniProtKB:P63165}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}. | Sus scrofa (Pig) |
A7WM73 | HEXO1_ARATH | MSTNLLRLILLFITLSITSSLSTPSPADSPPYLWPLPAEFSFGNETLSVDPTVTLIVAGNGGGSLIIRAAFDRYMGIIFKHASGRGSLLSRIRFLKMVEYDITSLKIVVHSDSEELQLGVDESYTLMVSKKNEQSIVGAATIEANTVYGALRGLETFSQLCAFDYITKSVQIYKAPWYIQDKPRFGYRGLLIDTSRHYLPIDVIKQIIESMSFAKLNVLHWHIVDEQSFPLETPTYPNLWKGAYSRWERYTVEDASEIVRFAKMRGINVMAEVDVPGHAESWGTGYPDLWPSLSCREPLDVTKNFTFDVISGILADMRKIFPFELFHLGGDEVNTDCWKNTTHVKEWLQGRNFTTKDAYKYFVLRAQQIAISKNWTPVNWEETFSSFGKDLDPRTVIQNWLVSDICQKAVAKGFRCIFSNQGYWYLDHLDVPWEEVYNTEPLNGIEDPSLQKLVIGGEVCMWGETADTSVVLQTIWPRAAAAAERMWSTREAVSKGNITLTALPRLHYFRCLLNNRGVPAAPVDNFYARRPPLGPGSCYAQ | 3.2.1.52 | null | carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203] | membrane [GO:0016020]; plant-type vacuole [GO:0000325]; secretory vesicle [GO:0099503]; vacuole [GO:0005773] | beta-N-acetylhexosaminidase activity [GO:0004563]; hexosaminidase activity [GO:0015929]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00728;PF14845; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | PTM: N-glycosylated. {ECO:0000269|PubMed:17644627}. | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:17644627}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627}; Vmax=151 umol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627}; | null | FUNCTION: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves. {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}. | Arabidopsis thaliana (Mouse-ear cress) |
A7WPL6 | BBLB_TOBAC | MFPLIILISFSLTSLSATATSGAGGGVANLYTCLIDHNVHNFSIYPTKNDQSSSNYFNLLDFSLQNLRFAASYMPKPTVIILPNSKEELVSTILCCRQASYEIRVRCGGHSYEGTSYVSFDGSPFVIVDLMKLDEVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQLLQKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNSTPIEIFPQFNALYLGPKTEVLSISNEEFPELGVKNDECKEMTWIESALFFSELADINGNSSNDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKIDDQAIAFPHRKGNLFAIQYLAQWNEEDDYKSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMDDDYLLRNASSRNSSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE | 1.1.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O64743}; | alkaloid biosynthetic process [GO:0009821]; nicotine biosynthetic process [GO:0042179]; response to jasmonic acid [GO:0009753] | plant-type vacuole [GO:0000325] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21343426}. | null | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21343426}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:21343426). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (PubMed:21343426). {ECO:0000269|PubMed:21343426}. | Nicotiana tabacum (Common tobacco) |
A7WYY0 | HCHA_STAA1 | 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 Mu3 / ATCC 700698) |
A7X5R6 | BAG6_ORNAN | MDPGGGGGGGGPGPGPDMEEPADLEVSVKTLDSQTRTFTVGAEMTVKEFKEHIAAAVSIPPDKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQGPSSGGASRAGSPSAPHAGAPPAGPRGPGAPVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMLRDIQALLARLEPQPGQQGQQGQQQGQALLAESGPPRPGPPGQTDGETSPREPTETREPTETREPEDGVAARGTGPAPGPAPAPAPEGNAAPNHPSPAEYAEVLQELQRVESRLQPFLQRYRAILGAAATTDYNNNTEGREEDQRVINLVGESLRLLGNTFVALSDLRCNLSATAPRHLHVVRPMSHYTAPMVLQQAAIPIQINVGTTVTMTGSGARPGPTDTTPTSGQTSSPTPSPTSGEPGPDGAPSGPAPPQAAGPPRLIRISHQSVEPVVMMHMNIPDSGSQTGGTSSASTASTGLPGQGLGQQVSGFPAAPTRVVIARPTPPQARPPHPGGPPPAPGATIPVPGSNASLAQMVSGLVGQLLMQPVLVAQGASGLGAPQAPATASASAGTTNTATTAGPAPGGPAQPPPPPPPGPPQAEVQFSQLLGSLLGPGVPGGPGTAGGATSVGSPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPAPEQAPAAAPPGSPPAGPGGAGGGPEALPPEFFTSVVQGVLSSLLGSLGARAGSGESIAGFIQRLSGSSNIFEPGADGALGFFGALLSVICQNLSMVDVVMLLHGHSQPLQRLQPQLRGFFHQHYLGGREPTGPAIRRATHTLITGLEEYVRDSFASVQVQPGVDITRTNLDFLQEQFNGIAAHVLHCTDSSFGVRLLELCNQGLFECLALNLHCLGGQQSALTNVINGRIRRLSGGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDQVLRYVRRLGEPPQPPPEEPMDVQGAERAPPEPERENASPAPGTTAEEAMSRGPPPAPEGPPPLEEQDGAAAAESEPWAAAVPPEWVPIIRQDLQTQRKVKPQPPLSDAYLSGMPAKRRKLRSDLQQRLRADPNYSPQHFPNAQRAFMDEP | null | null | brain development [GO:0007420]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; immune system process [GO:0002376]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; lung development [GO:0030324]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of proteolysis [GO:0045861]; proteasomal protein catabolic process [GO:0010498]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of embryonic development [GO:0045995]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; ubiquitin-dependent protein catabolic process [GO:0006511] | BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634] | misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022] | PF12057;PF00240; | null | null | PTM: Ricin can induce the cleavage by the caspase CASP3. {ECO:0000250|UniProtKB:P46379}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells. {ECO:0000250|UniProtKB:P46379}. | null | null | null | null | null | FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: May mediate ricin-induced apoptosis. {ECO:0000250|UniProtKB:P46379}. | Ornithorhynchus anatinus (Duckbill platypus) |
A7X657 | ITPK1_SOYBN | MAEKRFGVIGYALAPKKQNSFIRDSLVSLAKSRGIELVRVDSDKPLADQGPFDCVLHKLYGDDWKRQLQEFHTLYPNAVILDAPEAIERLHNRISMLQVVSELRIEDRPETFGIPKQIVIYDKATLLDPQAWESLKFPVIAKPLVADGSAKSHKMALVFTRDALNKLKPPIVLQEFVNHGGVIFKVYVVGEHVRCVKRKSLPDVSDEEKALGGVSEDLMSFSQVSNLATVNDCDGYYRLMHLDDDTEMPPDAFVVDIAGGLRRALKLNLFNFDVIRDARYGNRYLIIDINYFPGYAKMPGYEAVLTQFFCEVMLKKKQQEEQQQEEGNAPKEKEESLQA | 2.7.1.134; 2.7.1.159; 2.7.4.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13254; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20941; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; EC=2.7.1.134; Evidence={ECO:0000269|PubMed:18474240, ECO:0000269|PubMed:35635723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12453; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12454; Evidence={ECO:0000269|PubMed:35635723}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,6-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:70287, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:189099, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70288; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628, ChEBI:CHEBI:456216; EC=2.7.4.21; Evidence={ECO:0000269|PubMed:35635723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12794; Evidence={ECO:0000269|PubMed:35635723}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.28 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.5 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.083 umol/min/mg enzyme with Ins(3,4,5,6)P4 as substrate {ECO:0000269|PubMed:18474240}; | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). Able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting InsP6 kinase activity (PubMed:35635723). Has also some Ins(1,3,4,5,6)P5 phosphatase activity (PubMed:35635723). {ECO:0000269|PubMed:18474240, ECO:0000269|PubMed:35635723}. | Glycine max (Soybean) (Glycine hispida) |
A7X665 | ITPK2_SOYBN | MSESEVAGQRYRVGYALQGKKVESFIQPSLLDHAKQHSIDLVQIDPTAPLQQQGPFHCIIHKLHTQHWKNLLQQFSSKHPNTVIIDPPELVDRLHNRVSMLDAVTHLQFSLENATIGVPKQVVVNEPKSFDLHKFEEEQGLRFPVIAKPLAADGGAGSHELCLVFDEEGLHALSVPMVLQEFVNHGGVVFKIYVAGQRVNCVKRKSLGDITEEKLKVLRGSLPFSRVSSLGVEDEGGGAVEDAEMPPQSLVGELARGLREALGLNLFNVDVIRDGKEPTRYLVIDINYFPGYAKLPSYEPFITDFLLDIVRSKTA | 2.7.1.134; 2.7.1.159; 2.7.4.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; myo-inositol hexakisphosphate biosynthetic process [GO:0010264]; phosphorylation [GO:0016310]; response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.1490.220;3.40.50.11370;3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13254; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20941; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; EC=2.7.1.134; Evidence={ECO:0000269|PubMed:18474240, ECO:0000269|PubMed:35635723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12453; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12454; Evidence={ECO:0000269|PubMed:35635723}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,6-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:70287, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:189099, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70288; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628, ChEBI:CHEBI:456216; EC=2.7.4.21; Evidence={ECO:0000269|PubMed:35635723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12794; Evidence={ECO:0000269|PubMed:35635723}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46.2 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.78 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=1.97 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.76 umol/min/mg enzyme with Ins(3,4,5,6)P4 as substrate {ECO:0000269|PubMed:18474240}; | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). Barely able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting negligible InsP6 kinase activity (PubMed:35635723). Has also Ins(1,3,4,5,6)P5 phosphatase activity (PubMed:35635723). Probably involved in the regulation of drought and salinity tolerance by diverting the flux of inositol phosphate pool towards phytate biosynthesis (PubMed:29289899). {ECO:0000269|PubMed:18474240, ECO:0000269|PubMed:29289899, ECO:0000269|PubMed:35635723}. | Glycine max (Soybean) (Glycine hispida) |
A7X672 | ITPK3_SOYBN | MRLREEVACKNDDVCEKEEVVIENDVTVAQNHWCPVVNAGFSSPKRVVVVGYALTTKKIKSFLQPKLEGLARNKGILFVAIDHNRPLSDQGPFDIVLHKLSGKEWRQVLEDYRLSHPEVTVLDPPDAIQHLRNRQYMLQAVADMNLSDSYGIVGVPRQLVIKRDALAIPELVNKAGLTLPLVAKPLVADGSAKSHELSLAYEHFSLQNLEPPLVLQEFVNHGGVLFKVYIVGDAIKVVRRFSLPDVSKWELSKDAGIYRFPRVSCAAASADDADLDPTVAELPPRPLLEKLAKELRWRLGLRLFNLDIIREYGTRNHFYVIDINYFPGYGKMPEYEHIFTDFLLSLGQGKYKKK | 2.7.1.134; 2.7.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13254; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20941; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; EC=2.7.1.134; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12453; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12454; Evidence={ECO:0000250|UniProtKB:Q84Y01}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,6-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:70287, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:189099, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70288; Evidence={ECO:0000269|PubMed:18474240}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.4 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=1.05 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.86 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.22 umol/min/mg enzyme with Ins(3,4,5,6)P4 as substrate {ECO:0000269|PubMed:18474240}; | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). {ECO:0000269|PubMed:18474240}. | Glycine max (Soybean) (Glycine hispida) |
A7X680 | ITPK4_SOYBN | MRLNGEISSGEEEEEEKQTGTTTFSSQKVVVGYALTSKKKKSFLQPSFTGLARNRGINFVAIDLNKPLPEQGPFDIILHKLSGEVWREIIEDYREKHPEVTVLDPPDAIQHLHNRQSMLQDVLDLNLSDCHGKVGVPRQLVITKEKDPSSIPYEVTKAGMKLPLVAKPLVVDGTAKSHELFLAYDEFSLSAVEPPLVLQEFVNHGGLLFKIYIVGETIKVVRRFSLPNISKRELSKVAGVFRFPRVSCAAASADDADLDPNIAEHPPRPLLERLARELRHRLGLHLFNIDMIREYGTKDVFYVIDINYFPGYGKMPGYEHVFTDFLLSLVESKCSNKKLAA | 2.7.1.134; 2.7.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.1490.220;3.40.50.11370; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13254; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20941; Evidence={ECO:0000269|PubMed:18474240}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; EC=2.7.1.134; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12453; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12454; Evidence={ECO:0000250|UniProtKB:Q84Y01}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,6-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:70287, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:189099, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70288; Evidence={ECO:0000269|PubMed:18474240}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.7 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.007 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.004 umol/min/mg enzyme with Ins(3,4,5,6)P4 as substrate {ECO:0000269|PubMed:18474240}; | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). {ECO:0000269|PubMed:18474240}. | Glycine max (Soybean) (Glycine hispida) |
A7X8B3 | PRGR_PANTR | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSNEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGCKAGDSSGTAAAHKVLPRGLSPSRQLLLPASGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPXRSPLATTMMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAXSAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK | null | null | intracellular steroid hormone receptor signaling pathway [GO:0030518]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270] | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1 (By similarity). {ECO:0000250}.; PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity). {ECO:0000250}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity). {ECO:0000250}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000250|UniProtKB:P06401}. | Pan troglodytes (Chimpanzee) |
A7X8B7 | PRGR_GORGO | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK | null | null | glandular epithelial cell maturation [GO:0002071]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:0042326]; ovulation from ovarian follicle [GO:0001542]; paracrine signaling [GO:0038001]; progesterone receptor signaling pathway [GO:0050847]; regulation of epithelial cell proliferation [GO:0050678]; regulation of transcription by RNA polymerase II [GO:0006357]; tertiary branching involved in mammary gland duct morphogenesis [GO:0060748] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | ATPase binding [GO:0051117]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; estrogen response element binding [GO:0034056]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]; transcription coactivator binding [GO:0001223]; zinc ion binding [GO:0008270] | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1 (By similarity). {ECO:0000250}.; PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity). {ECO:0000250}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity). {ECO:0000250}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000250|UniProtKB:P06401}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A7XDQ9 | B3GTK_ARATH | MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVDSKESKTTSWFKRFIGREQKPEVTWSFPFAEGKVFVLTLRAGIDGFHINVGGRHVSSFPYRPGFTIEDATGLAVTGDVDIHSIHATSLSTSHPSFSPQKAIEFSSEWKAPPLPGTPFRLFMGVLSATNHFSERMAVRKTWMQHPSIKSSDVVARFFVALNPRKEVNAMLKKEAEYFGDIVILPFMDRYELVVLKTIAICEFGVQNVTAPYIMKCDDDTFIRVESILKQIDGVSPEKSLYMGNLNLRHRPLRTGKWTVTWEEWPEAVYPPYANGPGYIISSNIAKYIVSQNSRHKLRLFKMEDVSMGLWVEQFNASMQPVEYSHSWKFCQYGCTLNYYTAHYQSPSQMMCLWDNLLKGRPQCCNFR | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26690932}; | arabinogalactan protein metabolic process [GO:0010405]; protein O-linked glycosylation via hydroxyproline [GO:0018258]; root hair cell development [GO:0080147] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | carbohydrate binding [GO:0030246]; hydroxyproline O-galactosyltransferase activity [GO:1990714] | PF00337;PF01762; | 2.60.120.200;3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23430255}; Single-pass type II membrane protein {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:23430255}; | null | FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. {ECO:0000269|PubMed:23430255, ECO:0000269|PubMed:25974423, ECO:0000269|PubMed:26690932}. | Arabidopsis thaliana (Mouse-ear cress) |
A7XGN8 | LOV1B_ARATH | MAEGVVLFGVHKLWELLNRESARLNGIGEQVDGLKRQLGRLQSLLKDADAKKHESERVRNFLEDVRDIVYDAEDIIESFLLNEFRTKEKGIKKHARRLACFLVDRRKFASDIKGITKKISEVIGGMKSLGIQEIIDGASSMSLQERQREQKEIRQTFANSSESDLVGVEQSVEALAGHLVENDNIQVVSISGMGGIGKTTLARQVFHHDMVQRHFDGFAWVFVSQQFTQKHVWQRIWQELQPQNGDISHMDEHILQGKLFKLLETGRYLVVLDDVWKEEDWDRIKAVFPRKRGWKMLLTSRNEGVGIHADPKSFGFKTRILTPEESWKLCEKIVFHRRDETGTLSEVRVDEDMEAMGKEMVTCCGGLPLAVKVLGGLLATKHTVPEWKRVYDNIGPHLAGRSSLDDNLNSIYRVLSLSYEDLPMCLKHCFLYLAHFPEYYEIHVKRLFNYLAAEGIITSSDDGTTIQDKGEDYLEELARRNMITIDKNYMFLRKKHCQMHDMMREVCLSKAKEENFLEIFKVSTATSAINARSLSKSRRLSVHGGNALQSLGQTINKKVRSLLYFAFEDEFCILESTTPCFRSLPLLRVLDLSRVKFEGGKLPSSIGDLIHLRFLSLHRAWISHLPSSLRNLKLLLYLNLGFNGMVHVPNVLKEMQELRYLQLPMSMHDKTKLELSDLVNLESLMNFSTKYASVMDLLHMTKLRELSLFITDGSSDTLSSSLGQLRSLEVLHLYDRQEPRVAYHGGEIVLNCIHLKELELAIHMPRFPDQYLFHPHLSHIYLWCCSMEEDPIPILERLLHLKSVILTFGAFVGRRMVCSKGGFPQLCFLKLEELEELEEWIVEEGSMPLLRALTICNCRKLKLPGGINYITSLKELTIVGMKWKEKLVPGGEDYYKVQNIPNVQFINCDE | null | null | defense response [GO:0006952]; defense response to other organism [GO:0098542]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | ADP binding [GO:0043531]; ATP binding [GO:0005524] | PF00931;PF18052; | 1.20.5.4130;1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10; | Disease resistance NB-LRR family, RPP8/HRT subfamily | null | null | null | null | null | null | null | FUNCTION: Confers susceptibility to the fungus Cochliobolus victoriae by conditioning victorin-dependent (victorin is a toxin synthesized by C.victoriae) induction of defense-associated proteins. {ECO:0000269|PubMed:17804803, ECO:0000269|PubMed:18052878}. | Arabidopsis thaliana (Mouse-ear cress) |
A7XUJ6 | TRAF6_PIG | MSLLHCENSCGSSQSESDCCAAMAASSCGAAAKDDGVSGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNVGCLHKMELRHLEDHQAHCEFALMNCPQCQRPFQKCQLNIHILKECPRRQVSCVNCAVSMAFEDKEIHDQNCPLANVICEYCNTVLIREQMPNHYDLDCPTAPVPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMMAQALQGLSLAVAPVPQRDMLPYDSSPLSRISSGCCSDQNFQETIQQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRSLEDKVAEIEAQQCNGIYIWKIGNFGMHLKSQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPIRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLDALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDSGT | 2.3.2.27 | null | DNA damage response [GO:0006974]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; nucleus [GO:0005634] | tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF21355;PF18048;PF13923;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Sumoylated on Lys-125, Lys-143 and Lys-472 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated on Lys-125 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. LRRC19 induces 'Lys-63' ubiquitination (By similarity). Ubiquitinated at Lys-338 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250|UniProtKB:P70196}. | 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 ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN (By similarity). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (By similarity). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | Sus scrofa (Pig) |
A7XY94 | NMDE2_XENLA | MRPTEACCYLKISLIILFYMGCYAQKHPNMDIAVILVGTTEEVAIKDVHEKDDFHHLPVTPRVALVTMNESDPKSIITRICDLMSDKKVQGVVFGDDTDQEAIAQILDFISVQTLTPILGIHGGSSMIMADKEEASMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFENKVRSTIENSFVGWELEEVIHLDMSLDDIDSKIQNQLKKLQSPVILLYCTKEEATYIFEVAHSVGLTGYGFTWIVPSLVAGDTDTVPDEFPTGLISVSYDEWDYDLPARVRDGIAIITTAASTMLSEHNSIPQSKSSCNNIQESRVYEAHMLKRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNQERKWERVGKYKDRSLKMKYYVWPVFDLYPNSEEHKDEHLSIVTLEEAPFVIVEDVDPLSGTCMRNTVPCRKQIRPENRTEEGGNYIKRCCKGFCIDILKKIAKTVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVTKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPAFRFGTVPNGSTERNIRNNYLEMHSYMVKFNQRSVQDALLSLKSGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFATTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIMEHLFFWQLRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEDRQSALDSPSATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSFQPEENLFSDYISEVERTFGNLQLKDSNVYQDHFHHHRPHSIGSNSSIDGLYDCDNAPFTTQPRSLSKKPLDIGLPSKHPSPQIGDLYGKFSFKSDHYGAPDDLIRSDVSDISTHTVTYGNIEGNAKRRKQYKDSLKKRPASAKSRREFDEIELAYRRRQRSPDHKRYFRDKEGLRDFYLDQFRTKENNPHWEHVDLTHIYAERADDFKHDTSCSNRQHQKHVGEFVQTDRKHGSGGNAWEKNMSNIEWEDRASSNFCRNCPSKMHNYTGQNTNRPACIRCEVCKKAGNLYDISEDNSLQDLEARPIQAPNSKYPQSPNGKAQKRNRSKLHRQHSYDTFVDLQKEDVTLAPRSVSLKDKERFLDGSPYAHMFEMPNETSFTSKSHGPTHNPGGYMLSRSLYPDRVTQNPFIPTFGDDQCLLHGSKPYYFRQPAIGGLKGRADFRGAGKSLSAQHSGPSGHFQKDICIGNQPNACVSNNKNPRSFNNSTNGHVYEKLSSIESDV | null | null | excitatory postsynaptic potential [GO:0060079]; long-term synaptic potentiation [GO:0060291]; response to magnesium ion [GO:0032026]; response to zinc ion [GO:0010043] | late endosome [GO:0005770]; lysosome [GO:0005764]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | metal ion binding [GO:0046872]; NMDA glutamate receptor activity [GO:0004972] | PF01094;PF00060;PF10613;PF10565;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, NR2B/GRIN2B subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:18177891, PubMed:25008524, PubMed:28232581). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581, ECO:0000305}. | Xenopus laevis (African clawed frog) |
A7XYQ1 | SOBP_HUMAN | MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGHAENFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRGAAAEGAKSAEPPPEQPPPPPPPAPPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK | null | null | animal organ development [GO:0048513]; cochlea development [GO:0090102]; cognition [GO:0050890]; inner ear morphogenesis [GO:0042472]; locomotory behavior [GO:0007626]; sensory perception of sound [GO:0007605] | nucleus [GO:0005634] | metal ion binding [GO:0046872]; SUMO polymer binding [GO:0032184] | PF15279; | null | SOBP family | null | null | null | null | null | null | null | FUNCTION: Implicated in development of the cochlea. {ECO:0000250|UniProtKB:Q0P5V2}. | Homo sapiens (Human) |
A7YE96 | IT70A_DANRE | MPPMTIKDGEYTATVYKMIKEGRYGDAIHILSKEHQKHTKSRAALSLLGYCYYHMQDFTNAAECYEQLTQLHPEVEDYKLYYAQSLYGACAFPEAMKSTFLLDNTTSHTKMIKLQAAIKYGEEDYSGAKTLVEQLPQEDPDYDVDLGCLLYKEGEFEEACKKFMSSMNVLGYQPDLAYNIALCYYSLKQYASALKYIAEIIERGIREHPELSIGMTTEGIDVRSVGNTLILHETALIEAFNLKAAIEYQLKNYAAAQEALTDMPPRSEEELDPVTLHNQALMNMDTKPTEGFEKLAFLLQQNPFPPVTFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYEFLDAMITCQTAPEEAFRKFDENAGKLTEQLRKVTKQVQEARHNRDDESLKKYVQDYDEVLEKYIPVLMAQAKIYWNRENYSMVEKIFHKSLEFCNEHDTWKLNVAHVLFMQDNKYKEAIGFYEPIVKKHYENILNVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQISYDDPDKKIFHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYNKKLGTDTWFYAKRCFLSLLENMAKHMIMLRDSVVQECIQFLEHCELYGKDVLAIIEQPLEEDRMHIGKNTVTYESRLIKALFYEVTGWNE | null | null | cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; establishment of planar polarity [GO:0001736]; intraciliary transport [GO:0042073]; opsin transport [GO:0036372]; protein polyglutamylation [GO:0018095] | axonemal microtubule [GO:0005879]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | intraciliary transport particle B binding [GO:0120170]; tubulin-glycine ligase activity [GO:0070738] | PF07719;PF13174; | 1.25.40.10; | TTC30/dfy-1/fleer family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17761526}. | null | null | null | null | null | FUNCTION: Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip (By similarity). Required for polyglutamylation of axonemal tubulin, which is a prerequisite for correct assembly of cilia and for normal cilia beat amplitude. Does not seem to be required for neuronal microtubule polyglutamylation. {ECO:0000250, ECO:0000269|PubMed:17761526}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7YW45 | ANM5_BOVIN | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFTQEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTSHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNIQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPESLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL | 2.1.1.320 | null | circadian regulation of gene expression [GO:0032922]; DNA-templated transcription termination [GO:0006353]; endothelial cell activation [GO:0042118]; Golgi ribbon formation [GO:0090161]; peptidyl-arginine methylation [GO:0018216]; regulation of DNA-templated transcription [GO:0006355]; spliceosomal snRNP assembly [GO:0000387] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; methylosome [GO:0034709]; nucleus [GO:0005634] | E-box binding [GO:0070888]; histone arginine N-methyltransferase activity [GO:0008469]; histone H4R3 methyltransferase activity [GO:0044020]; methyl-CpG binding [GO:0008327]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N symmetric methyltransferase activity [GO:0035243]; transcription corepressor activity [GO:0003714] | PF05185;PF17286;PF17285; | 3.20.20.150;2.70.160.11;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14744}. Nucleus {ECO:0000250|UniProtKB:O14744}. Golgi apparatus {ECO:0000250|UniProtKB:O14744}. Note=Localizes to promoter regions of target genes on chromosomes (By similarity). Localizes to methylated chromatin (By similarity). {ECO:0000250|UniProtKB:O14744}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320; Evidence={ECO:0000250|UniProtKB:O14744}; | null | null | null | null | FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). May methylate the N-terminal region of MBD2 (By similarity). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL. Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (By similarity). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity). {ECO:0000250|UniProtKB:O14744, ECO:0000250|UniProtKB:Q8CIG8}. | Bos taurus (Bovine) |
A7YY44 | PAR1_BOVIN | MGPRWLLLWAAGLGLCSPLVSARTRGPRPGTDPTNGTLGPRSFFLRNSNDGYEQIPLPEDEDSSEGEFTEDRLSSGNRSSPPQKSPPGFISKSASGYLTSAWLTVFIPSVYTGVFLVSLPLNIMAVVVFVLKMKVKKPAVVYMLHLAAADVLFVCVLPFKISYYFSGSDWRFGSAMCRFVTAAFYGNMYASIMLMTAISVDRFLAVVYPIQSLSWRTLGRASFICLAIWAMAIAGVAPLLLQEQATQVPGLNITACHDVLNQTLLEGYYSYYFSAFSAVFFFVPLTLSTVSYVSIIRCLSSSTVANQNKKSRALLLSAAVFCIFILCFGPTNILLLLHYAFLSSDPMTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRHLFAILHCKESSDPGSCNSSGQLMPSKMDTCSSNLSSSLYKKLLT | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; establishment of synaptic specificity at neuromuscular junction [GO:0007529]; G protein-coupled receptor signaling pathway [GO:0007186]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of glomerular filtration [GO:0003105]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of renin secretion into blood stream [GO:1900134]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; platelet activation [GO:0030168]; positive regulation of blood coagulation [GO:0030194]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of vasoconstriction [GO:0045907]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of interleukin-1 beta production [GO:0032651]; regulation of sensory perception of pain [GO:0051930]; regulation of synaptic plasticity [GO:0048167]; release of sequestered calcium ion into cytosol [GO:0051209]; response to lipopolysaccharide [GO:0032496]; response to wounding [GO:0009611]; thrombin-activated receptor signaling pathway [GO:0070493] | caveola [GO:0005901]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; platelet dense tubular network [GO:0031094]; postsynaptic membrane [GO:0045211] | G protein-coupled receptor activity [GO:0004930]; G-protein alpha-subunit binding [GO:0001965]; G-protein beta-subunit binding [GO:0031681]; thrombin-activated receptor activity [GO:0015057] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Proteolytic cleavage by thrombin generates a new N-terminus that functions as a tethered ligand. Also proteolytically cleaved by cathepsin CTSG. {ECO:0000250|UniProtKB:P25116}.; PTM: Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26824}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26824}. | null | null | null | null | null | FUNCTION: High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores. The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores (By similarity). In astrocytes, the calcium released into the cytosol allows the (Ca2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). May play a role in platelets activation and in vascular development (By similarity). {ECO:0000250|UniProtKB:P25116, ECO:0000250|UniProtKB:P26824, ECO:0000250|UniProtKB:P30558}. | Bos taurus (Bovine) |
A7Z019 | SMCA4_BOVIN | MSTPDPALGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSIMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYTQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQPQMPALPPPSVSATGPGPSPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQPAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGPSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED | 3.6.4.- | null | nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; hydrolase activity [GO:0016787]; RNA binding [GO:0003723] | PF07533;PF00439;PF00271;PF07529;PF08880;PF14619;PF00176; | 1.20.5.170;3.40.5.120;1.20.920.10;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TKT4}. Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities (By similarity). In brown adipose tissue, involved in the regulation of thermogenic genes expression (By similarity). {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}. | Bos taurus (Bovine) |
A7Z056 | UBP20_BOVIN | MGDSRDLCPHLDSIGEVTKEDLLLKSKSTCQSCGVSGPNLWACLQVSCSYVGCGESFADHSTLHAQAKKHNLTVNLTTFRVWCYACEKEVFLEPRLAAHPPGPAPKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHRKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATAAALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRSGGGSQAEAELLMADEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALEQQPPETQPPSPRSTSPCRTPEPDNEAHMRSSRPCSPVHHHEGHAKLASSPHRASPVRMGPAYVLKKAQVPGSRRRKEQSYRSVISDIFDGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYVAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKISSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQNVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEIDTFIKLNKAFQAEESPSVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHIQLKPGADYGQISEETWVYLNNLYGGGPEIAIRQSVAQLPDPESLHGEQKIEAETRAL | 3.4.19.12 | null | 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]; endoplasmic reticulum [GO:0005783]; 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 {ECO:0000250|UniProtKB:Q8C6M1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2K6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y2K6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2K6}. | 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:Q9Y2K6}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis. Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination. Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization. Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1. Acts as a positive regulator for NF-kappa-B activation by TNF-alpha through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination 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, possibly 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. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability. Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol. {ECO:0000250|UniProtKB:Q9Y2K6}. | Bos taurus (Bovine) |
A7Z063 | WASH1_BOVIN | MTPTGTQHSLAGQTYAVPLIQPDLRREEAIQQVADALQYLQKVSGDIFSRISQRVELSRSQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFMGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKFFPVCVNTKPEPEDEAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISRREQLERQVPENYFYVPDLGQVPDIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPTFHTEVAQPFKPDLEDGVLTARPPPPPPPPPPPAPAVLMSVPPPPPPPQAPPGQPAKGDDSGGASPSAPVQGAPKEVVDPSSGRATLLESIRQAGGIGKAKLRSVKERKLEKKKQKEQEQVRATSQGGDLMSDLFNKLAMRRKGISGKGPGSGASEGPGGAFARMSDSIPPLPPPQQPPGEEDEDDWES | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; exocytosis [GO:0006887]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147] | autophagosome [GO:0005776]; centriole [GO:0005814]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015] | PF11945; | null | WASH1 family | null | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome {ECO:0000250|UniProtKB:A8K0Z3}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2. {ECO:0000250|UniProtKB:A8K0Z3}. | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}. | Bos taurus (Bovine) |
A7Z064 | HMDH_BOVIN | MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKLEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLVDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADNSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQAETESTLSLKNPITSPVVTQKKITDDCCRRDPVLVRNDQKFHAMEEETRKNRERKVEVIKPLLAENDTSHRATFVVGNSSLLGTSLELETQEPEMELPVEPRPNEECLQILENAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLPEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRFPRACDSAEVKAWLETPEGFTVIKEAFDSTSRFARLQKLHMSVAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLQEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACRDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMIHNRSKINLQDLQGTCTKKAA | 1.1.1.34 | null | cholesterol biosynthetic process [GO:0006695]; coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADP binding [GO:0050661] | PF00368;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1 or INSIG2. The INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78, RNF139 or RNF145, initiating ubiquitination of the reductase. The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97. The INSIG2-binding leads to the recruitment of the ubiquitin ligase RNF139, initiating ubiquitination of the reductase. Lys-248 is the main site of ubiquitination. Ubiquitination is enhanced by the presence of a geranylgeranylated protein. {ECO:0000250|UniProtKB:P04035}.; PTM: N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner. {ECO:0000250|UniProtKB:P04035}.; PTM: Phosphorylated. Phosphorylation at Ser-872 reduces the catalytic activity. {ECO:0000250|UniProtKB:P00347}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000250|UniProtKB:P04035}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15991; Evidence={ECO:0000250|UniProtKB:P04035}; | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. {ECO:0000250|UniProtKB:P04035}. | Bos taurus (Bovine) |
A7ZN88 | HCHA_ECO24 | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 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]; zinc ion binding [GO:0008270] | null | 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}. | Escherichia coli O139:H28 (strain E24377A / ETEC) |
A8A1G6 | HCHA_ECOHS | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 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]; zinc ion binding [GO:0008270] | null | 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}. | Escherichia coli O9:H4 (strain HS) |
A8ACZ4 | FADB_CITK8 | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALDVLEKQTDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLSAINGYALGGGCECVLATDYRLVTPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDIGAEQALKIGLVDGVVKPEKLLDGAIAVLRQAIDGSLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMIAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQFVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLTLGMTEAAKLLNKQLERGRIDGLKLAGVISTIHPTLNYAGFDRVDVVVEAVVENPKVKKAVLAETEDNVRPDTVLASNTSTIPISELASALKRPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDASRYGQKNGLGFWRYKEDSKGKPKKEEDAAVDSLLAEVSQPKRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA | 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}. | Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) |
A8AWU7 | HSA_STRGC | MFFKRQKGQYHEVERVTRFKLIKSGKHWLRAATSQFGLLRLMKGADISSVEVKVAEEQSVEKGGLNYLKGIIATGAVLGGAVVTSSSVYAEEEQALEKVIDTRDVLATRGEAVLSEEAATTLSSEGANPVESLSDTLSASESASANSVSTSISISESFSVSASASLSSSSSLSQSSSESASASESLSVSASTSQSFSSTTSSTQSSNNESLISSDSSNSLNTNQSVSARNQNARVRTRRAVAANDTEAPQVKSGDYVVYRGESFEYYAEITDNSGQVNRVVIRNVEGGANSTYLSPNWVKYSTENLGRPGNATVQNPLRTRIFGEVPLNEIVNEKSYYTRYIVAWDPSGNATQMVDNANRNGLERFVLTVKSQNEKYDPADPSVTYVNNLSNLSTSEREAVAAAVRAANPNIPPTAKITVSQNGTVTITYPDKSTDTIPANRVVKDLQISKSNSASQSSSVSASQSASTSVSASISASMSASVSVSTSASTSASVSASESASTSASVSASESASTSASVSASKSSSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASISASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESSSTSASVSASESASTSSSVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASMSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESAYTSASASASESASTSASISASESASTSASVSASESAYTSASVSASESGSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSTSESASTSASVSASESASTSASVSASESASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSVSVSASESASTSASVSASESASSSASVSASKSASMSASVLASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSANESASTSASVSASTSASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASISASISASESSSTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVFASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASISASESASTSASISASESSSTSASVSASTSASTSASVSASESTSTSVSISASESVSISTSVSQSMSVSESLSLSVSTSTLHSQLNGIYESELNSLSLSESLSMSQSLSQSLSDSQSTSATQSMHDRISKGQLPRTGESESKASILALGIGALGLAFKKRKKNESED | null | null | biofilm matrix assembly [GO:0098785]; cell adhesion [GO:0007155]; surface biofilm formation [GO:0090604] | extracellular region [GO:0005576] | null | PF18938;PF00746;PF20164;PF19258; | 2.60.40.4140;3.10.20.890; | Serine-rich repeat protein (SRRP) family | PTM: The protein is glycosylated in vivo; constructs without SR1 and SR2 are not glycosylated. {ECO:0000269|PubMed:15213130, ECO:0000269|PubMed:27616700}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:15213130, ECO:0000269|PubMed:19884334}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | null | null | null | null | null | FUNCTION: A cell wall protein involved with PadA in host cell interactions required for colonization and pathogensis (Probable) (PubMed:19884334, PubMed:27616700). Mediates hemagglutination and adherence to ghst glycoproteins (PubMed:11854202). Recognizes fetuin-A (AHSG), a highly glycosylated human plasma protein, also involved in recognition of human platelets, probably via platelet glycoprotein Ib alpha (GP1BA) (PubMed:19884334). Acts in concert with PadA to promote binding to glycosylated human fibronectin (FN1) and vitronectin (VTN), and biofilm formation. Plays a major role in fibronectin and vitronectin binding; binding is mediated by glycosylated regions. Probably mediates interaction of PadA with resting platelets (PubMed:27616700). {ECO:0000269|PubMed:11854202, ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:27616700, ECO:0000305|PubMed:11854202}. | Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
A8AZP4 | PADA_STRGC | MKDFLKKVLILFTVLLMSMPSSVLNLGTSVVRADDPLNIETRRIDEHTTITQNGCYRKIEKTDATDWTVPRKPIDLVILQDASGSFRTTIPSVKNALKRLTTYVSPEQYDENDPHLVKTDDPRTTDRVFVASYQGLDQVRYFENNDFSGNPANVYTDANSTGKNYTYGNSGLTSDQNKVHNFIDNIAVDGGTPTVPAIDDTIAQYNRVKGNMENGRKTVFLLVTDGVANGYRLPGTNTVVMDKSWTRTDAIQKAWRVDSYPEAAQDIIGRANELKAAGNQLKAAVGSEGSVVVGFWERVDNFTEKYYQYGPAYLNGFGNTINIGDNRSVQAIFHDALQSMASPDKVVNGKNVSFYVNEQNNIDVFSQKILESVAAALVKDDITGEFDITEGYKVDAIRINGKKIVPKVTDPSKEIRGTITQTGNKVKISVPDSVFNPGKNSFDYDLSKEARAPETDEDSEVDPPENYVPEKEEITVPELTGKFKAGDFETRQIGGRNQTVEVQKLEYCYPSATKTVKDADASNDIGVIPDPLELTKKPSYSAQLSKKDEEFTYTVDYNFNNVPYEFEKNVMLTDPIDYRLEVVSHSAQGPDGQSWPTRVVTQQDAGGNSQSVVVADVPPQGKDYNYLIMKKAKLKMTVRLKEEYRKNQASKAYLAILQNNNGYGLVNQGNIMWNGEDDSPNQDAHAKTKDKASTIRRSNPIYVKPPLDTEVDKKVNEKEHEGLQADGEEFEYKVTAPWPGIADKFTLTDTVVDELEIVPNSAKVTVAGKSYNALTKAISINGQTIDITLDKAQLTSLNRLISRRGGSEVQEIELIFKAKIRPGADLSKYKKNGAVNIPNTADVILNDKKKTSKEVTVTPPKPKEPTVSKKINNTLDSLVTFDGQPYTYNITTAVPSDVAGYKKFVISDKLDADLEFDGQASISGPLADVFEIQTNGQTVTATVKEGKFKELAKYSFVELTIPAKVKAGVTGKTIENKAKISFTNENNVAKEVESNPVTVTPPPVTKKINENLDHLDIATGQPYKYNVKTTLPSDITSYKEFVITDTLEDELSVINEGTDKPVISGPAAEFFDVTVSGQKVTATMKNFAGASALAGQEIELVIPAKINDGVTRSNIPNKATFSFKDKNDHKGEKETIPVTVTPPTEPNVSKKINGDQDNATIAAETDFTYNIKTTLPNDIDTYKSFAITDTLDENLGVVNPEPSISEEAKKFFDITVSGNTVTATMKDFAKASALANKEIELVIHAKVKKESVLPEIPNTAKITYTNKNNESKEKETEPVKVTPPPITKKVNGKDQEDLASLTSTFKYTVDSKVPIVADKFVLSDTLEEVLTFDGDATVTIDGQTVTDVTVAKKDQKLTVTFDKDQVKKYAGKAVQVAFDAKIKSGYTVDQLVAKYPNGDKAAIPNKASFVVNDNPETEKFSNPVTVTPPPPNTPEIEKKVNGADSYNLQTRLEEFTYSLNTAMPTNATEFTVTDELKSVLEFAGKKGDVQVKIDGKAANDQATISTDKNTLTVAFAEKAVKANAGKSIEVTFKAKIREGANLLDYLVPGQGIRIPNKASYDIDHNPKFHKDSNEVPVTPPSPEQPPIEKDVNDKAEATLEARDEEFTYHVKTKIPYEATAFNITDTLKEVLDFSGEKGQAEATVDGKKLSDDHIAINGQTITVTLNQEELKANADKEIKLTFKAKIRPNANLAAYVVGDKVVINNQASYNVDLPDNPGVHKDSNIVPVTPPSPEKPEIEKTVNDAKEATLANRDEIFTYKVKTKVPFDATAFSIDDTIKDVLEFADAGSATLNGEALEADRISIADQKITLTLTEDQVKNNGGKEVVLTFKAKIRQGANLSGYIEKGKTVINNQASYNAAFPNDPNFHKDSNIVPVTPPNPENPPIEKKVNEAESANLGARDEEFTYTIDTTVPLDVTGFAVYDTIEKVLEFSGENGQASATVDGQPLDASHITIKGQKITVKLTEDEAKALGGKAVHVSFKAKIKAGANLSDYIEKDGTTRIYNTAKYNFNNDPGTEQSSKPVPVIPPTPTEPELKKEVNGKEAETLANRDDVFTYTVKTTVPQDATAFSISDSLVPVLEFAGEDAEASLTLNGEKLDAKQIKLKDQTISAELTEAQVKANGGKEVVLNFKAKIREGANLADYIEADGVTRVPNKASYVANFPHRPKVEKDSNIVPVTPPSPENPPVEKKVNNKPSATLDSRDEEFTYTIDTKVPVDATGFKITDELKDVLEFSGKKGQAEVTVDGDKDVIEDSQITVDKQVLTVTLTKDQVKKYGNKAVHVSFKAKIRKNVSLAGYIEADGVTRIPNIAKYIINDDPKTEKSTEPVPVIPPSPEEPGIKKEVNGQPEATLKERYEEFTYKVTTSVPQDATAFSVSDTLVPVLEFSGEKGQATATLDGQEIDANRINVADQTISMALTEDEVKANGGKEVTLTFKAKIREGANLSAYIEKGKTSIPNTASYTAGFPNRPEIHKDSNRVPVTPPTPEEPEIKKDVNGKEEETLANRNDEFTYHINTKVPFDATAFSINDELKDVLEFADGTGRATASLNGQALDADRISINGQTITVNLTEEQVKNNGGKDVNLTFTAKIRQGVNLSGYIKDGKTSIPNKASYRVDFPNNPGVTKDSNEVPVTPPSPENPPIEKKVNEAESANLGARDEEFTYTIDTTVPLDVTGFAVYDTIEKVLEFSGENGQASATVDGQPLDASHITIKGQKITVKLTEDEAKALGGKAVHVSFKAKIKAGANLSDYIEKDGTTRIYNTAKYNFNNDPGTEQSSKPVPVIPPTPTEPELKKEVNGKEAETLANRDDVFTYTVKTTVPQDATAFSISDKLEDVLEFAGESSATLAGEDLKADQITTDGQIIKLTLTEDQVKANGGKEVVLNFKAKIREGANLSAYMKADKAEVPNKASYTVGFPNKPAVTKDSNEVPVTPPSPEQPPIEKDVNSKPSETIADRTEEFTYNIHTTMPQDATGFTVTDELKDVLEFAGDVQVTLGGKKADAAVAKNGQTLEVTFPEETVKANGGKKVQVTFKAKIKADADLTPYETANSYSVPNTASYLINNNPTSKKETKPVTVEVPKQPGPEVTKKINRTLDHLDVDRDVPYMYNVNTQIPKDIRLYKEFTVTDTLEPVLEITGTPVAYVDGYATDAVETKVEGNTVTVTVKDFARISGYKEIQLYIPAKLKADSDLSAYENQTVPNKATIAFKDSNGKNGTKESNPVTVRPRDPEKPEEPKPNEPAKTVGPADGSNPSTAYRLKELKEGFRFDVTAKVPTDPVDESGNPIKDAQGRDVKTELNSFTVTDELEKVLKVDRVAVKVEENKVAEAIAKITAKIEKAESDLKELEGKETNGTFAKKLAEAEKKVEELTAQLAAAKEKAAAAPATPAPASDSDAGNATATPAPADNNAEVAALEESLKAAQAELEQLKADGAKAGNLATPEEQKVEQDKLNKNLEQLKESKEKLEKALEAFTTVNDKGEITDEALAKIAKVTVEGQKVTVEVTDKAVLEALKGSTFRVIIYSSIKDGADLSSYLNKENNETKIPNKATVTFNDKPKVTNTVNVYPPEPTTPPQTPPHTPPTTPGTPPPTTPDTPPAPKGDLPPAPTPEPEKPKNILPKTGTSATMVNEVIIGMILVLMGLLLRRKPKH | null | null | biofilm matrix assembly [GO:0098785]; cell adhesion [GO:0007155]; surface biofilm formation [GO:0090604] | extracellular region [GO:0005576] | null | null | 2.60.40.740;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:27616700}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | null | null | null | null | null | FUNCTION: A cell wall protein involved with Hsa in host cell interactions required for colonization and pathogenesis (PubMed:19884334, PubMed:21071690, PubMed:24136582, PubMed:27616700). Involved in recognition of platelets. Interacts with human platelet integrin receptor GPIIbIIIa (a complex of ITGA2B and ITGB3) (PubMed:19884334). Involved in platelet spreading, presumably by activation of outside-in signaling leading to platelet activation and then spreading. Spreading also involves GPIIbIIIa (PubMed:21071690). Binding to platelets under static conditions causes platelet dense granules to secrete ADP (similar to release induced by fibrinogen binding), has no effect on platelet alpha granule release. The N-terminal 656 aa residue fragment (called F2) also binds platelets, causes dense granule secretion and allows platelet spreading (PubMed:24136582). Acts in concert with Hsa to promote binding to human fibronectin (FN1) and vitronectin (VTN), and biofilm formation. F2 bind activated platelets more strongly than unactivated platelets. Binding to both FN1 and VTN is mediated at least in part by their glycosylation (PubMed:27616700). {ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:21071690, ECO:0000269|PubMed:24136582, ECO:0000269|PubMed:27616700}. | Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
A8B296 | IFT81_GIAIC | MQPPTSTDQLQTITDGLNLPPFERRMTLITLSEILHDPVRAMQLLADVAYQVRPHSLAEDSKAVPPPVKVNAANLEQVAAGITDFTVCLLNLNESRSMADKQAFVQELVLSDSANMRVLLSAILKDLAASRETIYVSKFKLPPVIPADYMVDPQIQTLLSQLREAQSRFTEALNQNRDVQKDQILQKMERLATDKTTFLTRRDKLFDRVKQAKALSVPKEAVRLASRRRVALSEIEELKTQINSQNEIRRAALNAAKAVVNSARGTPANILEASEAENKRLKQEIINLTAEITEKESLAHLIQSEPGQEAIELMENELETLRTDLVKYREMVSTVGSPDEEDNEQEKMSFLNQQITKIKTQRAQLENRLTNARRESAEVDAEVAKRCSSTDMASLMKDIDDMDSIPMLLFKNLLSKGRALKPLHKKAMDEQQLLRKENAIVSRTKDILAAIPNLSAEAPDELTDAGGLRPIGGGKQRVLGSIGGVGLNAKNLMEAKAVLAELDATLQQKKRDLAPRVSELAALKRQCAQLEADTESENQRARTLEVSREGSVYKLRLSVRALELEIDNLKTQAIVTDKKAELLRLELEQADNVREFDRLKREITSENNACKTQMMEIRAKQEELKCNLPNRMAQNKLFKSLVSILEFRKQAALERQEDHAAEMRMDKIRITN | null | null | intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992] | tubulin binding [GO:0015631] | PF18383; | 1.10.418.70; | IFT81 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips (PubMed:18463165, PubMed:31855176). Localizes to the basal bodies (PubMed:31855176). Main cytoplasmic localization in the posteriolateral axonemes (PubMed:18463165). In the examined anterior and posteriolateral flagella, higher levels are observed in the cytoplasmic portions of the axonemes compared to the membrane-bound portions, but lower levels compared to the flagellar pores (PubMed:31855176). Dynamic in the cytoplasmic axonemes and at flagellar pores, accumulating at the flagellar pores (PubMed:31855176). {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. | null | null | null | null | null | FUNCTION: Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable). {ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8B2U2 | ALF_GIAIC | MPLCTLRQMLGEARKHKYGVGAFNVNNMEQIQGIMKAVVQLKSPVILQCSRGALKYSDMIYLKKLCEAALEKHPDIPICIHLDHGDTLESVKMAIDLGFSSVMIDASHHPFDENVRITKEVVAYAHARGVSVEAELGTLGGIEEDVQNTVQLTEPQDAKKFVELTGVDALAVAIGTSHGAYKFKSESDIRLAIDRVKTISDLTGIPLVMHGSSSVPKDVKDMINKYGGKMPDAVGVPIESIVHAIGEGVCKINVDSDSRMAMTGAIRKVFVEHPEKFDPRDYLGPGRDAITEMLIPKIKAFGSAGHAGDYKVVSLEEAKAWYK | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17166851}; Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; tagatose-bisphosphate aldolase activity [GO:0009025]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622, ECO:0000269|PubMed:31409864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Evidence={ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622, ECO:0000269|PubMed:31409864}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 uM for fructose 1,6-bisphosphate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:17166851}; KM=1.8 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:31409864}; Note=kcat is 3.55 sec(-1) with fructose 1,6-bisphosphate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:17166851). kcat is 4.3 sec(-1) with fructose 1,6-bisphosphate as substrate (PubMed:31409864). {ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:31409864}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000305|PubMed:17166851}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17166851}; | null | FUNCTION: Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:17166851). Does not cleave D-tagatose-1,6-bisphosphate (PubMed:17166851, PubMed:19236002). {ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BB91 | KIN2B_GIAIC | MSKSKGKGSSDNVMVMVRVRPFNKREEQEGATEIIEMDKTLCTVTLHKPVEKGAGSATSECLPSKKVFTYDAVYPSNSTQVEVFDESVREMIDGCLEGYNATVFAYGQTGSGKTHTMMGQKDNPGMIPLAFQRIFDFIAQAKDDQFLVRASFVEIYNEDLKDLLTGATHLQLKEDPVKGVFIKDLSEHPVSDERHIDKLIQKGNESRAVAATLMNATSSRSHSIFQVVLERMTVIDGRECIRVGKLNLVDLAGSERQEKTGATGDRLKEAAKINLSLTTLGCVISKLVEGSKHIPYRDSKLTRLLQDSLGGNSKTLMVVAVSPASTNYDETMSTLRYADRAKQIKNKPRINEDPKDAQIREMRNYVTKLEAQLAEIMQQANAGSGSEVEDKEAYDGEGNMGAGFTGYTADEMANVQSLRKNLDKTKKKRVKYVEQRKENEEAVSAEELATLEEEQKKLEEQIKESERKAKERQLMAKKIAALIEANKSKMVDKKVLENEERLKDAAIREARNALVAQKKEAERLKKELIEAEQQRKQLEEQCTTALDQAQQLELRLNEYKEQLAERREELHNVEADQAKEREIIRNDYADQIKLCELRQFIVSMFVPEEYQRSIESIASWDEDNQAWHFRTQKSHRGMAGFG | null | null | cytoskeleton-dependent intracellular transport [GO:0030705]; intraciliary anterograde transport [GO:0035720]; intraciliary transport involved in cilium assembly [GO:0035735]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]; transport along microtubule [GO:0010970] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips (PubMed:18463165, PubMed:31855176). Localizes at a lower level to the cytoplasmic axonemes and to the basal bodies (PubMed:31855176). {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. | null | null | null | null | null | FUNCTION: Involved in anterograde intraflagellar transport (IFT) (Probable). Involved in flagellar assembly (Probable). {ECO:0000305|PubMed:19377039, ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BKD1 | KIN2A_GIAIC | MSSDNIKVIVRCRPLNARETRENALNIIRMDEASAQVIVDPPEQEKSATQAKKVPRTFTFDAVYDQTSCNYGIFQASFKPLIDAVLEGFNSTIFAYGQTGAGKTWTMGGNKEEPGAIPNSFKHLFDAINSSSSNQNFLVIGSYLELYNEEIRDLIKNNTKLPLKEDKTRGIYVDGLSMHRVTTAAELSALMDKGFANRHVAATQMNDTSSRSHSIFMVRIECSEVIENKEVIRVGKLNLVDLAGSERQSKTGATGETLVEGAKINLSLSALGLVISKLVEGATHIPYRDSKLTRLLQDSLGGNSKTLMCANISPASTNYDETMSTLRYADRAKQIKNKPRINEDPKDAQIRQLRDHIARLEAQLAEAQANGAKPMDVLRIGKSLMKAINGDELNLDGTFQGTAGAKLSEARDGDSEGESTEEEIVFVEDEASRKAADELEAKRRALAEAKQKRESELEQKEALNKEAIVTLTDLKSQLSAIKNSVFVVKQLEIKDKVLGKAQQKLTTRQEKHNALQQALQNKQTEHQTKTAEILSAVEKLERLKADISKTEAEINEVNQEIDDITEQHALSIEEERRELKEVDKRSALLDAIIQTFIPQCEVAKAEALAEYDEETMKWAISPEKVDREHQMLLKRVRHMQILYPSGSTKPVFFGKGKDTRALVNFSQLSGNILELEPELPERMTVGEEMDGYQSYGMNEDEMHDTQLQMFYSQIDTYE | null | null | cilium assembly [GO:0060271]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips (PubMed:18463165, PubMed:31855176). Localizes at a lower level to the cytoplasmic axonemes and to the basal bodies (PubMed:31855176). {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. | null | null | null | null | null | FUNCTION: Involved in anterograde intraflagellar transport (IFT) (Probable). Involved in flagellar assembly (PubMed:18463165). {ECO:0000269|PubMed:18463165, ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BPK8 | PLK_GIAIC | MSHSNAPELHPQIVDPFHNVTYRPGKLLGKGGFAYVYEFHDVNSDSSYACKITPRSALQKKKYYDKFVTEVTIHRGLVHPNICRVLNVFKDQMNYYIILEKCNGGTLTDLIRRRKHLTETEARFFSKRILNALWYLHDLYIIHRDIKTSNIFLMEDFDVKVGDFGLAVKCETPEELHWTMCGTPNFLPSEVIYSHIMKRKASGRGPDPNLDEDCVNLCHQLLPAYSGQGHSFSADMWSFGCLVFSMIYGRPPFEAADIKTTYKRIVRCDFSFPGSISVSEDLKNFIKGLLTPDPRKRFTVKECLDHSWLNPSKYFIPESLPPRIISEPYEVPPLCSASPTRNMQMTINMAKNAGGTDGRFIAATPQAIGGTEHIPTPGTANFYKPQNAILTTKSAAGISRASTAMAMQNVGSAQGVVNKYGINEAEYPQIDPPCYIMSWVDYSNRYGFAYQISNGSIGVIFNDESAAILSPNALIVDYSPSLLDAAFDRALFEEGTTILSEKKFKLLSFFRDYLENRSIVPIPAADRPKEDEELKRVIEQERMNNQEIDFKRLTKGLPLPQLFLKKWKLYDDGTLCLLFNTKVFQVNFADHSKVVVAHRSVTFMSEKREIYTYPSEYLKDDRFSFKELRRRVDRARKYYEIIKAARPVDSLAQYRYNKDSTKKSASGSSTRQLGQGGE | 2.7.11.21 | null | cell division [GO:0051301]; mitotic spindle organization [GO:0007052]; negative regulation of cilium assembly [GO:1902018]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; membrane [GO:0016020]; motile cilium [GO:0031514]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00659; | 3.30.1120.30;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Autophosphorylated (PubMed:33789729, PubMed:35772734). Autophosphorylation is critical for its function in cell growth, cytokinesis and formation of flagella (PubMed:33789729). {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:33789729}. Membrane {ECO:0000269|PubMed:33789729}. Note=Found in both the membrane and the cytoplasmic fractions in interphase, G1/S and G2/M phases of the cell cycle (PubMed:33789729). Localizes to basal bodies, flagella, axonemes, adhesive disk and median bodies of trophozoites in interphase (PubMed:33789729). Remains localization at the basal bodies in metaphase, anaphase, telophase and cytokinesis (PubMed:33789729). Localizes also to mitotic spindles and axonemes in anaphase (PubMed:33789729). Colocalizes with microtubules (MTs) in the basal bodies, flagella, axonemes and median bodies in interphase and anaphase (PubMed:33789729). Colocalizes with MTs in the mitotic spindles present between two separated groups of basal bodies in anaphase (PubMed:33789729). Colocalizes with centrin in interphase as well as during cell division (PubMed:33789729). Phosphorylated form localizes to basal bodies and distinctly to the cytoplasmic portion of anterior flagella, median bodies, and flagella tips in interphase cells (PubMed:33789729, PubMed:35772734). Phosphorylated form localizes to basal bodies and mitotic spindles in dividing cells (PubMed:33789729). {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. | 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=2.7.11.21; 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=2.7.11.21; Evidence={ECO:0000255|RuleBase:RU361162, ECO:0000269|PubMed:33789729}; | null | null | null | null | FUNCTION: Involved in cell cycle (PubMed:33789729, PubMed:35772734). Involved in cell division (PubMed:33789729). Involved in cytokinesis (PubMed:33789729). Involved in flagella biogenesis and in regulation of flagella length in interphase (PubMed:33789729, PubMed:35772734). Involved in formation of median bodies during interphase (PubMed:35772734). Phosphorylates Kin-13 in vitro (PubMed:35772734). Likely regulates microtubule (MT) depolymerizing activity of Kin-13 (PubMed:35772734). {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8C927 | NPMA_ECOLX | MLILKGTKTVDLSKDELTEIIGQFDRVHIDLGTGDGRNIYKLAINDQNTFYIGIDPVKENLFDISKKIIKKPSKGGLSNVVFVIAAAESLPFELKNIADSISILFPWGTLLEYVIKPNRDILSNVADLAKKEAHFEFVTTYSDSYEEAEIKKRGLPLLSKAYFLSEQYKAELSNSGFRIDDVKELDNEYVKQFNSLWAKRLAFGRKRSFFRVSGHVSKH | 2.1.1.180 | null | methylation [GO:0032259]; response to antibiotic [GO:0046677] | null | methyltransferase activity [GO:0008168] | null | 3.40.50.150; | Methyltransferase superfamily, Kanamycin-apramycin resistance family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine(1408) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(1408) in 16S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42776, Rhea:RHEA-COMP:10227, Rhea:RHEA-COMP:10228, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.180; Evidence={ECO:0000269|PubMed:17875999}; | null | null | null | null | FUNCTION: Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin, apramycin, ribostamycin and gentamicin. Methylates only fully assembled 30S subunits. {ECO:0000269|PubMed:17875999, ECO:0000269|PubMed:20667473, ECO:0000269|PubMed:21062819}. | Escherichia coli |
A8C984 | MYLK3_DANRE | MGTSLYRSTLLSTGGFSVSDYIRKFTKNKPDVNNIQPNVGFCHQSTQTSQQVKEVISAELELQQPEVTLPNDPSSQHSPEAHTGASEPLKPVSAGESSKALQKAKEISVKSSEPTHVQTFAPAVHLEQIDVHNVPKQETNSLVAAPADAKCVIETMTKVEKDIALQQERALERADDSHVANKVFLKSIIPGQQLEKIEDPQQQAEVSLFVDEDSLEKSVPGQHLDKKMEVLQKQAKDLPVVDEDSLNLSAPGQRQLEEKVDVPEKAEKKIDEAHKKMEEVPRKDELCIEKPVIRHAGIKTQHEETMGMETTVPKHDESKCPTETYVEKTENKNADVTLESDKIMICAVSPQNTSLDEDEKSKAAPLRKVESTLLIIDDSPPLPAPFDHRIVSAKQVPINSYYAVNPVEVLGGGRFGQVHKCAELSSGLTLAAKIIKVRGMKERDEVKNEIGVMNQLNHVNLIQLYDAFESRTNLTLIMEYVEGGELFERIIDESYQLTELDAIVFTRQICEGVQYLHQQYILHLDLKPENILCVNSTGNQIKIIDFGLARKYRPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFMGDNDAETMNNILHAKWEFDTEAFENVSEEAKDFISSLLVSAKCSRLSASGCMKHSWLNNLEDKAKMYKVRLKSQMMLQRYLVAHRQWKKHFYAVAAANRLKRFQQSRSISTPN | 2.7.11.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | heart morphogenesis [GO:0003007]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; sarcomerogenesis [GO:0048769]; ventricular cardiac myofibril assembly [GO:0055005] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; myosin light chain kinase activity [GO:0004687] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900, Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.18; | null | null | null | null | FUNCTION: Kinase that phosphorylates MYL2 in vitro (By similarity). Increases cardiomyocyte contractility (By similarity). Required for sarcomere formation in the developing heart. {ECO:0000250, ECO:0000269|PubMed:17885681}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8CG34 | P121C_HUMAN | MSPAAAAAGAGERRRPIASVRDGRGRGCGGPAGAALLGLSLVGLLLYLVPAAAALAWLAVGTTAAWWGLSREPRGSRPLSSFVQKARHRRTLFASPPAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAPAPEGQDLRNRPGRRPPARPAPRSTPPSQPTHRVHHFYPSLPTPLLRPSGRPSPRDRGTLPDRFVITPRRRYPIHQTQYSCPGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVASGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGAYTSGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADKESQGEKAADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPTTQPSFTFTLPAAATASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLSQSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSASPMFKPIFTAPPKSEKEGLTPPGPSVSATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTVTTFSQSLPTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAEGQPPGAAKPALTPSFGSSFTFGNSAAPAPATAPTPAPASTIKIVPAHVPTPIQPTFGGATHSAFGLKATASAFGAPASSQPAFGGSTAVFSFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSATTGAFSFGAGQSGSTATSTPFTGGLGQNALGTTGQSTPFAFNVGSTTESKPVFGGTATPTFGQNTPAPGVGTSGSSLSFGASSAPAQGFVGVGPFGSAAPSFSIGAGSKTPGARQRLQARRQHTRKK | null | null | mRNA transport [GO:0051028]; protein import into nucleus [GO:0006606]; RNA export from nucleus [GO:0006405] | endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654] | nuclear localization sequence binding [GO:0008139]; structural constituent of nuclear pore [GO:0017056] | PF15229; | null | POM121 family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}. | Homo sapiens (Human) |
A8CG78 | PA2A2_DABSI | MRTLWIVAVCLIGVEGNLYQFGEMINQKTGNFGLLSYVYYGCYCGWGGKGKPQDATDRCCFVHDCCYGRVKGCDPKTATYSYSFENGDIVCGGDDPCLRAVCECDRVAAICFRENMNTYDKKYMLYSIFDCKEESDQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | null | null | null | null | FUNCTION: Exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17611171}. | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
A8CG82 | PA2B1_DABSI | MRTLWIVAMCLIGVEGNLFQFARLIDAKQEAFSFFKYISYGCYCGWGGQGTPKDATDRCCFVHDCCYARVKGCNPKLVEYSYGYRTGKIVCENYNRCKRAVCECDRVAAICLGQNVNTYNKGYMFLSSYYCRQKSEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17611171}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | null | null | null | null | FUNCTION: Exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17611171}. | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
A8CG86 | PA2A1_DABRR | MRTLWIVAVCLIGVEGNLFQFAEMIVKMTGKEAVHSYAIYGCYCGWGGQGKPQDATDRCCFVHDCCYGTVNDCNPKMATYSYSFENGDIVCGDNNLCLKTVCECDRAAAICLGQNVNTYDKNYENYAISHCTEESEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17611171}. | Daboia russelii (Russel's viper) (Vipera russelii) |
A8CL69 | PBAN_APIME | MIGFAVFSSFNRFTTIFVCVLLCVVYLLSYASGEYDGRDSSSGSNNDRAPSNEFGSCTDGKCIKRTSQDITSGMWFGPRLGRRRRADRKPEINSDIEAFANAFEEPHWAIVTIPETEKRQITQFTPRLGRESGEDYFSYGFPKDQEELYTEEQIYLPLFASRLGRRVPWTPSPRLGRQLHNIVDKPRQNFNDPRF | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular space [GO:0005615] | myostimulatory hormone activity [GO:0016084]; neuropeptide hormone activity [GO:0005184] | null | null | Pyrokinin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17068263}. | null | null | null | null | null | FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity). {ECO:0000250|UniProtKB:P09971, ECO:0000269|PubMed:17068263}. | Apis mellifera (Honeybee) |
A8CVX7 | TTLL6_DANRE | MGTPAERSVSEVCRCEPDPGLEGEGWGSDTHAEPSNTPIPLPVANKKKKRKKKLWINLTNCKYESVRRAARRYGIREAAEGEDWTLYWTDCSVSLDRVMDMKRYQKINHFPGMNEICRKDLLARNMNRMLKLFPKEYNIFPRTWCLPADYSDFQAYTRAKKHKTFICKPDSGCQGRGIYLTKSSKDIRPGEHMICQVYMSKPFIIDGFKFDLRIYVLVTSCDPFRVFMYDEGLVRFCTTHYTEPTVSNLEDVCMHLTNYAINKHSENFVRDEDTGSKRKLSSFKKHMEDMSYDTEKLWTDIEDAIIKTLISAHPILKHNYQTCFPNHASGSACFEILGFDVLLDRRLKPWLLEVNHSPSFTTDSRLDREVKDSLLYDTLVLINLGACDRRKITEEEKRRVKERLQQNRSREARNEEPRQSQAASMELMQKYEAKHMGGFRRIFPRDGGEKYEKYFQHSSSLFQETAASKAREECARQQLQELRLKQEQKERDKKGSRKQDLQGESAGEKVKPRKSQPPHKTSNSLPAMLELSSVREETPVSLERIEKEEAERVRELQQRETLLLNMGVVNQVRQLLQSANRLTQCINHSHEQASFPPHCRHDHKLDTLAEISWRQKNIYSTMQHQILARNRPSLPNVHSQTLQNRKPWPSLEHGLLQPVQTQAAALKHYGLEEMVASNAEEQANLIKATSAQQIPLTINGSFIWRQGSLSSSLAESRARATMLAMPPLGPGRLHRPTIFHDPNSLSIISTPAPLVPRPHLSHDLRKAPRRVLPHEHSL | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | axoneme assembly [GO:0035082]; cilium movement [GO:0003341]; microtubule cytoskeleton organization [GO:0000226]; protein polyglutamylation [GO:0018095]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glutamic acid ligase activity [GO:0070739]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=CEP41 is required for its transport between the basal body and the cilium axoneme. {ECO:0000269|PubMed:22246503}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; 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:A4Q9E8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | null | null | null | null | FUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (By similarity). Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction (By similarity). Preferentially modifies the alpha-tubulin tail over a beta-tail (By similarity). Mediates microtubule polyglutamylation in cilia axoneme, which is important for ciliary structural formation and motility (PubMed:17761526, PubMed:22246503). Polyglutamylates olfactory cilia, necessary for the regulation of ciliary sructure and beating (PubMed:17761526). {ECO:0000250|UniProtKB:A4Q9E8, ECO:0000269|PubMed:17761526, ECO:0000269|PubMed:22246503}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8D8P8 | SIWI_BOMMO | MSEPRGRGRARGRAGRGGDGGGPAPRRPGEQAGPSQQSMPPGPRPQPPSGWGPQSSVPPVRAGVPTPTAQAGRASHRVTPTTHEHPGDIDVQQRMQKLELGPHSSGGGDASSVVGRGSRRGGGRVLPETISILRTRPEAVTSKKGTSGTPLDLLANYFTVETTPKWGLYQYHVDISPEEDSTGVRKALMRVHSKTLGGYLFDGTVLYTVNRLHPDPMELYSDRKTDNERMRILIKLTCEVSPGDYHYIQIFNIIIRKCFNLLKLQLMGRDYFDPEAKIDIPEFKLQIWPGYKTTINQYEDRLLLVTEIAHKVLRMDTVLQMLSEYAATKGNNYKKIFLEDVVGKIVMTDYNKRTYRVDDVAWNVSPKSTFKMRDENITYIEYYYKKYNLRIQDPGQPLLISRSKPREIRAGLPELIYLVPELCRQTGLSDEMRANFKLMRSLDVHTKIGPDKRIEKLNNFNRRFTSTPEVVEELATWSLKLSKELVKIKGRQLPPENIIQANNVKYPAGDTTEGWTRDMRSKHLLAIAQLNSWVVITPERQRRDTESFIDLIIKTGGGVGFRMRSPDLVVIRHDGPIEYANMCEEVIARKNPALILCVLARNYADRYEAIKKKCTVDRAVPTQVVCARNMSSKSAMSIATKVAIQINCKLGGSPWTVDIPLPSLMVVGYDVCHDTRSKEKSFGAFVATLDKQMTQYYSIVNAHTSGEELSSHMGFNIASAVKKFREKNGTYPARIFIYRDGVGDGQIPYVHSHEVAEIKKKLAEIYAGVEIKLAFIIVSKRINTRIFVQRGRSGENPRPGTVIDDVVTLPERYDFYLVSQNVREGTIAPTSYNVIEDTTGLNPDRIQRLTYKLTHLYFNCSSQVRVPSVCQYAHKLAFLAANSLHNQPHYSLNETLYFL | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27693359}; | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; piRNA processing [GO:0034587]; spermatogenesis [GO:0007283] | P granule [GO:0043186]; PET complex [GO:1990923] | magnesium ion binding [GO:0000287]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Arginine methylation is required for the interaction with Tudor domain-containing protein Papi/TDRKH (PubMed:23970546, PubMed:26919431). {ECO:0000269|PubMed:23970546, ECO:0000269|PubMed:26919431}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25558067}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:25558067). {ECO:0000269|PubMed:25558067}. | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:19460866, PubMed:27693359). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells (PubMed:19460866, PubMed:25558067, PubMed:27693359). Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females (PubMed:18191035). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:19460866, PubMed:25558067, PubMed:27693359). Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:19460866, PubMed:25558067, PubMed:27693359). Recognizes piRNAs containing a phosphate at the 5'-end and a 2'-O-methylation modification at the 3'-end (PubMed:27693359). Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias) and a complementary adenosine in the target (t1A bias) (PubMed:24757166, PubMed:27693359). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle: antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally cleave complementary transcripts, to couple the amplification of piRNAs with the repression of transposable elements. In this process Siwi acts as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto Ago3 (PubMed:27693359). In this process, Siwi requires the RNA unwinding activity of the RNA helicase Vasa for the release of the cleavage products (PubMed:25558067). {ECO:0000269|PubMed:18191035, ECO:0000269|PubMed:19460866, ECO:0000269|PubMed:24757166, ECO:0000269|PubMed:25558067, ECO:0000269|PubMed:27693359}. | Bombyx mori (Silk moth) |
A8DS38 | ERVC2_TABDI | MSTLFIISILLFLASFSYAMDISTIEYKYDKSSAWRTDEEVKEIYELWLAKHDKVYSGLVEYEKRFEIFKDNLKFIDEHNSENHTYKMGLTPYTDLTNEEFQAIYLGTRSDTIHRLKRTINISERYAYEAGDNLPEQIDWRKKGAVTPVKNQGKCGSCWAFSTVSTVESINQIRTGNLISLSEQQLVDCNKKNHGCKGGAFVYAYQYIIDNGGIDTEANYPYKAVQGPCRAAKKVVRIDGYKGVPHCNENALKKAVASQPSVVAIDASSKQFQHYKSGIFSGPCGTKLNHGVVIVGYWKDYWIVRNSWGRYWGEQGYIRMKRVGGCGLCGIARLPYYPTKAAGDENSKLETPELLQWSEEAFPLA | 3.4.22.- | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83654}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.063 mM for N-benzoyl-Phe-Val-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.548 mM for D-Val-Leu-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=1.475 mM for D-Ile-Phe-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=0.355 mM for Ala-Ala-Val-Ala-pNA {ECO:0000269|PubMed:18167146}; KM=0.716 mM for D-Ile-Pro-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.776 mM for N(a)-benzoyl-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=1.683 mM for D-Leu-Ser-Thr-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=225 mM for E64 {ECO:0000269|PubMed:18167146}; Note=kcat is 9.312 sec(-1) with N-benzoyl-Phe-Val-Arg-pNA as substrate (PubMed:18167146). kcat is 0.385 sec(-1) with D-Val-Leu-Lys-pNA as substrate (PubMed:18167146). kcat is 0.264 sec(-1) with D-Ile-Phe-Lys-pNA as substrate (PubMed:18167146). kcat is 0.192 sec(-1) with Ala-Ala-Val-Ala-pNA as substrate (PubMed:18167146). kcat is 0.015 sec(-1) with D-Ile-Pro-Arg-pNA as substrate (PubMed:18167146). kcat is 0.007 sec(-1) with N(a)-benzoyl-Arg-pNA as substrate (PubMed:18167146). kcat is 0.037 sec(-1) with D-Leu-Ser-Thr-Arg-pNA as substrate (PubMed:18167146). {ECO:0000269|PubMed:18167146}; | null | null | null | FUNCTION: Cysteine proteinase (PubMed:18167146). Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (By similarity). Has little or no activity against synthetic substrates (By similarity). {ECO:0000250|UniProtKB:P83654, ECO:0000269|PubMed:18167146}. | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
A8DYE2 | TRPCG_DROME | MVVTDSPLAPHKYVRRISKDFSTVRRYSNTPAVVVGSFRASTSAFIAAESAAHLPTCSSPTTRTPVSTPRGIRRRQRMRKRSSVSSTLSKVLILNVRDLLKAHAGSEPLKEHQPRSWIETNFQKRECIKFIPCPKDDTKCCCGQAQITHQTIPGIESGSPGDLWLPTKHTRPQPTDAYGTIEFQGGAHPTKAQYVRLSFDTRPELLVQLFTKEWNLELPKLLITVQGGKANFDLQAKLKKEIRKGLLKAAKTTGAWIFTGGTNTGVTKQVGDALLLEGQQRTGRVVSIGIAPWGIVERNHELLGHNREVPCHSISSPRSKLAVLNNRHAYFLLVDNGTQAKYGAELILRRKLEKFISNLKLHPFTHSSTPVVCLVIEGGTNTIRAVLEYVTDSPPVPVVVCDGSGRAADLLAFVHKYASDGEEQPVLESMRDYLIGTIQKTFEVGLDQSEKLYQELLQCTRNKNLITVFRIQEKPEGEAQELDQTILTALFKSQHLSPPEQLSLALTWNRVDIARSEIFVYGQEWPNGALDEAMMQALEHDRIDFVKLLLENGVSMKKFLTIPRLEELYNTKHGPANTLGYILRDVRPHIPKGYIYTLHDIGLVINKLMGGAYRSYYTRRKFRPIYAKVMNSYANACRKSSTYQYQRYAGANSLSLVTGLLPFTSEMALFEFPFNELLIWAVLTKRQQMALLMWTHGEEALAKSLVSCKLYKAMAHEAAEDDLDTEIYEELRSYAKEFESKGNKLLDFSYRQDAEKAQRLLTCELHSWSNQSCLSLAVAANHRALLAHPCSQVILADLWMGGLRTRKNTNFKVILGLAMPFYIRQLDFKSKEELQQMPQTEEEHLENQNLDNDDSDRSQPDAEALLADTYSVRDTKVHENGKVSLTDSDTAQFREFFNLSEYNEVKQHQPLRLKKKFYEFYTAPITKFWADSIAYMFFLIMFSFTVLVKMEQMPRWQEWYSIAYITTLGFEKVREIISSEPVAITHKFSVWAWNMWNPCDGAAIILFVIGLAFRFRENTMDIGRVIYCVDSIYWYLRILNILGVNKYLGPLVTMMGKMVKNMIYFVVLLAVVLMSFGVSRQAILYPNKQPTWSLIKEVTFQPYFMLYGEVFAGDIDPPCGEDPSQPGCVTGHWVTPITMSMYLLIANILLINLLIAVFNNIFNEVNSVSHQVWMFQRFTVVMEYQQKPVLPPPFIALCHFYSLLKYCVRKAKGLEVQRDNGLKLFLEKDDLERLYDFEEECVEGFFHEQEIILNQSTDERVKNTTERVETMSQKIEDINQKENIQTATVQNIEFRLRKMEESSEQILSHLAVIHRFMSTHTAGADDLRGSTINIPGEMQRMRTISISDTEGGSGPGGNGGGGGGGGAIVPLGLGAGLNLNSLQVTTRRRFNRSLTEVRPDAYIFDEGTHFEVVPLPEEPDEVVKSREALNEQVVRKASMQSEADSDIYIPVSQRPSTCETVKRTPYVTVRQDTGASTESKDTLTPMGNNDDDQTLVGGDNSDDATPDINFEAARHRALRQRTVSLCRRNSETYSLTGADINRSHISLNQLASLSRRQMSLTQSEPDSDKDAPIAQGSAHPGKSVLHAKPSRNILLKLHSEYTSITDELESVCHMIASPTVSLPSNKASLDRPKTEMSRAEAAALLEKKHLKECEENDYMILEGLIESRGSIDASAQGFEIGVSIDYSHRYPLRRETAVELSPSKPSVDGDLMGGGEGGGAGGGDSSDTSGAGSCGAMVGISSGFQLKNERPWQRNSSMEQQTYPSPLVPTRATSDFLNPPYEGRLFKKSSESLQKNSSTETDYSAHPYRFIKQSSNETNTSLTGSYNVDTPSLTAEPSLDAGDSHSATGISISVGAVGGTATARYQPIRTASVGAADGRRLREESSSSLDLSSSGPVTMQAAPAPPVRPMLLKKQFSVDQGKPSQTAAEAVPQTPEAAQAGQAKLISTLKPQPFASKLGMNVLKESSSSTDESVGSSAKSSNPALSIPQISTHLVQDEIAKLSSNIKSSTESEKDPPFNETMC | null | null | intracellular zinc ion homeostasis [GO:0006882]; magnesium ion homeostasis [GO:0010960]; metal ion transport [GO:0030001]; monoatomic cation transmembrane transport [GO:0098655]; protein tetramerization [GO:0051262] | cation channel complex [GO:0034703] | inorganic cation transmembrane transporter activity [GO:0022890]; intracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity [GO:0097682]; monoatomic cation channel activity [GO:0005261]; zinc ion transmembrane transporter activity [GO:0005385] | PF00520;PF18139;PF16519; | 1.20.5.1010; | Transient receptor (TC 1.A.4) family, LTrpC subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Calcium channel mediating constitutive calcium ion entry. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
A8DYP0 | OBSCN_DROME | MDAVADIVFVSRDYQAQSLATDEISVSRGDLVELISSKASEKSRCFVRMFDSGDSPKEGWVPIDILEFNPTMSSSNGKESGDAEFRKLTILRELVETEEEFSRDLLHVVEKYIKGIDKPVVPRSVRDNKDIIFCNFLQIAEFHNNVLKEGLKCYSNQPNMVAKTFLRLERDFDKHVVYCQNEPLAQDYLGSSPDAKKYFQELSKQLGDDKSLAEHLKLPIQRINDYQLLFKDFIKYSLSLKENVKDLERALELMLSVPSRAYDNRFLSSIEGCRGNIYKLGRLLLHAWCNVVDKEGKAHDRYCFLFKSRILVTKVRKISENRSVFILQNIVKLPLCNIELKADEKQIHLSLKAPEANSFLPIDIKPHGPEAHLTWFNEISSHINQDVTLQEHNADDLKVDASQIASESELILHLPQRAEAHDPNLSVRPSDVAENYFLSKETKERLQHEQQELLKLEQEAIELYKKQQSSKSVSSKTESVEITSSQVKSSSEVRKVVSPPPPPQAQVKEVTPVKVVSSPPPPKEITPAKVATPPPQPQVVTSPVKEVAPPPQPRAVASPAKEVTPSQSEPVKAPSPIKEVRKEVPPSASHSKEVEALVATEIRESLTETRSTVVESGQSSEIREEIVVTEESSLEGKQVVALEREPSPCSIPKIQVYRPVECENPVVTKHKPIELKDIVGYSESLRDGDTAPAGGSPGRQQGYSANITDHASLTIWNNRLANIAGDRSGANQHLQQSGPPPPPIPPNFTRMPGFFQPLPLIAYETTIEILIVKARPPSPPPPPPPTIKRVLVHTESLEQKTQNFFEGIYDAASSDTSLRNAKQKIRSIKSTVLKSKDSTNYAQDTVQKAKARDFLHIFTPPVKKRPIYEIVEEPVNIFELEGDYTESIADDFREPSADFEARGQSVGGMDDYYSGYSRASTRRYETKTRDYDRGTSYDSTVERSQYGISSRRDRSSVDKVEARSSLLATGRTESRAASRAESRAESRASYSVAESRAGIRSSSRLQEDRPLRSVDKPVVVKMLKSVQVEPGETAHFEIQFKDQPGLVTWLKDNKPLEDRLADRITQTAAPMNSYRLDIKNCSETDAGTYTIRAQSASETTTVSAQLAVGQAPGHDETKTNTEPAFLVSLKDAEMIENTLFRFMVKIIGDPKPRVKFYKDEKEILETNDRIQIIRDKDYLGFYELVIADVQKTDAGTYSCKATNKHGEANCEAIATTVEDKNPFGALSGQILPAGEKPVFQWKRNGEEFDPEERFKVLFGEDEDSLALVFQHVKPEDAGIYTCVAQTSTGNISCSAELSVQGAIQTLNREPEKPTLVIEHREANASIGGSAILELQCKGFPKPAVQWKHDGEVIQVDDRHKFMYEDEESMSLVIKNVDTVDAGVYTIEAINELGQDESSINLVVKAPPKIKKITDITCSAGETIKMEIEVEGFPQPTVQVTNNGKDVTAESNVKISSSSIGKSLEKVVVEVKEIKLSQAGNYSIKATNDLSQTSEYWSCTVKSKPVIVKNFESEYIHGEKENVQMTVRIDAYPEAKLTWYHDETEIKITDSKYTVSSDGNAYTLKITGATRVDAGKYTVKATNEHGSATSSTQLLIKCAPEFTHKLKNITVAEGDSNVELVVGVDAYPRPHAKWYIDGIEIDEKRNDFRHVEEGNDFKLIMNQVATNMQGNYTCKIMNDYGKLEDNCVVTVNCKPKVKRGLKNVEVQEGKSFTLEVEVYSEPEAKIKWFKDGHEIYEDARIKISRDTQRIENYYLTLNLARTEDAGTYEMKATNFIGETTSTCKVAVLTSEALSLEQTVTKTLIATTEEPEEGAVPEIVHVDVFQQHSYESVPLKYEVIATGIPKPEAIWYHDGKPITPDKHTAITVDGDHYKLEVQSLDLVDAGEYKVVVQNKVGEKSHQGELSLSGIAEYRKPILTQGPGLKDIKVNKGDKVCEPVVFTADPAPEIVLLKDGQPVVETNNVKLKVDKKDAENGLVQYTCTLNILEAEIKDSGRYELKVKNKYGELVTSGWIDVLAKPEISGLNDTKCLPGDTICFEALVQANPKPKVSWTRGNENLCNHENCEVIADVDADKYRLVFQSVSPCEDGKYTITATNSEGRAAVDFNLAVLVEKPTFIVQPESQSIHDYRPVSTKVLVHGVPLPTIEWFKDDKPINYEAINKPGKDKLYAKEDTKKGTDQIESVLDIKSFRENDVGAYTCVATNEIGVTKAPFKLAMLSLAPSFVKKLDNALDVLQGEPLVLECCVDGSPLPTVQWLKDGDEVKPSESIKISTNPDGLVKLEINSCQPNDSGAYKLIISNPHGEKVALCAVAVKPEEMQPKFLKPITSQTVVVGEPLKLEAQVTGFPAPEVKWYKDGMLLRPSPEINFINSPNGQIGLIIDAAQPLDAGVYKCLIANKGGEIEGVSKVEIVPKESKPVFVAELQDASSIEGFPVKMDIKVVGNPKPKLQWFHNGHEIKPDASHIAIVENPDNSSSLIIEKTAPGDSGLYEVIAQNPEGSTASKAKLYVAPKADETATEEAPQFVSALRDVNADEGQELVLSAPFISNPMPEVIWSKDGVTLTPNERLLMTCDGKHIGLTIKPAEAADSGNYTCLLANPLGEDSSACNANVRKVYKPPVFTQKISDQQQVFGNNAKIPVTVSGVPYPDLEWYFQDKPIPKSEKYSIKNDGDHHMLIVNNCEKGDQGVYKCIASNREGKDITQGRLDIVNEIKKHSRSEPPVFLKKIGDCDIYEGMVAKFTACATGYPEPEVEWFKNDQKLFPSDRFLIDIEPNGLLRLTIKNVTEYDVGRYSCRIFNPYGDDICHAELFYDSLDSQQKPLEDQYTDFKKYKKSGAPPPLSEGPIISRMTDRGLLLSWNPSVPLTPRYPITYQIEMMDLPEGDWRTLRTGVRSCACDIRNLEPFRDYRFRVRVENKFGVSDPSPYTQTYRQKLVPDPPKTYTYLPPGTDFRPETSPYFPKDFDIERPPHDGLAQAPQFLLREQDISYGVKDHNTELMWFVYGYPKPKMTYYFDDMLIESGGRFDQSYTRNGQATLFINKMLDRDVGWYEAVATNEHGEARQRVRLEIAEHPRFLKRPDETFIMARKNGRIEAKLVGIPLPEVHWFKDWKPIVDSSRIKISSYDPDIYVLSIHDSIIKDGGLYSISARNIAGSISTSVTVHIEENEDQYIYKTYGRHPYVRSKQLRYQDKYDIGDELGRGTQGITYHAVERSSGDNYAAKIMYGRPELRPFMLNELEMMNTFNHKNLIRPYDAYDTDRSVTLIMELAAGGELVRDNLLRRDYYTERDIAHYIRQTLWGLEHMHEMGVGHMGLTIKDLLISVVGGDIIKVSDFGLSRKINRHNLSTLDYGMPEFVSPEVVNKEGVNFSHDMWTVGLITYVLLGGHNPFLGIDDRETLTKIREGRWDFKDEIWTHISDDGRDFISRLLLYSPEERMDVKTALKHPWFFMLDRPVYDHDYQIGTDRLRNYYDHFRDWYANASCKNYFRRRRLSGCFQHPSKMVYPPGHVYTPENTPEPLPEPRIRAKREEVVSKYLHPDYELGLIQSESHYQYGPDTYLLQLRDVNFPVRLREYMKVAHRRSPSFALNDSVDWSLPVIRERRRFTDIMDEEIDDERTRSRISMYAANESYSIRRLRTELGPRLDEYTEADAMIETQREGYPPFFREKPQTIAITENQPSHIHCFAVGDPKPCVQWFKNDMVLTESKRIKISVDEDGRSILRFEPALHFDVGVYKVVARNKVGQTVARCRIVVATLPDAPDSPEISANSGTEILLRWKQPRDDGHSTVLCYSLQYKLSNCDAWTTVADNIDHEFYLLHDLQPNTNYQFRLASKNRIGWSEMGIPVSASTVGGDAPKIHITKAMKHLQQLTENGHQVVPEEERVHTDYHCEREPPNWVTDSSVSDKYSFISEIARGEFSTIVKGIQKSTDTVVVAKILEVTDENEDNVVAEFDNFKTLRHERIPALFSAYKPLNVPIAIFVMEKLQGADVLTYFSSRHEYSEQMVATVVTQLLDALQYLHWRGYCHLNIQPDNVVMASVRSIQVKLVDFGSAKKVNKLGMKVTPCGSLDFQPPEMINDEPIFPQSDIWSLGALTYLLLSGCSPFRGADEYETKQNISFVRYRFENLFKEVTPEATRFIMLLFKRHPTKRPYTEDCLEHRWLMSSDYMVRKRERAIFLGSRLKTFCDEYHDLKNASATSSKVLNTVAGGPTPTQLLRSNSIQEELLTTF | null | null | adult somatic muscle development [GO:0007527]; protein localization to M-band [GO:0036309]; sarcomere organization [GO:0045214] | M band [GO:0031430] | ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]; tropomyosin binding [GO:0005523] | PF00041;PF07679;PF13927;PF00069;PF00621; | 1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439}. Note=In the embryo, localizes across the muscles in a striped pattern and is positioned laterally to the sites at which muscles are attached to the epidermis. In the larval body wall muscles, localizes to the M line and moves away from the attachment sites. During pupal development, progressively forms broad striations at the M line which become more defined after pupal eclosion. Colocalizes with myosin thick filaments at the M line. {ECO:0000269|PubMed:22467859}. | null | null | null | null | null | FUNCTION: Structural component of the muscle M line which is involved in assembly and organization of sarcomere (PubMed:22467859, PubMed:26251439). Required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere (PubMed:22467859, PubMed:26251439). Lacks serine/threonine-protein kinase activity (PubMed:37121260). {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439, ECO:0000269|PubMed:37121260}. | Drosophila melanogaster (Fruit fly) |
A8DYP7 | CGLR2_DROME | MKESRNLENFVEKKLYECKKKYVDIPKDEGQRYGGKHYEALTSKIFEILRKENPELDIIIAEFSLEGSVGMLKIAKPNEFDLVFKLKFPYYKSIAVTRDPKIPGNVLLDMTRVLELLKDDPREDFQRIRELIQGRLVDAQNFFVVDRLRSWLQSLFSQALNRISYRVELVAGVVSHLKYRTCGPAHTIYVYGDYEYSVDYVPAICLAAEQNVLPTKQLECFKRANTSYWEAIPKPLKPLTETSMISFRSSFYAVEKILLQDVHENCRNAIRFMKKFRDVKTNLGNCKSYYIKTLFLWKIIQEPESYWLNPLSFILADMFDDLAENLRRGVITFFWDPELNMIDALTRDQVWEMYLCVQRIPRDLRGAEISRNKWSFFVLREFSHKKERNVNLKCSSRRKRNVIKGLKTTSICKLRNARTNGTWTAGLWTRPGHAYRGPSETVSTWDTVKDAAWSEGIVE | 2.7.7.-; 2.7.7.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A1ZA55}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A1ZA55}; | cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; immune response involved in response to exogenous dsRNA [GO:1902615]; innate immune response [GO:0045087] | cytosol [GO:0005829] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; 3',2'-cyclic GMP-AMP synthase activity [GO:0140700]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',2'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:68344, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:177334; Evidence={ECO:0000269|PubMed:34261128}; CATALYTIC ACTIVITY: Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:143093; EC=2.7.7.86; Evidence={ECO:0000269|PubMed:34261128}; | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP from ATP and GTP and plays a key role in antiviral innate immunity (PubMed:34261128). Directly binds some unknown nucleic acid, activating the nucleotidyltransferase activity, leading to synthesis of both 3',2'-cGAMP and 2',3'-cGAMP second messengers (PubMed:34261128). 3',2'-cGAMP and 2',3'-cGAMP bind to and activate Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:34261128). {ECO:0000269|PubMed:34261128}. | Drosophila melanogaster (Fruit fly) |
A8DYY6 | SCHI1_DROME | MDIYITKGITNPNYPGFQKFAHTLSDDYIEYSDMECNESDLTDSDREDDPTFPSKMAKESGSETFKNGQDSILSNCDNGNTYISEEESVNRSENIPDIVNENYSATSENSKRALQKPDLIYNLSQNYTTNPEFPSWSCTINSKYEGQLQGQSPIDIVGDFGGEVEREFELLLTGYKNKKEADELKGSNLDKICDAELSNGTEALKQTSSTRLSGNSTRKNKKKNTPYGHQIVKTKHPKPSHDERQLPPDTFDYKTYSQRKYIICDADQYSSVPEKNKNDSPNLNQAEIPNMSSLEIGGSGSQQNLDEDNNKVASRKYSNQSRWSQYLEDPIKYSKDPCSTMVLEQFDAYKIANDMDVETLQNHYKKVKQIEKKRRFNRDEIRKRLAIGDKDSLNNDIKKEEFLTGSDNESYSSDSETCPKLSSGVLRKQSEFCETKRNKEFENDKIFQKNQINQDKSMNHMNGNPIGTTDYPSDENLFFFANQSKLQIEVRIALAQSKEIAQMKVKARKHGVTPIVDVIRSMLCDVGIKMNSNHRWISRQLLTGIQVPTLQLLVNNLQEYIENLNVTLLESLKERDDLNSDQDDILHDLEKINNFFVFQQQSGQQVNKIVRHGHLD | null | null | negative regulation of growth [GO:0045926]; positive regulation of hippo signaling [GO:0035332]; positive regulation of protein serine/threonine kinase activity [GO:0071902] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; plasma membrane [GO:0005886] | null | PF10148; | null | SCHIP1 family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:26954546}. Apical cell membrane {ECO:0000269|PubMed:26954546}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (hpo), in complex with its regulatory protein Salvador (sav), phosphorylates and activates Warts (wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (yki) oncoprotein. Schip1 promotes kinase activity of Tao and enhances phosphorylation of hpo by Tao. {ECO:0000269|PubMed:26954546}. | Drosophila melanogaster (Fruit fly) |
A8DZE6 | WTIP_DANRE | MDEYDEDPGRRASKLMETLSIYDVYQDGMYGEPNPDMEKTKRMNGSSSTPGNKVYSAAPVRSVNGNRASVPLDFCSPQREAVYPDPDVYCTKSEVALPCYSGASDRLRRYTHAEVQGHRYSTGCAYDGLVLGKQVAVSGARSNSLCMSSPDGRYTATSPRSSLASSHSSQDQSKHTSPRSSISSPRSSLVSPGQGEGTSVISPRSSYASTASDTSKHSSPRTSLNSYDCGSKPSSNRTSGISMGYDQRHISPRSSTTSPRSSYSDSRFTPAGGHDPESAAVHGIPMASPRSSICSQPAVAANCVVSPRSSISSHSSRSSRSSRGSMSAYPELQLPMLGPGLPEDALLQDFTEPNGLHNNRVHLQTFPVLEEPQQQNSEVNIGFNYCKAGAGGQRFKLPYQVTPSRDSGPSQAERRLEALTLELEKELEIHMKKEYFGICVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRRLRGKAFYNVNGKVYCEEDFLYSGFQQTAEKCFVCGHLIMEMILQALGRSYHPGCFRCVICKEGLDGVPFTVDVENNIYCVKDYHTVFAPKCASCNQPILPAQGSEETIRVVSMDKDYHVDCYHCEDCGLQLNDEEGHRCYPLEGHLLCHRCHLHRLKTPLAPHPPPSYPLHVTEL | null | null | cilium assembly [GO:0060271]; cloaca development [GO:0035844]; cytoskeleton organization [GO:0007010]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; establishment of mitotic spindle orientation [GO:0000132]; heart looping [GO:0001947]; negative regulation of hippo signaling [GO:0035331]; neural crest cell development [GO:0014032]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of cell morphogenesis [GO:0022604]; regulation of DNA-templated transcription [GO:0006355]; response to hypoxia [GO:0001666]; visceral serous pericardium development [GO:0061032] | adherens junction [GO:0005912]; ciliary basal body [GO:0036064]; 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 {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: May monitor slit diaphragm protein assembly, a specialized adherens junction characteristic of podocytes. In case of podocyte injury, it shuttles into the nucleus and acts as a transcription regulator. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Acts as a transcriptional corepressor for snai1 and snai2/slug and plays a role in regulating neural crest development (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8DZH4 | XPR1_DANRE | MKFTEHLSAHITPEWRKQYIQYEAFKEMLYSAQDQAPSIEVTDEDTVKRYYAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQRESSRAAGLRHRRTVFHLSQQERCKHRNIKDLQLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKIFETSRGADWRVAHVEVAPFYTCKKITQLISETETLVTTELEGGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLYCGVFVALTVTVIIAGVVKLVEHFGDNTDVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLFEIAGFLGVLWCVSILSCLFAENTLIPIHMNPLALYGFFFLFLINPLKTCYYKSRFWLLKLLFRVVTAPFHRVGFADFWLADQLNSLVVVLMDLEYMICFYSLELNWTMSEGELWIKEGERICYSYSYGVRAVIKCLPAWFRFVQCLRRYRDTKRAFPHLVNAGKYSTTFFVVIFEALFKTHSGDERFVFLYIMIACRIVNSCYTLLWDLKMDWGLFDRNAGENTLLREEIVYPQKAYYYCAIVEDVILRFAWTIPLSLEVVYDRPVISNILGTVLPPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQEDGVRNRLGKKNWKRSYSMSLRRPRLSSQSKVRDTKVLIEDTDDDT | null | null | cellular response to phosphate starvation [GO:0016036]; intracellular phosphate ion homeostasis [GO:0030643]; macrophage differentiation [GO:0030225]; microglia differentiation [GO:0014004]; phosphate ion transmembrane transport [GO:0035435]; phosphate ion transport [GO:0006817]; skeletal system development [GO:0001501] | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | efflux transmembrane transporter activity [GO:0015562]; inositol hexakisphosphate binding [GO:0000822]; phosphate ion transmembrane transporter activity [GO:0015114] | PF03124;PF03105; | null | SYG1 (TC 2.A.94) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23791524}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell (PubMed:23791524). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q9UBH6, ECO:0000269|PubMed:23791524}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8E2V8 | PA2A_TRIGS | MRTLWIMAVLLLGVEGSLMQFEMLIMKLAKSSGMFWYSAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKATGCDPKKDVYTYSEENGDIVCGGDDPCRKEVCECDKAAAICFRDNMDTYNSKTYWMFPAKNCQEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the ADP-(IC(50)=272 nM) and collagen-induced (IC(50)=518 nM) human platelet aggregation in platelet rich plasma. Exhibits very high hydrolytic activities toward the synthetic lecithin, and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:22115990}. | Trimeresurus gracilis (Kikuchi habu) |
A8E5T6 | TCF21_XENTR | MSTGSLSDVEDFQEVEMLECDGIKLDPNKEFGISNDSNEESSTCDNGSPKKGRGTSGKRRKAPSKKSPLGNINQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENDLKEVVSTSRLCGPTAS | null | null | branching involved in ureteric bud morphogenesis [GO:0001658]; branchiomeric skeletal muscle development [GO:0014707]; bronchiole development [GO:0060435]; diaphragm development [GO:0060539]; embryonic digestive tract morphogenesis [GO:0048557]; epithelial cell differentiation [GO:0030855]; gland development [GO:0048732]; glomerulus development [GO:0032835]; kidney development [GO:0001822]; lung alveolus development [GO:0048286]; lung morphogenesis [GO:0060425]; lung vasculature development [GO:0060426]; metanephric glomerular capillary formation [GO:0072277]; metanephric mesenchymal cell differentiation [GO:0072162]; morphogenesis of a branching structure [GO:0001763]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; reproductive structure development [GO:0048608]; respiratory system development [GO:0060541]; roof of mouth development [GO:0060021]; Sertoli cell differentiation [GO:0060008]; sex determination [GO:0007530]; spleen development [GO:0048536]; ureteric bud development [GO:0001657]; vasculature development [GO:0001944] | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43680, ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. {ECO:0000250|UniProtKB:O43680}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8E5V9 | STING_XENTR | MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQQHSEEYSML | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709] | autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; protein homodimerization activity [GO:0042803]; proton channel activity [GO:0015252] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited (PubMed:30842662). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842662}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (PubMed:26300263, PubMed:30842662). Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Exhibits guanine base-specific ligand recognition: binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate LC3 lipidation (By similarity). Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling (PubMed:26300263). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:30842662}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8FNH9 | NSPC_CAMJ8 | MFYEKIQTPAYILEEDKLRKNCELLASVGEKSGAKVLLALKGFAFSGAMKIVGEYLKGCTCSGLWEAKFAKEYMDKEIHTYSPAFKEDEIGEIASLSHHIVFNSLAQFHKFQSKTQKNSLGLRCNVEFSLAPKELYNPCGRYSRLGIRAKDFENVDLNAIEGLHFHALCEESADALEAVLKVFKEKFGKWIGQMKWVNFGGGHHITKKGYDVEKLIALCKNFSDKYGVQVYLEPGEAVGWQTGNLVASVVDIIENEKQIAILDTSSEAHMPDTIIMPYTSEVLNARILATRENEKISDLKENEFAYLLTGNTCLAGDVMGEYAFDKKLKIGDKIVFLDQIHYTIVKNTTFNGIRLPNLMLLDHKNELQMIREFSYKDYSLRN | 4.1.1.96 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20534592}; | lysine biosynthetic process via diaminopimelate [GO:0009089]; nor-spermidine biosynthetic process [GO:0045312]; spermidine biosynthetic process [GO:0008295] | cytoplasm [GO:0005737] | carboxy-lyase activity [GO:0016831]; diaminopimelate decarboxylase activity [GO:0008836]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, NspC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=carboxynorspermidine + H(+) = CO2 + norspermidine; Xref=Rhea:RHEA:34099, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57920, ChEBI:CHEBI:65070; EC=4.1.1.96; Evidence={ECO:0000269|PubMed:20534592}; CATALYTIC ACTIVITY: Reaction=carboxyspermidine + H(+) = CO2 + spermidine; Xref=Rhea:RHEA:34095, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57834, ChEBI:CHEBI:65072; EC=4.1.1.96; Evidence={ECO:0000269|PubMed:20534592}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.1 mM for carboxyspermidine {ECO:0000269|PubMed:20534592}; KM=2.1 mM for carboxynorspermidine {ECO:0000269|PubMed:20534592}; Note=KM values are given with the protein sequence containing Glu instead of Lys at position 184, the effect of the variation on activity is unclear.; | null | null | null | FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine in vitro. In vivo, responsible for synthesizing spermidine, but not sym-norspermidine. {ECO:0000269|PubMed:20534592, ECO:0000269|PubMed:22025614}. | Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) |
A8FP63 | FADB_SHESH | MIYQSPTIQVELLEDNIARLCFNASGSVNKLDRETINSLDAALDAIQQDSHIQALVLTSAKGAFIVGADITEFLGLFAQEDSVLLPWIAEANVVFNKLEDLPFPTISAINGFALGGGFETVLATDFRIADTTAKIGLPETKLGLIPGFGGTVRLPRLIGTDNALEWITSGKDQRPEAALKVGAIDAVVAPENLQASAIKMLKDALAEKLDWQSRRARKQAALTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAAISVIEQAARCGRADALKVEHQAFVKLAKTDVAQALIGIFLNDQLVKGKAKKAGKLAKNIDTAAVLGAGIMGGGIAYQSASKGTPIIMKDIAQPALELGLGEASKLLAAQIKRGRSTPQKMAKVLNNITATLDYTPVKDVDVVVEAVVEHPKVKSMVLAEVEQNVSDDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGIDTGHHAQAVMAEGFPDRMGKNGKDAIDIMFEAERFGQKNSKGFYAYSVDRRGKPKKDVDPTSYELLGAEFGELKAFESEDIIARTMIPMIIETVRCLEEGIIATPAEADMGLVFGLGFPPFRGGVFRYIDTMGVANFVALADKYAHLGGLYQVTDAMRELAANNGSYYQS | 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}. | Shewanella sediminis (strain HAW-EB3) |
A8GYG0 | FADB_SHEPA | MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDSSIKALMLSSAKDAFVVGADITEFLGLFAEEDTVLQSWLEQANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPEAALKVGAIDAVVAPEQLKPAALKMLKDALIEKLDWQTRRAKKQAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVISVIEQAAQLDRAGALQVEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLTAQVKRGRSTPAKMAAVLNNITPALDYAPVKDADVVVEAVVEHPKVKSMVLAEVEQHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKTGKDAIDVMFEAERFGQKNSKGFYQYSVDRRGKPKKDLDPTSYELLQAEFGEQKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDTMRELAANNGSYYQQA | 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}. | Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) |
A8HAL1 | UBP16_DANRE | MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLLDGMRAEEAKRVNSGILEALKSSGKNFEAEQTKKIVKEYEKDGAPKNFVDRVFGGAMSSTVMCKECKTVSLVTEMFLDLSLPVADEAYRKKNQKKAVQHRHSVSDDGDQDTSSLANGNEDMPTGTGSKYQQKKAKKQAKKQAKNQRRQQKQGGKVTLDAITNQSSTDPADSSMQTQTVSVNGSADAQPADTNQEDLSLEKHNEDQDDEEPEQEQAASVNNRFTALSEDQTTEDIAEQVNEDEDEIEQNCAEEEELVEELNTMSLTTPSEGDVENGEDTLEDVKEYTVVNRDPELAFRALASRTAPVKQECSVESCLYQFTEVEHLTENNRLMCVTCTKQQPGYKDGCKKAVYRDALKQMLISDPPVVLTLHLKRFQQVAYSVCKVNRHVQFPQILDLAPFCSLNCTGVKEGETQVLYSLYGIVEHSGTMRSGHYTAYVKSRPSTHNCVQNGTAAASGDAEASKGSWFHISDSSVHPVPEAKVQSSQAYLLFYEKIS | 3.4.19.12 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; mitotic nuclear division [GO:0140014]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of translational elongation [GO:0045901]; protein homotetramerization [GO:0051289]; proteolysis [GO:0006508]; regulation of cell cycle [GO:0051726] | nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; histone binding [GO:0042393]; histone H2A deubiquitinase activity [GO:0140950]; transcription coactivator activity [GO:0003713]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family, USP16 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}. | 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:0000255|HAMAP-Rule:MF_03062}; | null | null | null | null | FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8HN58 | IFT27_CHLRE | MVKKEVKPIDITATLRCKVAVVGEATVGKSALISMFTSKGSKFLKDYAMTSGVEVVVAPVTIPDTTVSVELFLLDTAGSDLYKEQISQYWNGVYYAILVFDVSSMESFESCKAWFELLKSARPDRERPLRAVLVANKTDLPPQRHQVRLDMAQDWATTNTLDFFDVSANPPGKDADAPFLSIATTFYRNYEDKVAAFQDACRNY | null | null | null | cytoskeleton [GO:0005856]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:17276912}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:17276912}. Note=Colocalizes with IFT25 at the distal-most portion of basal bodies, probably the transition zones, and concentrates in the basal body region. | null | null | null | null | null | FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B. Forms a subcomplex within the IFT complex B with IFT25. Has very low GTPase activity either because it lacks the conserved catalytic Gln in position 79 or because it requires some GTPase-activating protein (GAP) for GTP turnover. {ECO:0000269|PubMed:21505417}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8I4E9 | CP100_CHLRE | MPIYDEASVPGTAAGRSTTDVGATAGANPFNIPADEEIFRFREEERARKEQDKLIAQTMRVADKTTFAAQMQATATADARTLLRELRPPKGPKATTTLAASSVGTLDRRKEKENMADFIAKKREIFLLQMSLDTKRAEIKKLEERARQREEALKKSEQMLEEDALRFDAFLKENDEKVQEAIKKAEAEAKAKQDKVLEIKRLNTATAALRSELNKYEEQLEDCRRYKEFLDSITPPEWFEQQAAKLQRRKDALVAEWQSQCEALKQRREAALAAKTAAESDYANARTQQQAERAERAIKESVAALKEIMKEKEPQPPNLDFEMDPEDEEMYFQEPGQLLAVYKQLEESNLFYIQNAQETEEALEELRQKLRDTKTRMDAEAQGLQGQVSTLQASIVAAREKAKRLKDRTLENEGAFTLSMGSSNAPTSSVTGSSGPGGPVNLKELGDKVREVYVRCGFDADASISTLQMLTNIEMKLEEYLNLAEGMTPDYVDGAEKAREKDRRKVARDEKLSTQHREHEARMARALERAAAPVFKKTGKPLMFRSAPPQRKKVVQADDRNDEEAELEAYLAQDMI | null | null | cell motility [GO:0048870]; cilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159] | axonemal outer doublet [GO:0097545]; motile cilium [GO:0031514] | dynein complex binding [GO:0070840] | PF13863; | null | CFAP100 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23569216}. Note=Localizes to the outer doublet microtubules of the axoneme. {ECO:0000269|PubMed:23569216}. | null | null | null | null | null | FUNCTION: As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm. {ECO:0000269|PubMed:23569216}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8ID55 | BLD10_CHLRE | MAIDVDRTLAVLRRKLEALGYSDPLEPASLQLVQKLVEDLVHTTDSYTAVKQQCAKQAQEIAAFDTRLESVRQDSVRLQSENSQLHVLVMQHAERHEREAREHYTAVKRLEDTIAELSYWKHAAAEKLASADKENAGLRKRCEELAKLTDRLASGAATPQSVAPKISSRSPIRVAPPPSPPRPRQATVDVLQAANGRILSLQRQLADATAELQELRQRVAEDEDQIRRRDVEIDRLGTRAGTDTNVLALRARNEANESMILQLNGTVESLAARVRELEAVEVRCEELQGALRRAEMDRDQAEERYSRSARDHDALSREVLGLRRDLAALQDTNNRAAGLLAADAAGASTPDTTAGAPALRQRLADSRADVERLSGQLAAADMERRNLAQQLSALRSELDDTQFLLAEAQSRAAGLAAAQAVAESEARRLAGEAAAREGRLRELDSQLAVVLSDLEARQAGFAALEKDRAEANARAEELARRLDEVERSAASERAAAAAAQQSVSRLDSELRVVRGSAAALEAEAAALRQELQDVSVGKVRATSALSSTEDEAVRARQQAEALRMQLTAERRAAEELRAGHDTLQLEVDRLGGQLALQQQEAELLRQQLAAARGELAASEAAASGAEQKLSGLGALSQRLEEMGEQARRAQAATAEAEAEAVRLRAAVSEAKEGQARAERGLREARREVEGAREAEALVRAQLREVEAQAEGTSKALKAAEADRDRALMDARLAAGDLASLRDQLAAETSSAADAGSTARQMAARLSAAERAAAAAQEERERAAVAAEEAEAAAAAARGREEEARAQGREWAERARRAEALVAEYEADVAQLRAARDSDAAALRSLEDTVAAARRDLDARRSEVEQLTTLSLRGDATVQEYMANLKAMSTDLRAAEMRAADLAGEAAAAQDAAASWRSEAEQLRGLLRQMDADRDNLQHELDAKAERLVAQEQQLAGAQAAEQEAARLLALAEGRLALTDNRAREGEAEAAAVRAQLAAALDSVRALSGEGEALREELRAVSEDLEALVRENQVVGGELAAVAAQRDSAAEEARRLGGRRASAEQLLRAKEAEAEDLRRVYEALAAEHRRLQGGVGALEREGAMREAALQAKAAEVSSLAESQRAAQATINQYVMDLQAFERQVDSLSRQLSQAEADGEELVRQREALLEEIRAAQQVRLGLERHREELQRQVASLDSQVAIGRARLEDSNSEAASLNQRLAMERSRVAELEGLLAGMRAREFRSDFASDRAGGQLAVMVDRNRALEEQVASLQHQVGALQASREAQDRELSRLRGEALALAASTAASLEGRTAAAGGAAAGAAKDQAAALDRLTSERDAAQDEAARLRGALAAAEAAAASASTAAAVSIPAAGSGSEAAAVLRVRCSELERRNTELMQELRTLQDTCRQQESLLSAAQNELSALQAEHRRLVELVARLDQDKAAAAAEAAAARQQVATATRRVATAEQEAAAGAARLQSQLRDEQGRRRQAERDFLELLSSIEGAGGEAAAAAVAAAHGEGAAELASRRLRELQTQVDALEAEKAGLEEATQRTRATLGAMSGQMAAIQAEYDATNTALAGLAGAMAAGAQGQGQVQGPAGTAPAAAAGAPGPQPGQAQAGGFGGAHGGGSISLSGGPRR | null | null | ciliary basal body organization [GO:0032053]; cytoskeleton organization [GO:0007010]; regulation of cell division [GO:0051302] | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary pro-basal body [GO:0120280]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803] | null | 1.10.287.1490; | CEP135/TSGA10 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15173189}. Note=Localized at the cartwheel, the first ninefold symmetrical structure appearing during basal body/centriole assembly near the proximal end of the organelle. {ECO:0000269|PubMed:15173189}. | null | null | null | null | null | FUNCTION: Microtubule-binding protein essential for cytoskeletal organization (e.g. rootlet microtubule bundles) and flagellar basal body/centriole assembly. {ECO:0000269|PubMed:15173189, ECO:0000269|PubMed:27477386}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8IKD2 | CAH_AZOC5 | MPIAKVHRIATASPDDVSGLAAAIATGAIAPAGILAIFGKTEGNGCVNDFSRGFAVQSLQMLLRGHMGAAADEVCLVMSGGTEGGMSPHFLVFERAEGNAPEAAPALAIGRAHTPDLPFEALGRMGQVRMVAQAVRRAMAAAGITDPEDVHFVQVKCPLLTAMRVKEAEARGATTATSDTLKSMGLSRGASALGIALALGEVAEDALSDAVICADYGLWSARASCSSGIELLGHEIVVLGMSEGWSGPLAIAHGVMADAIDVTPVKAALSALGAEAGEATIVLAKAEPSRSGRIRGKRHTMLDDSDISPTRHARAFVAGALAGVVGHTEIYVSGGGEHQGPDGGGPVAVIAARTMG | 3.5.2.15 | null | atrazine catabolic process [GO:0019381] | null | cyanuric acid amidohydrolase activity [GO:0018753]; metal ion binding [GO:0046872] | PF09663; | 3.30.1330.160;3.30.1330.170;3.30.1330.180; | Cyclic amide hydrolase (CyAH) family | null | null | CATALYTIC ACTIVITY: Reaction=cyanurate + H2O = 1-carboxybiuret + H(+); Xref=Rhea:RHEA:70363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:38028, ChEBI:CHEBI:142864; EC=3.5.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=370 uM for cyanuric acid {ECO:0000269|PubMed:22730121}; Note=kcat is 50 sec(-1) with cyanuric acid as substrate. {ECO:0000269|PubMed:22730121}; | PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}. | null | null | FUNCTION: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121}. | Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571) |
A8IQT2 | CCD40_CHLRE | MADPMDQPSTSDPVDNQIFGEQGGLRPDHPLLRRAQEALKVQFEANRTRLQEELREKANALKQAKARREALGVELYGFQQNLAKLQLNLETTHQNYQCEDQLNQLKQQLSLEEGDTKGERSRRVCVCVCRVCCRIDTLQDNLKGTQQQLALVSAQLEAQKRETRAALETLAEAEVGGCVRDEALSAIQDGMREQQQQELSLVLEIEGYKKDVVREQLKHESLTAVVRKVEGDAVFVQKQIEGAQERQARLQEILAKLAKSLEHTEAEGEADAVDRAITKVAAEGRAIEEEMLSALSDQTTAEKATSKTAADTQELRKRIRAEELAVVETENELAKLQVDILNTEAHNSRLGETLGLLDEELRDKGRTIEKYELEIKRRNDEIEKKTREIDILNRRRDCRGSAALDTRPLQAPPPPQVKSDLALTTPMYTPPPVPQPSVGMTVTTEKLVSDMEKALTKREIISVKGRATAAKSKSSTPAGSATASSRASPSASVASSTLTRNQLDRATTDLAKSIKDLEAGRYRPVVEDAAAVGEELGRAQDKLGRVVALLEGLRQAAPHLAGELDKVLCHVADVRA | null | null | axoneme assembly [GO:0035082]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart looping [GO:0001947] | cytoplasm [GO:0005737]; motile cilium [GO:0031514] | null | null | null | CCDC40 family | PTM: Asymmetrically dimethylated at Arg-246 and Arg-523 during flagellum resorption. Probably methylated by PRMT1. {ECO:0000269|PubMed:24152136}. | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:25395538}. | null | null | null | null | null | FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (PubMed:25395538). Together with CCDC39/FAP59 forms a 96-nm-long complex in flagella. This complex does not act as a physical ruler, but rather act as a negative regulator for radial spokes: the complex lays along specific protofilaments, masking radial spoke binding sites and allowing recruitment of inner dynein arm (IDA) and nexin-dynein regulatory complexes (N-DRC) (PubMed:25395538). {ECO:0000269|PubMed:25395538}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8IU92 | CFA20_CHLRE | MFKNAFQSGFLSVLYSIGSKPLEIWDKQVSNGHIKRITDADIQSSVLEIMGQNVSTTYITCPADPNKTLGIKLPFLVLIIKNLNKYFSFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDSGWNQIQFNLSDFTRRAYGTNYIETLRVQVHANCRIRRIYFSDRLYSEEELPAEFKLFLPIQKS | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; establishment of protein localization to organelle [GO:0072594]; positive regulation of cilium-dependent cell motility [GO:2000155]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296] | axonemal central pair [GO:0097540]; axonemal microtubule [GO:0005879]; axonemal outer doublet [GO:0097545]; ciliary basal body [GO:0036064]; microtubule associated complex [GO:0005875]; motile cilium [GO:0031514] | null | PF05018; | null | CFAP20 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9Y6A4}. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes predominantly along the length of all nine axonemal outer doublet microtubules (DMTs). Localizes to the inner junction (IJ) between A- and B-tubules of the DMTs. Associates to the basal bodies in a microtubule-dependent manner. Enters into the flagella through diffusion. | null | null | null | null | null | FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (PubMed:24259666, PubMed:24574454). Involved in the control of flagellar beating in an asymmetric and planar waveform (PubMed:24259666, PubMed:24574454). Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6 (PubMed:24259666, PubMed:24574454). Not essential for flagellar assembly (PubMed:24574454). {ECO:0000269|PubMed:24259666, ECO:0000269|PubMed:24574454}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8J637 | PETS_CHLRE | MLRELGRTATVKAHGRSVLRPVRGPAGRRQVAFTGVRPSVRVFAEAPAAEQAAKAIKLEDVKEGSEYEGTVTTVEEFGAFVNFGANTNGLVHISKLASGFTKNAKDVVQPGQKVTVKVLSVDAEKKRVSLELKSAVAAEASAEESDDIITEPDREGADATDDDEDVEVELEDGQVEVRADLPGFEDIPFVMEEADMDAEMSEAAIAALEADLDGAEIRYELEAPAYMEEVTGKVARIEDYGVFLEFEWNGKTLTGLLAKDEMKVPSSALSAEAQAALRAEWADTGFEMPAFVELPDDELDVKKYYQPGESVPAFVLESSLVDGRGISLTHFTDEEVSAEAVAAYEELEDDEDEELDKMMADAAGLEDEVLAFDPEALMEEDEGEEAGAAADAGDDAEYEGVSADGLEGANGNYALGATRSGLIKGKNGYQVAPMGLPSRPLNDAVTSSGLAILGTSEVDFDGDEVQLVDYWTSEAFDNIPKDVLKKLGLKMSYTEAGEAEFEERADFEATDVPFYLYGGDVESRAKEFVADLLSDDVDEAELPARAGRAPIVLAAAVQNISAAEVKALREKTGAGMMDCKKALAECAGDAEAAAEWLRKKGLSGADKKAGRIAAEGAVARYIHPGSRLGVLLEVNCETDFVAASEKFQALVNELGMIIAATDCICVSPEDVPEEVLAKEREVEMGKEDLANKPEAIRAKIVEGRLQKMRDQVALTNQATLSNPDKTVAELVKETIAAVGENVKIRRFIKYRLGEGLEKKANDFAAEVAQQTQAKAAAPAAPKKEEPKKEEPKKATVAVSAGTVKELRDKTGAGMMDCKKALAENENDMEKATEWLRMKGLAGADKKAGRIAAEGVVASYIHPGSRLGVLLEVNCETDFVAASEKFNELVNYIAMGIVAGQNVQYVSADEIPAEVFEREKQLEMARDDLKGKPDAIRAKIAEGRAKKIATEMCLLDQPFLTDPSKTVAEAIKESIAAIGEKISVRRFVKFQLGEGLEKKSNDFAAEVAAATGAK | null | null | mitochondrial translational elongation [GO:0070125]; response to light stimulus [GO:0009416] | chloroplast [GO:0009507]; chloroplast ribosome [GO:0043253]; mitochondrial matrix [GO:0005759] | mRNA binding [GO:0003729]; translation elongation factor activity [GO:0003746]; translation elongation factor binding [GO:0061770] | PF00889;PF00575; | 1.10.286.20;1.10.8.10;3.30.479.20;2.40.50.140; | EF-Ts family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:12417713, ECO:0000269|PubMed:15548736}. | null | null | null | null | null | FUNCTION: [Elongation factor Ts, chloroplastic]: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP (PubMed:15548736). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (PubMed:15548736). {ECO:0000269|PubMed:15548736}.; FUNCTION: [Plastid-specific ribosomal protein-7, chloroplastic]: Binds to psbD and psbA mRNAs 5'-untranslated regions (UTRs) in vitro. {ECO:0000269|PubMed:15548736}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8JB22 | DRC2_CHLRE | MVKAGKKVKGASKVRENETEEEKKIRLEMEALAADEAERKAQEAARVALRERQLREQRYAHLNGIKIHNQWRKIMRMAKVEELRREIEILSQNHEREVDRKDAIMQMLDRDLEEAEEQYSLAVRSHMLVVDNLLDLQYQRMRALEAEFAADLKALEDEFETERTEIVNAHTRQRKDMGDMIAAMEGEFADAEAELRQEYEAQREEIKNRNSEEYNVLKIQLEGIIEELEKSFELAHRAYLESTEHRTNTFRTLTKDDAKAALKIERQMRKLVRLQEALQHWRTKIATNGREWEERNRALRNEKEIMARHYAKLKSSMDAFRAGQAERLKQLSLASSGAMETLRGKLAVAENVLKLAELARKYETEQEKVLPFWNPAQAVPSGEQGDEEAAAQAEAEAAALEPSAAELGELGLRASMPEDSSKEAPGPSKSSAGPGKPKFSSYGLDPSSGSEVDEWDYLNCFFRRYNKALLDKTAIDKEKSRLERENADLRSILKQYLDGISVNDDVLNNPVNPLLVVNNRLQITLTERNKARAAAMAQRAAAATGAGLSVTGQGAGGGGQKQLVEVQVVSRVS | null | null | axonemal dynein complex assembly [GO:0070286]; cilium-dependent cell motility [GO:0060285]; regulation of cilium movement [GO:0003352] | axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; motile cilium [GO:0031514] | null | PF14772;PF14775; | null | DRC2 family | PTM: Asymmetrically dimethylated at Arg-96 and Arg-142 during flagellum resorption. Probably methylated by PRMT1. {ECO:0000269|PubMed:24152136}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:29167384}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29167384}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (PubMed:23427265, PubMed:25411337). Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules (PubMed:29167384). {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337, ECO:0000269|PubMed:29167384}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8JQX3 | NOCT_DROME | MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVRMGSFNSAPKINNVDSQDDGLVLPSGLSTPALLQHVQQLRGGGIEQPSLLTRGFLKPLLADEDVADGLRCLKLNSVSRVCSAPVEGDDIRLLQWNILSQTLGQHNDGFVRCPEEALTWEHRKYLIVQEILQNQPDVICLQEVDHFKFLQTVLGSQNYAGIFFPKPDSPCLYIEQNNGPDGCAIFYKRDKLQLQGYDTRILEVWRVQSNQVAIAARLRMRSSGREFCVATTHLKARHGALLAKLRNEQGRDLIRFVKQFAGDTPLLLCGDFNAEPVEPIYATILGCDLLRLGSAYADVKLDREEILHPNADVGEFVAKSMKREPPYTTWKIREEGEECHTIDYVFYTPDRLKIKNCLDFPAGEQIGKNRTPSFQYPSDHFSLVCDFELLPPTENGKESGSGSGSDGENETEVEGSKHGSIQ | 3.1.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UK39}; Note=Binds 2 magnesium ions, but the ions are only loosely bound to the protein. {ECO:0000250|UniProtKB:Q9UK39}; | locomotor rhythm [GO:0045475]; NADP metabolic process [GO:0006739]; response to light stimulus [GO:0009416] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; NADP phosphatase activity [GO:0019178]; NADPH phosphatase activity [GO:0102757] | PF03372; | 3.60.10.10; | CCR4/nocturin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19581445}. | CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31147539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051; Evidence={ECO:0000269|PubMed:31147539}; CATALYTIC ACTIVITY: Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:31147539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665; Evidence={ECO:0000269|PubMed:31147539}; | null | null | null | null | FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference for NADPH over NADP(+) (PubMed:31147539). Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay (PubMed:20504953). Required at the pupal stage for proper wing morphogenesis after eclosion (PubMed:19581445). {ECO:0000269|PubMed:19581445, ECO:0000269|PubMed:20504953, ECO:0000269|PubMed:31147539}.; FUNCTION: [Isoform C]: Doesn't have a role in light-mediated behavioral response. {ECO:0000269|PubMed:19966839}.; FUNCTION: [Isoform D]: In dorsal neurons, contributes to the light-mediated behavioral response. {ECO:0000269|PubMed:19966839}.; FUNCTION: [Isoform E]: Doesn't have a role in light-mediated behavioral response. {ECO:0000269|PubMed:19966839}. | Drosophila melanogaster (Fruit fly) |
A8JUP7 | HAYAN_DROME | MAMISARRYFLLGLLVLTTSAYVTVGDEGDPCQVRSDIPGICLSSSACENIRGYLKSGTLSTSQVPSCGFGAREEIICCPTVACCATDRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQNFFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQSVGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPNNNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRDKDTQPQEPWNDVSNNLDADPAPSIFNPAETRPTTPNPNPSRVNLPEKERPSVAACEKIRSGGKPLTVHILDGERVDRGVYPHMAAIAYNSFGSAAFRCGGSLIASRFVLTAAHCVNSDDSTPSFVRLGALNIENPEPGYQDINVIDVQIHPDYSGSSKYYDIAILQLAEDAKESDVIRPACLYTDRSDPPANYKYFVAGWGVMNVTNRAVSKILLRAALDLVPADECNASFAEQPSANRTLRRGVIASQLCAADKNQRKDACQGDSGGPLILEIDDVDGTYSIVGVISSGFGCATKTPGLYTRVSSFLDYIEGIVWPSNRF | 3.4.21.- | null | defense response to fungus [GO:0050832]; immune system process [GO:0002376]; melanin biosynthetic process [GO:0042438]; positive regulation of melanization defense response [GO:0035008]; proteolysis [GO:0006508]; regulation of melanization defense response [GO:0035007]; Toll receptor ligand protein activation cascade [GO:0160032] | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22227521}. | null | null | null | null | null | FUNCTION: Serine protease which, by converting prophenoloxidase 1 (PPO1) into its active form, plays an essential role in the melanization immune response to physical or septic wounding. May function in diverse PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A and Spn28D in the hemolymph, and Spn28D and Spn77BA in the trachea. Also required in the systematic wound response by mediating the redox-dependent activation of the JNK cytoprotective cascade in neuronal tissues after integument wounding. {ECO:0000269|PubMed:22227521}. | Drosophila melanogaster (Fruit fly) |
A8JUV0 | SBNO_DROME | MTSKKRKTLLDADDDNDNFDEDDSGSDFDDDEDPDQIEVPGGGRDLNTAVTYAQNIRSGVGVAPKGGIPIPISGAKIVVGNNKIKPISLLRINNNNNNIVTSVNNRNNNNIISTNGSSNNNNNSINNNSQIIKTTTVTTTPTTVGATPTVGGVALGGKLTVIPIAGRNVALDNNLSNMPKKLNNMVTAMGSPAARSSGNAGTTGSSQGGAIGSTSSYLNSLTTNELMNLAAYVAAKGSNAPPPPPPSTAANSVRHSPTGGIPNPGGNFFGGSAAASTSASAANFNMAASLLAQMSYAGGASQIRALKVAGNIGGVGNNQKPPPIATTPGSGGPAGGAPGSGVKGNNSMMEAVQKLIAMNPEYLTSGIPNTVFQMFMQSMQRPQATPSPNQPMNPGAMVTSAAAAAAHASAVAYVQQEEDEVDYEEMGVAETYADYWPAKLKLGKKHPDAVVETASLSSVEPCDVYYKLSLPLETINSGHLSALQLESITYASQAHDHLLPDGSRAGFLIGDGAGVGKGRTIAGIIYENYLKGRKKALWISVSNDLKYDAERDLSDIGATRIEVHALNKFKYAKISSDVNNNCKRGVIFSTYSALIGESNNKTGKYRSRFRQLLQWCGEDFEGLIIFDECHKAKNLCPVGSGKPTKTGQTVLELQQKLPKARVVYASATGASEPKNMAYMVRLGLWGQGTAFGNFNDFITAVERRGVGAMEIVAMDMKLRGMYIARQLSFKGVSFKIEEVPLSKEFRKIYDQSVELWVEAMQKFTEAAELIDAESRMKKTMWGQFWSSHQRFFKYLCIAAKVNHAVLVARESIKYGKCVVIGLQSTGEARTLDQLERDDGELTDFVSTAKGVFQSFVERHFPAPDRNRINRILGLYDETPSLSSVADSTSSLSNNSNITTAAGKRKGSNNNDNRSTKIKKKKRSGSWECSDSEDENTDMKRNRKRDGGNSNSDSDEANSDDDLKSDIDDEDEDHDVDSDQRSVASDASSDFNPFFSGSDSDIDPWVNARSKKSKKAQKKSKKKVKKEKTKKEITTSSATDPSGSTAMSATVVAALNAVKNRKSQLSTQDKIQDLLQKKQELKGTVTPVGVNGVKLNYGPPPKDAIERACTMKEELLRKIERLGARLPPNTLDQLIDELGGPDNVAEMTGRRGRVVQTDDGSIQYESRTESDVPLETLNITEKQRFMDGEKDVAIISEAASSGISLQSDRRVFNQRRRVHITLELPWSADRAIQQFGRTHRSNQVNAPEYIFLISDLAGERRFASTVAKRLESLGALTHGDRRATETRDLSQFNIDNKYGRQALETVMRTIMGYESPLVPPPTDYSGEFFKDIAGALVGVGIIVNSESHPGVLSLDKDYNNISKFLNRILGCPVDLQNRLFKYFTDTMTAIIQQAKRGGRFDLGILDLGAAGENVTRVRLIRFVRKHATGVAPTEMHTVRVERGMIWQEAIDKYADLFNENEGFYLSHQLRNQKRTAIMVVILESRNSSSTSSTTDLDSGSKKKKTHSKKEIMCQIYRPNTGLQVRHESLFELEKKYRKVASEEAEPHWTEQYDASVNTCSHAYWNGNCRNVSLGNDCEVGLRQRLYHVLAGSVLSVWGRVEHILNTRSNSKMQVIRMKTTEGEKIVGTLIPKSCFEPLVADLRSDSEKQEEFNY | null | null | imaginal disc-derived wing margin morphogenesis [GO:0008587]; Notch signaling pathway [GO:0007219]; photoreceptor cell development [GO:0042461]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; wing disc dorsal/ventral pattern formation [GO:0048190] | nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; histone binding [GO:0042393] | PF13872;PF13871; | 3.40.50.300; | SBNO family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9171377}. | null | null | null | null | null | FUNCTION: Notch pathway component, may contribute to the specificity between lateral and inductive Notch signaling pathways in the wing disk. Required during many developmental stages including oogenesis, embryogenesis and imaginal development of the eye, wing and leg. Ebi and sno regulate EGFR-dependent Delta transcription in the developing eye, by antagonizing a repressor function of Suppressor of Hairless (Su(H)). They are required in the R-cells for normal cone cell development. {ECO:0000269|PubMed:11731237, ECO:0000269|PubMed:12230979, ECO:0000269|PubMed:8287794, ECO:0000269|PubMed:9171377}. | Drosophila melanogaster (Fruit fly) |
A8K0Z3 | WASH1_HUMAN | MTPVRMQHSLAGQTYAVPFIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPGRLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIHVPSYLPDLPGIANDLMYSADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGWATLLESIRQAGGIGKAKLRSMKERKLEKQQQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFVRVSDSIPPLPPPQQPQAEEDEDDWES | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; exocytosis [GO:0006887]; extracellular matrix disassembly [GO:0022617]; negative regulation of autophagy [GO:0010507]; positive regulation of cell migration [GO:0030335]; positive regulation of pseudopodium assembly [GO:0031274]; protein transport [GO:0015031]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; regulation of protein ubiquitination [GO:0031396]; retrograde transport, endosome to Golgi [GO:0042147] | autophagosome [GO:0005776]; centriole [GO:0005814]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; ubiquitin protein ligase binding [GO:0031625] | PF11945; | null | WASH1 family | PTM: Ubiquitinated at Lys-220 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly. {ECO:0000269|PubMed:23452853}. | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:19922874}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome {ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:24344185}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2 (PubMed:19922874). Localizes to MMP14-positive late endosomes and transiently to invadipodia (PubMed:24344185). Localized to Salmonella typhimurium entry sites (By similarity). {ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:24344185}. | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922874, PubMed:19922875, PubMed:20498093, PubMed:23452853). Involved in endocytic trafficking of EGF (By similarity). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (PubMed:22114305). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation (By similarity). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (PubMed:24344185). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23452853, ECO:0000305|PubMed:20498093}. | Homo sapiens (Human) |
Subsets and Splits