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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P07663 | PER_DROME | MEGGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKGAGQGAGQAQTLISASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQAIEQLQQEEEEDQSGSESEADRVEGVAKSEAAQSFPIPSPLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSFCCVISMHDGIVLYTTPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRG... | null | null | behavioral response to cocaine [GO:0048148]; circadian behavior [GO:0048512]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; circadian sleep/wake cycle [GO:0042745]; circadian temperature homeostasis [GO:0060086]; copulation [GO:0007620]; courtship behavior [GO:0007619]; determinat... | cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222] | PF00989;PF14598; | 3.30.450.20;1.20.5.770; | null | PTM: Phosphorylated with a circadian rhythmicity, probably by the double-time protein (dbt). Phosphorylation could be implicated in the stability of per monomer and in the formation of heterodimer per-tim. {ECO:0000269|PubMed:8134384}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15629718, ECO:0000269|PubMed:24210908, ECO:0000269|PubMed:36994075}. Cytoplasm, perinuclear region. Cytoplasm, cytosol {ECO:0000269|PubMed:15629718, ECO:0000269|PubMed:24210908, ECO:0000269|PubMed:36994075}. Note=Nuclear at specific periods of the day (PubMed:15629718, ... | null | null | null | null | null | FUNCTION: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and ... | Drosophila melanogaster (Fruit fly) |
P07664 | SRYD_DROME | MDTCFFCGAVDLSDTGSSSSMRYETLSAKVPSSQKTVSLVLTHLANCIQTQLDLKPGARLCPRCFQELSDYDTIMVNLMTTQKRLTTQLKGALKSEFEVPESGEDILVEEVEIPQSDVETDADAEADALFVELVKDQEESDTEIKREFVDEEEEEDDDDDDEFICEDVDVGDSEALYGKSSDGEDRPTKKRVKQECTTCGKVYNSWYQLQKHISEEHSKQPNHICPICGVIRRDEEYLELHMNLHEGKTEKQCRYCPKSFSRPVNTLRHMRMHWDKKKYQCEKCGLRFSQDNLLYNHRLRHEAEENPIICSICNVSFKSR... | null | null | anterior/posterior axis specification, embryo [GO:0008595]; bicoid mRNA localization [GO:0045450]; oogenesis [GO:0048477]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sexual reproduction [GO:0019953] | cytosol [GO:0005829]; nucleus [GO:0005634]; polytene chromosome interband [GO:0005705] | chromatin insulator sequence binding [GO:0043035]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulato... | PF00096;PF12874; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2081456}. | null | null | null | null | null | FUNCTION: Transcriptional activator that controls bicoid gene expression during oogenesis. Found in transcriptionally active cells. Binds to specific sites on polytene chromosomes of third instar larvae. Binds to the consensus DNA sequence 5'-YTAGAGATGGRAA-3'. {ECO:0000269|PubMed:9154812, ECO:0000269|PubMed:9858707}. | Drosophila melanogaster (Fruit fly) |
P07668 | CLAT_DROME | MASNEASTSAAGSGPESAALFSKLRSFSIGSGPNSPQRVVSNLRGFLTHRLSNITPSDTGWKDSILSIPKKWLSTAESVDEFGFPDTLPKVPVPALDETMADYIRALEPITTPAQLERTKELIRQFSAPQGIGARLHQYLLDKREAEDNWAYYYWLNEMYMDIRIPLPINSNPGMVFPPRRFKTVHDVAHFAARLLDGILSHREMLDSGELPLERAASREKNQPLCMAQYYRLLGSCRRPGVKQDSQFLPSRERLNDEDRHVVVICRNQMYCVVLQASDRGKLSESEIASQILYVLSDAPCLPAKPVPVGLLTAEPRSTW... | 2.3.1.6 | null | acetylcholine biosynthetic process [GO:0008292]; neuromuscular synaptic transmission [GO:0007274] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuron projection [GO:0043005]; nucleus [GO:0005634]; terminal bouton [GO:0043195] | choline O-acetyltransferase activity [GO:0004102] | PF00755; | 3.30.559.10;3.30.559.70; | Carnitine/choline acetyltransferase family | PTM: The N-terminus of choline O-acetyltransferase 67 kDa and 54 kDa chains are blocked. | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + choline = acetylcholine + CoA; Xref=Rhea:RHEA:18821, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.6; Evidence={ECO:0000269|PubMed:1851526}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18822; Evidence={ECO:0000305|PubMed:1851526}; | null | null | null | null | FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. {ECO:0000269|PubMed:1851526}. | Drosophila melanogaster (Fruit fly) |
P07669 | TPIS_SCHPO | MARKFFVGGNFKMNGSLESMKTIIEGLNTTKLNVGDVETVIFPQNMYLITTRQQVKKDIGVGAQNVFDKKNGAYTGENSAQSLIDAGITYTLTGHSERRTIFKESDEFVADKTKFALEQGLTVVACIGETLAEREANETINVVVRQLNAIADKVQNWSKIVIAYEPVWAIGTGKTATPEQAQEVHAEIRKWATNKLGASVAEGLRVIYGGSVNGGNCKEFLKFHDIDGFLVGGASLKPEFHNIVNVHSL | 5.3.1.1 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; nucleus [GO:0005634] | triose-phosphate isomerase activity [GO:0004807] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000305|PubMed:3912263}; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:3912263}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000305|PubMed:3912263}. | null | null | null | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P07676 | TRFA_ECOLX | MNRTFDRKAYRQELIDAGFSAEDAETIASRTVMRAPRETFQSVGSMVQQATAKIERDSVQLAPPALPAPSAAVERSRRLEQEAAGLAKSMTIDTRGTMTTKKRKTAGEDLAKQVSEAKQAALLKHTKQQIKEMQLSLFDIAPWPDTMRAMPNDTARSALFTTRNKKIPREALQNKVIFHVNKDVKITYTGVELRADDDELVWQQVLEYAKRTPIGEPITFTFYELCQDLGWSINGRYYTKAEECLSRLQATAMGFTSDRVGHLESVSLLHRFRVLDRGKKTSRCQVLIDEEIVVLFAGDHYTKFIWEKYRKLSPTARRMF... | null | null | DNA replication [GO:0006260]; plasmid maintenance [GO:0006276] | plasma membrane [GO:0005886] | DNA binding [GO:0003677] | PF07042; | null | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10692384, ECO:0000269|PubMed:10783300}; Peripheral membrane protein {ECO:0000269|PubMed:10692384, ECO:0000269|PubMed:10783300}. Note=Probably the site where plasmid replication is initiated. | null | null | null | null | null | FUNCTION: Required for initiation of plasmid DNA replication, along with host-derived DnaA and other host proteins. Both forms of the protein are capable of initiating plasmid replication in a number of Gram-negative bacteria. Binds to 8 17-base pair repeat sequences (iterons) in the RK2 minimal replication origin (ori... | Escherichia coli |
P07685 | HIS2_NEUCR | METTLPLPFLVGVSVPPGLNDIKEGLSREEVSCLGCVFFEVKPQTLEKILRFLKRHNVEFEPYFDVTALESIDDIITLLDAGARKVFVKTEQLADLSAYGSRVAPIVTGSSAALLSSATESGLLLSGFDQTASEAAQFLEEARDKKITPFFIKPVPGADLEQFIQVAAKANAIPILPSTGLTTKKDEAGKLAISTILSSVWKSDRPDGLLPTVVVDEHDTALGLVYSSAESVNEALRTQTGVYQSRKRGLWYKGATSGDTQELVRISLDCDNDALKFVVKQKGRFCHLDQSGCFGQLKGLPKLEQTLISRKQSAPEGSYT... | 1.1.1.23; 3.5.4.19; 3.6.1.31 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion. {ECO:0000250}; | histidine biosynthetic process [GO:0000105] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; histidinol dehydrogenase activity [GO:0004399]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; phosphoribosyl-AMP cyclohydrolase activity [GO:0004635]; phosphoribosyl-ATP diphosphatase activity [GO:0004636] | PF00815;PF01502;PF01503; | 1.20.5.1300;1.10.287.1080;3.40.50.1980;3.10.20.810; | Histidinol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide; Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, ChEBI:CHEBI:59457; EC=3.5.4.19; CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-r... | null | PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-hi... | null | null | null | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P07686 | HEXB_HUMAN | MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFG... | 3.2.1.52 | null | astrocyte cell migration [GO:0043615]; chondroitin sulfate catabolic process [GO:0030207]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; intracellular calcium ion homeostasis [GO:0... | acrosomal vesicle [GO:0001669]; azurophil granule [GO:0042582]; azurophil granule lumen [GO:0035578]; beta-N-acetylhexosaminidase complex [GO:1905379]; cortical granule [GO:0060473]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:... | acetylglucosaminyltransferase activity [GO:0008375]; beta-N-acetylhexosaminidase activity [GO:0004563]; identical protein binding [GO:0042802]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00728;PF14845; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | PTM: N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc(2) and Man(5 to 7)-GlcNAc(2), respectively. {ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}.; PTM: The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain. | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9694901}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:P20060}. | 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:11329289, ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}; CATALYTIC ACTIVITY: Rea... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4. {ECO:0000269|PubMed:11329289}; | null | FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme B does ... | Homo sapiens (Human) |
P07687 | HYEP_RAT | MWLELVLASLLGFVIYWFVSRDKEETLPLGDGWWGPGSKPSAKEDESIRPFKVETSDEEIKDLHQRIDRFRASPPLEGSRFHYGFNSNYMKKVVSYWRNEFDWRKQVEILNQYPHFKTKIEGLDIHFIHVKPPQLPSGRTPKPLLMVHGWPGSFYEFYKIIPLLTDPKSHGLSDEHVFEVICPSIPGYGYSEASSKKGLNSVATARIFYKLMTRLGFQKFYIQGGDWGSLICTNMAQMVPNHVKGLHLNMAFISRSFYTMTPLLGQRFGRFLGYTEKDIELLYPYKEKVFYSIMRESGYLHIQATKPDTVGCALNDSPVG... | 3.3.2.9 | null | arachidonic acid metabolic process [GO:0019369]; aromatic compound catabolic process [GO:0019439]; cellular aromatic compound metabolic process [GO:0006725]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to organic substance [GO:0071310]; diol biosynthetic process [GO:0034312]; epoxide me... | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | cis-stilbene-oxide hydrolase activity [GO:0033961]; enzyme binding [GO:0019899]; epoxide hydrolase activity [GO:0004301]; oxysterol binding [GO:0008142] | PF06441; | 3.40.50.1820; | Peptidase S33 family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9854022}; Single-pass type III membrane protein {ECO:0000269|PubMed:9245728}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000269|PubMed:9245728}. | CATALYTIC ACTIVITY: Reaction=cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin; Xref=Rhea:RHEA:23900, ChEBI:CHEBI:15377, ChEBI:CHEBI:50004, ChEBI:CHEBI:50014; EC=3.3.2.9; Evidence={ECO:0000269|PubMed:9854022}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23901; Evidence={ECO:0000305|PubMed:9854022}; CATALYTIC ACT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87.5 uM for styrene 7,8-oxide {ECO:0000269|PubMed:9854022}; KM=6.8 uM for 9,10-epoxystearic acid {ECO:0000269|PubMed:9854022}; Vmax=365 nmol/min/mg enzyme with styrene 7,8-oxide as substrate {ECO:0000269|PubMed:9854022}; Vmax=10 nmol/min/mg enzyme with 9,10-epoxyst... | null | null | null | FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water. May play a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids. Metabolizes the abundant endocannabinoid 2-... | Rattus norvegicus (Rat) |
P07688 | CATB_BOVIN | MWRLLATLSCLLVLTSARSSLYFPPLSDELVNFVNKQNTTWKAGHNFYNVDLSYVKKLCGAILGGPKLPQRDAFAADVVLPESFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHSNGRVNVEVSAEDMLTCCGGECGDGCNGGFPSGAWNFWTKKGLVSGGLYNSHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKTCEPGYSPSYKEDKHFGCSSYSVANNEKEIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVSGEIMGGHAIRILGWGVENGTPYWLVGNSWNTDWGDNGFFKILRGQDHCG... | 3.4.22.1 | null | proteolysis involved in protein catabolic process [GO:0051603] | apical plasma membrane [GO:0016324]; extracellular space [GO:0005615]; lysosome [GO:0005764]; melanosome [GO:0042470] | cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activity [GO:0004175] | PF00112;PF08127; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:1856234}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.; EC=3.4.... | null | null | null | null | FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:1856234). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also... | Bos taurus (Bovine) |
P07692 | ACES_TORMA | MREMNLLVTSSLGVLLHLVVLCQADDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIWVPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGESAGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRRNLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVI... | 3.1.1.7 | null | acetylcholine catabolic process in synaptic cleft [GO:0001507]; choline metabolic process [GO:0019695] | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202]; synaptic cleft [GO:0043083] | acetylcholinesterase activity [GO:0003990] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: An interchain disulfide bond is present in what becomes position 596 of the T isoform. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor. Synapse.; SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane protein. Synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane. | CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; | null | null | null | null | FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions. | Torpedo marmorata (Marbled electric ray) |
P07700 | ADRB1_MELGA | MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLV... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0002025]; positive regulation of heart rate by epinephrine-norepinephrine [GO:0001996]; regulation of circadian sleep/wake cycl... | early endosome [GO:0005769]; membrane [GO:0016020]; plasma membrane [GO:0005886] | beta1-adrenergic receptor activity [GO:0004940]; identical protein binding [GO:0042802] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB1 sub-subfamily | PTM: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early endosome {ECO:0000250}. Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity (PubMed:18594507). In dorsal pons neurons, involved in the regulation of sleep/wake behaviors (By s... | Meleagris gallopavo (Wild turkey) |
P07702 | LYS2_YEAST | MTNEKVWIEKLDNPTLSVLPHDFLRPQQEPYTKQATYSLQLPQLDVPHDSFSNKYAVALSVWAALIYRVTGDDDIVLYIANNKILRFNIQPTWSFNELYSTINNELNKLNSIEANFSFDELAEKIQSCQDLERTPQLFRLAFLENQDFKLDEFKHHLVDFALNLDTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITASSKDSLPDPTKNLGWCDFVGCIHDIFQDNAEAFPERTCVVETPTLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT... | 1.2.1.31; 1.2.1.95 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000269|PubMed:10320345}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000269|PubMed:10320345}; | lysine biosynthetic process via aminoadipic acid [GO:0019878] | cytoplasm [GO:0005737] | L-aminoadipate-semialdehyde dehydrogenase activity [GO:0004043]; phosphopantetheine binding [GO:0031177] | PF00501;PF07993;PF00550; | 3.30.300.30;1.10.1200.10;3.40.50.12780;3.40.50.720;3.30.559.30; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2-amino-6-oxohexanoate + H2O + NADP(+) = 2 H(+) + L-2-aminoadipate + NADPH; Xref=Rhea:RHEA:12304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349, ChEBI:CHEBI:58672; EC=1.2.1.31; Evidence={ECO:0000269|PubMed:10320345}; CATALYTIC ACTIVITY: Re... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=620 uM for NADPH {ECO:0000269|PubMed:10320345}; Note=kcat is 670 min(-1). {ECO:0000269|PubMed:10320345}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3. | null | null | FUNCTION: Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate. {ECO:0000269|PubMed:10320345... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07703 | RPAC1_YEAST | MSNIVGIEYNRVTNTTSTDFPGFSKDAENEWNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRRIMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVDPDMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKGSTDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPDILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLLPQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDARKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTPEEIFFKSVRI... | null | null | nucleolar large rRNA transcription by RNA polymerase I [GO:0042790]; ribosome biogenesis [GO:0042254]; termination of RNA polymerase I transcription [GO:0006363]; termination of RNA polymerase III transcription [GO:0006386]; transcription by RNA polymerase I [GO:0006360]; transcription by RNA polymerase III [GO:0006383... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; protein dimerization activity [GO:0046983]; RNA polymerase I activity [GO:0001054]; RNA polymerase III activity [GO:0001056] | PF01000;PF01193; | 2.170.120.12;3.30.1360.10; | Archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I (Pol I) and III (Pol III) which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPC40 is part o... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07711 | CATL1_HUMAN | MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRN... | 3.4.22.15 | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; c... | apical plasma membrane [GO:0016324]; chromaffin granule [GO:0042583]; collagen-containing extracellular matrix [GO:0062023]; endocytic vesicle lumen [GO:0071682]; endolysosome lumen [GO:0036021]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO... | collagen binding [GO:0005518]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; fibronectin binding [GO:0001968]; histone binding [GO:0042393]; proteoglycan binding [GO:0043394]; s... | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propepti... | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Se... | CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000269|PubMed:9468501}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5, also active at pH 7.0 with CUX1 as substrate. {ECO:0000269|PubMed:10716919, ECO:0000269|PubMed:15099520, ECO:0000269|PubMed:18562523, ECO:0000269|PubMed:9468501}; | null | FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of th... | Homo sapiens (Human) |
P07713 | DECA_DROME | MRAWLLLLAVLATFQTIVRVASTEDISQRFIAAIAPVAAHIPLASASGSGSGRSGSRSVGASTSTALAKAFNPFSEPASFSDSDKSHRSKTNKKPSKSDANRQFNEVHKPRTDQLENSKNKSKQLVNKPNHNKMAVKEQRSHHKKSHHHRSHQPKQASASTESHQSSSIESIFVEEPTLVLDREVASINVPANAKAIIAEQGPSTYSKEALIKDKLKPDPSTLVEIEKSLLSLFNMKRPPKIDRSKIIIPEPMKKLYAEIMGHELDSVNIPKPGLLTKSANTVRSFTHKDSKIDDRFPHHHRFRLHFDVKSIPADEKLKA... | null | null | amnioserosa formation [GO:0007378]; anterior Malpighian tubule development [GO:0061327]; BMP signaling pathway [GO:0030509]; cardioblast differentiation [GO:0010002]; cell chemotaxis involved in Malpighian tubule morphogenesis [GO:0061352]; chorion-containing eggshell formation [GO:0007304]; compound eye morphogenesis ... | cell leading edge [GO:0031252]; dense core granule lumen [GO:0098898]; extracellular space [GO:0005615] | BMP receptor binding [GO:0070700]; collagen binding [GO:0005518]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; morphogen activity [GO:0016015]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein serine/threonine... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11136981, ECO:0000269|PubMed:11136982, ECO:0000269|PubMed:1692958, ECO:0000269|PubMed:35037619}. Note=Is internalized by receptor-mediated endocytosis. | null | null | null | null | null | FUNCTION: Required during oogenesis for eggshell patterning and dorsal/ventral patterning of the embryo. Acts as a morphogen during embryogenesis to pattern the dorsal/ventral axis, specifying dorsal ectoderm and amnioserosa cell fate within the dorsal half of the embryo; this activity is antagonized by binding to sog ... | Drosophila melanogaster (Fruit fly) |
P07720 | POLG_TBEVS | MAGKAILKGKGGGPPRRVSKETAKKTRQSRVQMPNGLVLMRMMGILWHAVAGTARSPVLKSFWKSVPLKQATAALRKIKKAVSTLMVGLQRRGKRRSAVDWTGWLLVVVLLGVTLAATVRKERDGTTVIRAEGKDAATQVRVENGTCVILATDMGSWCDDSLTYECVTIDQGEEPVDVDCSCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGDLTGRGHKWLEGDSLRTHLTRVEGWVWKNKVLTLAVIAVVWLTVESVVTRVAVVVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbion... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Tick-borne encephalitis virus Far Eastern subtype (strain Sofjin) (SOFV) (Sofjin virus) |
P07722 | MAG_RAT | MIFLTTLPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIINTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAESLYLDLEEVTPAEDGIYACLAENAYGQDNRTVEL... | null | null | axon regeneration [GO:0031103]; cell adhesion [GO:0007155]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cellular response to mechanical stimulus [GO:0071260]; central nervous system myelin formation [GO:0032289]; central nervous system myelination [GO:0022010]; myelination [GO:0042552]; nega... | compact myelin [GO:0043218]; membrane raft [GO:0045121]; mesaxon [GO:0097453]; myelin sheath [GO:0043209]; myelin sheath adaxonal region [GO:0035749]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220] | carbohydrate binding [GO:0030246]; ganglioside GT1b binding [GO:1905576]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; sialic acid binding [GO:0033691]; signaling receptor binding [GO:0005102] | PF08205;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20916}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:16998591}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P20917}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16998591, ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:8995428, ECO:0000269|PubMed:9298990}; Single-pass type I membrane protein {ECO:0000269|PubMed:16998591, ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:9298990}. Membrane raft {ECO:0000269|PubMed:16998591}. | null | null | null | null | null | FUNCTION: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (PubMed:8995428, PubMed:9298990). Not required for initial myelination, but seems to play a role in the maintenance of normal... | Rattus norvegicus (Rat) |
P07724 | ALBU_MOUSE | MKWVTFLLLLFVSGSAFSRGVFRREAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHD... | null | null | cellular response to calcium ion starvation [GO:0072732]; cellular response to starvation [GO:0009267]; negative regulation of mitochondrial depolarization [GO:0051902]; positive regulation of circadian sleep/wake cycle, non-REM sleep [GO:0046010] | basement membrane [GO:0005604]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; myelin sheath [GO:0043209]; protein-containing complex [GO:... | DNA binding [GO:0003677]; enterobactin binding [GO:1903981]; enzyme binding [GO:0019899]; exogenous protein binding [GO:0140272]; fatty acid binding [GO:0005504]; identical protein binding [GO:0042802]; modified amino acid binding [GO:0072341]; oxygen binding [GO:0019825]; protein-folding chaperone binding [GO:0051087]... | PF00273; | 1.10.246.10; | ALB/AFP/VDB family | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02768}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds... | Mus musculus (Mouse) |
P07725 | CD8A_RAT | MASRVICFLSLNLLLLDVITRLQVSGQLQLSPKKVDAEIGQEVKLTCEVLRDTSQGCSWLFRNSSSELLQPTFIIYVSSSRSKLNDILDPNLFSARKENNKYILTLSKFSTKNQGYYFCSITSNSVMYFSPLVPVFQKVNSIITKPVTRAPTPVPPPTGTPRPLRPEACRPGASGSVEGMGLGFACDIYIWAPLAGICAVLLLSLVITLICCHRNRRRVCKCPRPLVKPRPSEKFV | null | null | calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; cytotoxic T cell differentiation [GO:0045065]; defense response to virus [GO:0051607]; positive regulation of calcium-mediated signaling [GO:0050850]; T cell activation [GO:0042110]; T cell mediated immunity [GO:0002456]; T c... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; receptor complex [GO:0043235] | identical protein binding [GO:0042802]; MHC class I protein complex binding [GO:0023024]; protein kinase binding [GO:0019901] | PF07686; | 2.60.40.10; | null | PTM: Palmitoylated, but association with CD8B seems to be more important for the enrichment of CD8A in lipid rafts. {ECO:0000250|UniProtKB:P01732}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:P01732}.; PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following activation. {ECO:0000250|UniProtKB:P01732}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01732}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01732}. Note=CD8A localizes to lipid rafts only when associated with its partner CD8B. {ECO:0000250|UniProtKB:P01732}. | null | null | null | null | null | FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are de... | Rattus norvegicus (Rat) |
P07727 | GLRA1_RAT | MYSFNTLRFYLWETIVFFSLAASKEADAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLL... | null | null | acrosome reaction [GO:0007340]; adult walking behavior [GO:0007628]; cellular response to amino acid stimulus [GO:0071230]; cellular response to ethanol [GO:0071361]; cellular response to zinc ion [GO:0071294]; chemical synaptic transmission [GO:0007268]; chemical synaptic transmission, postsynaptic [GO:0099565]; chlor... | calyx of Held [GO:0044305]; chloride channel complex [GO:0034707]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; glycinergic synapse [GO:0098690]; inhibitory synapse [GO:0060077]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; ne... | extracellularly glycine-gated chloride channel activity [GO:0016934]; extracellularly glycine-gated ion channel activity [GO:0016933]; glycine binding [GO:0016594]; identical protein binding [GO:0042802]; ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099507];... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Glycine receptor (TC 1.A.9.3) subfamily, GLRA1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:6286620}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000269|PubMed:6286620}. Perikaryon {ECO:0000250|UniProtKB:Q64018}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q64018}. Cell membrane {ECO:0000269|PubMed:11981023... | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11981023, ECO:0000269|PubMed:1716350, ECO:0000269|PubMed:2483325, ECO:0000269|PubMed:3037383}; | null | null | null | null | FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:11981023, PubMed:1716350, PubMed:2483325, PubMed:3037383). Channel opening is also triggered by taurine and beta-alanine (PubMed:1716350). Channel characteristics depend on the subunit compositi... | Rattus norvegicus (Rat) |
P07732 | GTHB2_ONCTS | MLGLHVGTLISLFLCILLEPIEGSLMQPCQPINQTVSLEKEGCPTCLVIRAPICSGHCVTKEPVFKSPFSTVYQHVCTYRDVRYEMIRLPDCPPWSDPHVTYPVALSCDCSLCNMDTSDCTIESLQPDFCITQRVLTDGDMW | null | null | androstenedione secretion [GO:0035941]; G protein-coupled receptor signaling pathway [GO:0007186]; ovulation [GO:0030728]; progesterone secretion [GO:0042701]; testosterone biosynthetic process [GO:0061370]; testosterone secretion [GO:0035936] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | hormone activity [GO:0005179] | PF00007; | 2.10.90.10; | Glycoprotein hormones subunit beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Involved in gametogenesis and steroidogenesis. | Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha) |
P07735 | GPDA_DROVI | MAEKVNVCIVGSGNWGSAIAKIVGANAAALPEFEERVTMFVYEEMIDGKKLTEIINETHENVKYLKGHKLPTNVVAVPDLVEAAKNADILIFVVPHQFIPNFCKQLLGKIKPNAIAISLIKGFDKAEGGGIDLISHIITRHLKIPCAVLMGANLANEVAEGNFCETTIGCTDKKYGKVLRDLFQANHFRVVVVEDADAVEVCGALKNIVACGAGFVDGLKLGDNTKAAVIRLGLMEMIRFVDVFYPGSKLSTFFESCGVADLITTCYGGRNRRVSEAFVTSGKTIEDLEKEMLNGQKLQGPPTAEEVNYMLKNKGLEDKF... | 1.1.1.8 | null | carbohydrate metabolic process [GO:0005975]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerophospholipid metabolic process [GO:0006650]; NADH oxidation [GO:0006116] | cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]; nucleus [GO:0005634] | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF07479;PF01210; | 3.40.50.720; | NAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; | null | PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle. | null | null | null | Drosophila virilis (Fruit fly) |
P07737 | PROF1_HUMAN | MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY | null | null | actin cytoskeleton organization [GO:0030036]; modification of postsynaptic actin cytoskeleton [GO:0098885]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of actin filament bundle assembly [GO:0032232]; negative regulation of actin filament polymerization [GO:0030837]; negative regulatio... | blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; nucleus [GO:0005634] | actin binding [GO:0003779]; actin monomer binding [GO:0003785]; adenyl-nucleotide exchange factor activity [GO:0000774]; cadherin binding [GO:0045296]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphotyrosine residue binding [GO:0001784]; proline-rich region binding [GO:0070064]; RNA binding [GO:0003... | PF00235; | 3.30.450.30; | Profilin family | PTM: Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation. {ECO:0000269|PubMed:18573880}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-a... | Homo sapiens (Human) |
P07738 | PMGE_HUMAN | MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK | 5.4.2.11; 5.4.2.4 | null | carbohydrate derivative catabolic process [GO:1901136]; carbohydrate metabolic process [GO:0005975]; defense response to protozoan [GO:0042832]; erythrocyte development [GO:0048821]; establishment of blood-brain barrier [GO:0060856]; glycolytic process [GO:0006096]; neuroinflammatory response [GO:0150076]; oxygen trans... | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | PTM: Glycation of Lys-159 in diabetic patients inactivates the enzyme. | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4; Evidence={ECO:0000269|PubMed:21045285}; CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=R... | null | null | null | null | FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. {ECO:0000269|PubMed:21045285}. | Homo sapiens (Human) |
P07741 | APT_HUMAN | MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE | 2.4.2.7 | null | adenine salvage [GO:0006168]; AMP salvage [GO:0044209]; GMP salvage [GO:0032263]; grooming behavior [GO:0007625]; IMP salvage [GO:0032264]; purine ribonucleoside salvage [GO:0006166] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; secretory granule lumen [GO:0034774] | adenine binding [GO:0002055]; adenine phosphoribosyltransferase activity [GO:0003999]; AMP binding [GO:0016208] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7; Evidence={ECO:0000269|PubMed:15196008}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.9 uM for 5-phospho-alpha-D-ribose 1-diphosphate {ECO:0000269|PubMed:15196008}; KM=4 uM for adenine {ECO:0000269|PubMed:15196008}; | PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. {ECO:0000269|PubMed:15196008}. | null | null | FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. {ECO:0000269|PubMed:15196008}. | Homo sapiens (Human) |
P07742 | RIR1_MOUSE | MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGRHSPMVASSTLDIVMANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSEKWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGK... | 1.17.4.1 | null | 2'-deoxyribonucleotide biosynthetic process [GO:0009265]; cell proliferation in forebrain [GO:0021846]; deoxyribonucleotide biosynthetic process [GO:0009263]; DNA repair [GO:0006281]; DNA synthesis involved in DNA repair [GO:0000731]; male gonad development [GO:0008584]; mitochondrial DNA replication [GO:0006264]; posi... | cell projection [GO:0042995]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; ribonucleoside-diphosphate reductase complex [GO:0005971] | ATP binding [GO:0005524]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; purine nucleotide binding [GO:0017076]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748] | PF03477;PF02867;PF00317; | 3.20.70.20; | Ribonucleoside diphosphate reductase large chain family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;... | null | null | null | null | FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Mus musculus (Mouse) |
P07744 | K2C4_MOUSE | MIARQSSVRGASRGFSSGSAIAGGVKRVAFSSGSMSGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGAGFGAGGFGGGFGGSFNGRGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEV... | null | null | epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; negative regulation of epithelial cell proliferation [GO:0050680] | cell surface [GO:0009986]; extracellular space [GO:0005615]; keratin filament [GO:0045095] | structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | null | null | null | null | null | null | null | Mus musculus (Mouse) |
P07750 | IL4_MOUSE | MGLNPQLVVILLFFLECTRSHIHGCDKNHLREIIGILNEVTGEGTPCTEMDVPNVLTATKNTTESELVCRASKVLRIFYLKHGKTPCLKKNSSVLMELQRLFRAFRCLDSSISCTMNESKSTSLKDFLESLKSIMQMDYS | null | null | activated T cell proliferation [GO:0050798]; autophagy [GO:0006914]; B cell activation [GO:0042113]; B cell costimulation [GO:0031296]; B cell proliferation [GO:0042100]; cholesterol metabolic process [GO:0008203]; defense response to protozoan [GO:0042832]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-4 receptor binding [GO:0005136] | PF00727; | 1.20.1250.10; | IL-4/IL-13 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:3083412). Induces the expression of class II MHC molecules on resting B-cells (PubMed:349... | Mus musculus (Mouse) |
P07751 | SPTN1_CHICK | MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSSLRRQKLEDSYRFQFFQRDADELGKWIQEKLQIASDENYKDPSNLQGKLQKHQAFEAEVQANSGAIVKLDETGNQMINEGHFASETIRTRLQELHRLWELLLEKMREKGVKLLQAQKLVQFLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDLAAHEERVNEVNQFAGKLIQEQHPEEELIKSKQDEVNASWQRLKGLAQQRQGKLFGAAEVQRFNRDVDETISWIKEKGQLMASDDFGRDLASVQALLRKHEGLERDLAAFHHKVKALCAEADR... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693] | cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; costamere [GO:0043034]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516] | PF13499;PF08726;PF00018;PF00435; | 1.20.5.170;1.20.58.60;1.10.238.10;2.30.30.40; | Spectrin family | PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. | null | null | null | null | null | FUNCTION: Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane orga... | Gallus gallus (Chicken) |
P07752 | ALF_TRYBB | MSKRVEVLLTQLPAYNRLKTPYEAELIETAKKMTAPGKGLLAADESTGSCSKRFAGIGLSNTAEHRRQYRALMLECEGFEQYISGVILHDETVYQKAKTGETFPQYLRRRGVVPGIKTDCGLEPLVEGAKGEQMTAGLDGYIKRAKKYYAMGCRFCKWRNVYKIQNGTVSEAVVRFNAETLARYAILSQLCGLVPIVEPEVMIDGTHDIETCQRVSQHVWSEVVSALHRHGVVWEGCLLKPNMVVPGAESGLKGHAEQVAEYTVKTLARVIPPALPGVTFLSGGLSEVMASEYLNAMNNCPLPRPWKLTFSYARALQSSA... | 4.1.2.13 | null | fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; glycosome [GO:0020015] | fructose-bisphosphate aldolase activity [GO:0004332] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Glycosome. | 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; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | null | Trypanosoma brucei brucei |
P07753 | PSBA_CHLRE | MTAILERRENSSLWARFCEWITSTENRLYIGWFGVIMIPCLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIITGAVIPTSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVCHFLLGVYCYMGREWELSFRLGMRPWIAVAYSAPVAAASAVFLVYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFTALGLSTMAFNLNGFNFNQSVVDSQGRVLNTWADI... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; | null | null | null | null | FUNCTION: This is one of the two reaction center proteins of photosystem II.; FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core ant... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P07756 | CPSM_RAT | MTRILTACKVVKTLKSGFGLANVTSKRQWDFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDTTARDELGLNKYMESDGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDFVDPNKQNLIAEVSTKDVKVFGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQMDYDGLLIAGGPGNPALAQPLIQNVKKILESDRKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQ... | 6.3.4.16 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; carbamoyl phosphate biosynthetic process [GO:0070409]; cellular response to ammonium ion [GO:0071242]; cellular response to cAMP [GO:0071320]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to glucagon stimulus [G... | cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; endopeptidase activity [GO:0004175]; glutamate binding [GO:0016595]; metal ion binding [GO:0046872]; modified amino acid b... | PF02786;PF02787;PF00988;PF00117;PF02142; | 3.40.50.20;3.40.50.880;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.40.50.1380; | null | PTM: 50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded. Undergoes proteolytic cleavage in the C-terminal region corr... | SUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleolus {ECO:0000250|UniProtKB:P31327}. Cell membrane {ECO:0000250|UniProtKB:Q8C196}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:Q8C196}. Note=Localizes to the cell surface of hepatocytes. {ECO:0000250|UniProtKB:Q8C196}. | CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000269|PubMed:197544... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.06 mM for ATP {ECO:0000269|PubMed:19754428}; KM=6.43 mM for HCO(3)(-) {ECO:0000269|PubMed:19754428}; KM=1.07 mM for NH(4)(+) {ECO:0000269|PubMed:19754428}; Note=The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.; | null | null | null | FUNCTION: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. | Rattus norvegicus (Rat) |
P07758 | A1AT1_MOUSE | MTPSISWGLLLLAGLCCLVPSFLAEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTL... | null | null | acute-phase response [GO:0006953]; protein N-linked glycosylation [GO:0006487]; response to chromate [GO:0046687]; response to cytokine [GO:0034097]; response to lead ion [GO:0010288]; response to methanol [GO:0033986]; response to peptide hormone [GO:0043434] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10;2.10.310.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. | null | null | null | null | null | FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. | Mus musculus (Mouse) |
P07759 | SPA3K_MOUSE | MAFIVAMGMILMAGICPAVLCFPDGTKEMDIVFHEHQDNGTQDDSLTLASVNTDFAFSLYKKLALKNPDTNIVFSPLSISAALALVSLGAKGKTMEEILEGLKFNLTETPEADIHQGFGNLLQSLSQPEDQDQINIGNAMFIEKDLQILAEFHEKTRALYQTEAFTADFQQPTEAKNLINDYVSNQTQGMIKELISELDERTLMVLVNYIYFKGKWKISFDPQDTFESEFYLDEKRSVKVPMMKMKLLTTRHFRDEELSCSVLELKYTGNASALLILPDQGRMQQVEASLQPETLRKWRKTLFPSQIEELNLPKFSIASN... | null | null | response to cytokine [GO:0034097]; response to peptide hormone [GO:0043434] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Contrapsin inhibits trypsin-like proteases. {ECO:0000269|PubMed:6214866, ECO:0000269|PubMed:6224776}. | Mus musculus (Mouse) |
P07764 | ALF_DROME | MTTYFNYPSKELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAKKNTPEEIALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENI... | 4.1.2.13 | null | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycolytic process [GO:0006096]; mesoderm development [GO:0007498] | cytosol [GO:0005829]; M band [GO:0031430]; Z disc [GO:0030018] | fructose-bisphosphate aldolase activity [GO:0004332] | PF00274; | 3.20.20.70; | Class I 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:8537310}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-7.8 for isozyme alpha, and 7.2-7.5 for isozymes beta and gamma. {ECO:0000269|PubMed:8537310}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostability of the isozymes, calculated as the temperature causing half maximal stability, is 42-43 degrees Celsius for isozymes alpha and beta and 45 degrees Celsius for isozyme gamma. {ECO:0000269|PubMed:8537310}; | FUNCTION: May take part in developmental stage-specific or tissue -specific sugar-phosphate metabolisms. Protein acts on two substrates fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I aldolases). {ECO:0000269|PubMed:8537310}. | Drosophila melanogaster (Fruit fly) |
P07766 | CD3E_HUMAN | MQSGTHWRVLGLCLLSVGVWGQDGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRRI | null | null | adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; apoptotic signaling pathway [GO:0097190]; calcium-mediated signaling [GO:0019722]; CD4-positive, alpha-beta T cell proliferation [GO:0035739]; cell surface receptor signaling pathway [GO:0007166]; cerebellum development [GO:0021549]; dend... | alpha-beta T cell receptor complex [GO:0042105]; cell body [GO:0044297]; cell-cell junction [GO:0005911]; dendritic spine [GO:0043197]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; gamma-delta T cell receptor complex [GO:0042106]; Golgi apparatus [GO:0005794]; immunological synapse... | identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; signaling receptor complex adaptor activity [GO:0030159]; T cell receptor binding [GO:0042608]; transmembrane signaling receptor activity [GO:0004888] | PF16681;PF02189; | 2.60.40.10; | null | PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000269|PubMed:2470098}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10384095, ECO:0000269|PubMed:15294938}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... | Homo sapiens (Human) |
P07768 | SUIS_RABIT | MAKRKFSGLEITLIVLFVIVFIIAIALIAVLATKTPAVEEVNPSSSTPTTTSTTTSTSGSVSCPSELNEVVNERINCIPEQSPTQAICAQRNCCWRPWNNSDIPWCFFVDNHGYNVEGMTTTSTGLEARLNRKSTPTLFGNDINNVLLTTESQTANRLRFKLTDPNNKRYEVPHQFVTEFAGPAATETLYDVQVTENPFSIKVIRKSNNRILFDSSIGPLVYSDQYLQISTRLPSEYMYGFGEHVHKRFRHDLYWKTWPIFTRDQHTDDNNNNLYGHQTFFMCIEDTTGKSFGVFLMNSNAMEIFIQPTPIVTYRVIGGI... | 3.2.1.10; 3.2.1.48 | null | carbohydrate metabolic process [GO:0005975] | apical plasma membrane [GO:0016324] | alpha-1,4-glucosidase activity [GO:0004558]; carbohydrate binding [GO:0030246]; oligo-1,6-glucosidase activity [GO:0004574]; sucrose alpha-glucosidase activity [GO:0004575] | PF13802;PF01055;PF21365;PF00088; | 3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10; | Glycosyl hydrolase 31 family | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.; PTM: N- and O-glycosylated.; PTM: Sulfated. {ECO:0000250}. | SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.; EC=3.2.1.48; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; | null | null | null | null | FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. | Oryctolagus cuniculus (Rabbit) |
P07788 | COTA_BACSU | MTLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGYNGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSDSQHEEPEVKTVVHLHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHAMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSLFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVINASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDFTAYEGESIILANSA... | 1.10.3.2; 1.3.3.5 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:11514528, ECO:0000269|PubMed:11884407, ECO:0000269|PubMed:12198312, ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:20200715}; Note=Binds 4 copper ions per subunit. The 4 copper centers adopt structures classified as type 1, type 2 and type 3. ... | sporulation resulting in formation of a cellular spore [GO:0030435] | outer membrane-bounded periplasmic space [GO:0030288] | copper ion binding [GO:0005507]; oxidoreductase activity [GO:0016491] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Spore coat {ECO:0000269|PubMed:11884407, ECO:0000269|PubMed:2821284}. Note=Localized to the surface layers of the endospore. {ECO:0000269|PubMed:11884407}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:11514528, ECO:0000269|PubMed:11884407, ECO:0000269|PubMed:18307408, ECO:0000269|PubMed:20200715, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=106 uM for ABTS {ECO:0000269|PubMed:11884407}; KM=124 uM for ABTS {ECO:0000269|PubMed:18307408}; KM=120 uM for ABTS {ECO:0000269|PubMed:22481612}; KM=26 uM for SGZ {ECO:0000269|PubMed:11884407}; KM=18 uM for SGZ {ECO:0000269|PubMed:18307408}; KM=227 uM for 2,6-DMP ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 for SGZ and bilirubin oxidation (PubMed:11514528, PubMed:11884407, PubMed:16391148). Optimum pH is about 4 for ditaurobilirubin oxidation (PubMed:16391148). Optimum pH is below 3.0 for ABTS oxidation (PubMed:11884407). Optimum pH is 8.0 for UB oxidation, wh... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable (PubMed:11884407, PubMed:16391148). Optimum temperature is 45 degrees Celsius for SGZ oxidation (PubMed:11514528). Optimum temperature is 75 degrees Celsius with ABTS as substrate (PubMed:11884407). {ECO:0000269|PubMed:11514528, ECO:0000269|Pub... | FUNCTION: Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds. Substrates include syringaldazine (SGZ), 2,6-dimethoxyphenol (2,6-DMP) and the non-phenolic compound 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:11514528, PubMe... | Bacillus subtilis (strain 168) |
P07799 | TOP1_SCHPO | MSSSDSDSVSLSIRRRQRRGSSKRISMKESDEESDSSENHPLSESLNKKSKSESDEDDIPIRKRRASSKKNMSNSSSKKRAKVMGNGGLKNGKKTAVVKEEEDFNEIAKPSPKHKRVSKANGSKNGAKSAVKKEESDTDDSVPLRAVSTVSLTPYKSELPSGASTTQNRSPNDEEDEDEDYKWWTSENIDDTQKWTTLEHNGVIFAPPYEPLPKNVKLIYDGNPVNLPPEAEEVAGFYAAMLETDHAKNPVFQDNFFRDFLKVCDECNFNHNIKEFSKCDFTQMFHHFEQKREEKKSMPKEQKKAIKQKKDEEEEKYKWC... | 5.6.2.1 | null | chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; DNA topological change [GO:0006265]; mitotic chromosome condensation [GO:0007076] | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917] | PF14370;PF01028;PF02919; | 1.10.132.10;2.170.11.10;1.10.10.41; | Type IB topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P07800 | CHEZ_SALTY | MMQPSIKPADEGSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLDYVVQMTAQAAERALNSVEASQPHQDAMEKEAKALTQRWDEWFDNPIELSDARELVTDTRQFLRDVPGHTSFTNAQLLDIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQSARPKRENESLLNGPQVDTSKAGVVASQDQVDDLLDSLGF | 3.1.3.- | null | archaeal or bacterial-type flagellum-dependent cell motility [GO:0097588]; chemotaxis [GO:0006935]; regulation of chemotaxis [GO:0050920] | bacterial-type flagellum [GO:0009288]; cytoplasm [GO:0005737] | phosphoprotein phosphatase activity [GO:0004721] | PF04344; | 1.10.287.500;1.20.5.590; | CheZ family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P. {ECO:0000269|PubMed:14636076, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:8399392, ECO:0000269|PubMed:8816756, ECO:0000269|PubMed:9837737}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P07802 | KAP0_PIG | MASGSTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKASARADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGNDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPS... | null | null | regulation of meiotic cell cycle process involved in oocyte maturation [GO:1903538]; regulation of protein phosphorylation [GO:0001932] | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000250}. | Sus scrofa (Pig) |
P07805 | DCOR_TRYBB | MDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGV... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10563800, ECO:0000269|PubMed:10985770, ECO:0000269|PubMed:15476392}; | polyamine biosynthetic process [GO:0006596]; putrescine biosynthetic process from ornithine [GO:0033387] | cytoplasm [GO:0005737] | ornithine decarboxylase activity [GO:0004586] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000269|PubMed:10985770}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=400 uM for L-ornithine {ECO:0000269|PubMed:10985770}; Note=kcat is 15 sec(-1) with L-ornithine as substrate. {ECO:0000269|PubMed:10985770}; | PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000305|PubMed:3036823}. | null | null | FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.... | Trypanosoma brucei brucei |
P07808 | NPY_RAT | MMLGNKRMGLCGLTLALSLLVCLGILAEGYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENAPRTRLEDPSMW | null | null | adult feeding behavior [GO:0008343]; central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; chemical synaptic transmission [GO:0007268]; feeding behavior [GO:0007631]; monocyte activation [GO:0042117]; negative regulation of acute inflammatory response to antigenic stimulus [G... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; neuronal dense core vesicle [GO:0098992]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; terminal bouton [GO:0043195] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]; neuropeptide Y receptor binding [GO:0031841] | PF00159; | 6.10.250.900; | NPY family | PTM: The neuropeptide Y form is cleaved at Pro-31 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000250|UniProtKB:P01303}. | SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165}. | null | null | null | null | null | FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. | Rattus norvegicus (Rat) |
P07812 | PRGR_CHICK | MTEVKSKETRAPSSARDGAVLLQAPPSRGEAEGIDVALDGLLYPRSSDEEEEEEENEEEEEEEEPQQREEEEEEEEEDRDCPSYRPGGGSLSKDCLDSVLDTFLAPAAHAAPWSLFGPEVPEVPVAPMSRGPEQKAVDAGPGAPGPSQPRPGAPLWPGADSLNVAVKARPGPEDASENRAPGLPGAEERGFPERDAGPGEGGLAPAAAASPAAVEPGAGQDYLHVPILPLNSAFLASRTRQLLDVEAAYDGSAFGPRSSPSVPAADLAEYGYPPPDGKEGPFAYGEFQSALKIKEEGVGLPAAPPPFLGAKAAPADFAQP... | 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:00423... | chromatin [GO:0000785]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-DNA complex [GO:0032993]; receptor complex [GO:0043235] | ATPase binding [GO:0051117]; chromatin DNA binding [GO:0031490]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; estrogen response element binding [GO:0034056]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; identical protein b... | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylation of Ser-529 is sharply increased upon progesterone treatment, whereas phosphorylation of Ser-210 and Ser-259 is modestly induced by progesterone. {ECO:0000269|PubMed:2398063, ECO:0000269|PubMed:7877616, ECO:0000269|PubMed:8662804}.; PTM: Ubiquitinated. Ubiquitination is increased by progesterone and... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:9808061}. Cytoplasm {ECO:0000269|PubMed:9808061}. 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. | Gallus gallus (Chicken) |
P07814 | SYEP_HUMAN | MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNL... | 6.1.1.15; 6.1.1.17 | null | cellular response to insulin stimulus [GO:0032869]; cellular response to type II interferon [GO:0071346]; glutamyl-tRNA aminoacylation [GO:0006424]; negative regulation of translation [GO:0017148]; prolyl-tRNA aminoacylation [GO:0006433]; regulation of long-chain fatty acid import into cell [GO:0140212]; tRNA aminoacyl... | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904] | ATP binding [GO:0005524]; glutamate-tRNA ligase activity [GO:0004818]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; proline-tRNA ligase activity [GO:0004827]; protein homodimerization activity [GO:0042803]; RNA stem-loop binding [GO:0035613]; zinc ion binding [GO:0008270] | PF03129;PF09180;PF00749;PF03950;PF20974;PF00587;PF00458; | 1.20.1050.130;3.40.50.800;3.30.110.30;3.40.50.620;1.10.287.10; | Class-I aminoacyl-tRNA synthetase family, Glutamate--tRNA ligase type 2 subfamily; Class-II aminoacyl-tRNA synthetase family | PTM: Phosphorylated at Ser-886 by CDK5 (PubMed:19647514, PubMed:21220307). Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS1 release from the aminoacyl-tRNA synthetase multienzyme complex (PubMed:19647514, PubMed:21220307, PubMed:28178239). In monocytes, the IFN-gamma-induced sequential phosphorylation at Ser-886 an... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:3290852}. Membrane {ECO:0000269|PubMed:28178239}; Peripheral membrane protein {ECO:0000305|PubMed:19289464, ECO:0000305|PubMed:28178239}. Note=Translocates from cytosol to membranes upon phosphorylatio... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000269|Pub... | null | null | null | null | FUNCTION: Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activa... | Homo sapiens (Human) |
P07821 | FHUC_ECOLI | MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLSLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAPVSFVY | 7.2.2.16 | null | iron ion import across plasma membrane [GO:0098711] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; plasma membrane [GO:0005886] | ABC-type ferric hydroxamate transporter activity [GO:0015625]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ferric iron transmembrane transporter activity [GO:0015091] | PF00005; | 3.40.50.300; | ABC transporter superfamily, Iron (Fe3+)-hydroxamate importer (TC 3.A.1.14.7) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1551849}; Peripheral membrane protein {ECO:0000269|PubMed:1551849}. Note=FhuB mediates the association of FhuC with the cytoplasmic membrane. {ECO:0000269|PubMed:1551849}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Fe(3+)-hydroxamate complex-[hydroxamate-binding protein]Side 1 = ADP + phosphate + Fe(3+)-hydroxamate complexSide 2 + [hydroxamate-binding protein]Side 1.; EC=7.2.2.16; Evidence={ECO:0000269|PubMed:1551849, ECO:0000269|PubMed:34887516}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.69 mM for ATP using FhuCB complex {ECO:0000269|PubMed:34887516}; KM=0.74 mM for ATP using FhuCB complex with enclosed FhuD {ECO:0000269|PubMed:34887516}; KM=0.77 mM for ATP using FhuCB complex with enclosed ferrichrome-loaded FhuD {ECO:0000269|PubMed:34887516}; V... | null | null | null | FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system. {ECO:0000269|PubMed:1551849, ECO:0000269|PubMed:34887516}. | Escherichia coli (strain K12) |
P07822 | FHUD_ECOLI | MSGLPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGKA | null | null | iron ion import across plasma membrane [GO:0098711] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; outer membrane-bounded periplasmic space [GO:0030288] | null | PF01497; | 3.40.50.1980; | Bacterial solute-binding protein 8 family | PTM: Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system. {ECO:0000269|PubMed:17218314}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17218314}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobacti... | Escherichia coli (strain K12) |
P07823 | BIP_MESAU | MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSE... | 3.6.4.10 | null | endoplasmic reticulum unfolded protein response [GO:0030968]; maintenance of protein localization in endoplasmic reticulum [GO:0035437]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of protein-containing complex assembly [GO:0031333]; positive regulation of cell migra... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; protein domain specific binding [GO:0019904] | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activi... | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epi... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:G3I8R9}; | null | null | null | null | FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC... | Mesocricetus auratus (Golden hamster) |
P07824 | ARGI1_RAT | MSSKPKPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFGTKREGNHKPETDYLK... | 3.5.3.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637}; Note=Binds 2 manganese ions per subunit. {ECO:000025... | adaptive immune response [GO:0002250]; arginine catabolic process to ornithine [GO:0019547]; arginine metabolic process [GO:0006525]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucagon stimulus [GO:0071377]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to i... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | arginase activity [GO:0004053]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145] | PF00491; | 3.40.800.10; | Arginase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05089}. Cytoplasmic granule {ECO:0000250|UniProtKB:P05089}. | CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:16266687}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for arginine {ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:16266687}; | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}. | null | null | FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a l... | Rattus norvegicus (Rat) |
P07825 | SYPH_RAT | MDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYTGELRLSVECANKTESALNIEVEFEYPFRLHQVYFDAPSCVKGGTTKIFLVGDYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMMDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPMCRQTGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFMRAPPGAPEKQPAPGDAYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPASGGGGYGPQGDYGQQGYGQQGAPTSFSNQM | null | null | cellular response to organic substance [GO:0071310]; endocytosis [GO:0006897]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of opioid receptor signaling pathway [GO:2000474]; regulation of short-term neuronal synaptic plasticity [... | excitatory synapse [GO:0060076]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; neuron projection terminus [GO:0044306]; neuron spine [GO:0044309]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zo... | cholesterol binding [GO:0015485]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; SH2 domain binding [GO:0042169]; SNARE binding [GO:0000149]; syntaxin-1 binding [GO:0017075] | PF01284; | null | Synaptophysin/synaptobrevin family | PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.; PTM: Phosphorylated by SRC. {ECO:0000269|PubMed:26026271}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62277}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:P08247}. | null | null | null | null | null | FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P07829 | ACT3_DICDI | MESEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRYTGVMVGMGQKDSYIGDEAQSRKGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYSLPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAELQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYSNVVLSGGSTMFPGIADRMNKELTA... | 3.6.4.- | null | cell morphogenesis [GO:0000902]; phagocytosis [GO:0006909]; plasma membrane repair [GO:0001778]; response to cAMP [GO:0051591] | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell pole [GO:0060187]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; early phagosome [GO:0032009]; intranuclear rod [GO:0061836]; lamellipodium [GO:0030027]; phagocytic cup [GO:0001891]; phagocytic v... | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; myosin binding [GO:0017022]; structural constituent of cytoskeleton [GO:0005200] | PF00022; | 3.30.420.40; | Actin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. | Dictyostelium discoideum (Social amoeba) |
P07830 | ACT1_DICDI | MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTA... | 3.6.4.- | null | cell morphogenesis [GO:0000902]; chemotaxis [GO:0006935]; endocytosis [GO:0006897]; hyperosmotic response [GO:0006972]; mitotic cytokinesis [GO:0000281]; phagocytosis [GO:0006909]; phototaxis [GO:0042331]; plasma membrane repair [GO:0001778]; response to cAMP [GO:0051591]; vesicle-mediated transport [GO:0016192] | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell pole [GO:0060187]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; early phagosome [GO:0032009]; endocytic vesicle [GO:0030139]; intranuclear rod [GO:0061836]; lamellip... | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; myosin binding [GO:0017022]; structural constituent of cytoskeleton [GO:0005200] | PF00022; | 3.30.420.40; | Actin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. | Dictyostelium discoideum (Social amoeba) |
P07833 | HGXR_PLAFK | MPIPNNPGAGENAFDPVFVKDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVEMSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL | 2.4.2.22; 2.4.2.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein. {ECO:0000250}; | GMP salvage [GO:0032263]; guanine salvage [GO:0006178]; hypoxanthine metabolic process [GO:0046100]; IMP salvage [GO:0032264]; purine ribonucleoside salvage [GO:0006166]; XMP salvage [GO:0032265] | cytosol [GO:0005829] | guanine phosphoribosyltransferase activity [GO:0052657]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; xanthine phosphoribosyltransferase activity [GO:0000310] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000250|UniProtKB:Q26997}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; Evide... | null | PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1.; PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.; PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1. | null | null | FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or xanthine, leading to IMP, GMP and XMP, respectively. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. {ECO:0000250|UniProtKB:Q26997}. | Plasmodium falciparum (isolate K1 / Thailand) |
P07834 | CDC4_YEAST | MGSFPLAEFPLRDIPVPYSYRVSGGIASSGSVTALVTAAGTHRNSSTAKTVETEDGEEDIDEYQRKRAAGSGESTPERSDFKRVKHDNHKTLHPVNLQNTGAASVDNDGLHNLTDISNDAEKLLMSVDDGSAAPSTLSVNMGVASHNVAAPTTVNAATITGSDVSNNVNSATINNPMEEGALPLSPTASSPGTTTPLAKTTKTINNNNNIADLIESKDSIISPEYLSDEIFSAINNNLPHAYFKNLLFRLVANMDRSELSDLGTLIKDNLKRDLITSLPFEISLKIFNYLQFEDIINSLGVSQNWNKIIRKSTSLWKKLL... | null | null | cell division [GO:0051301]; endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000472]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transiti... | 90S preribosome [GO:0030686]; nuclear matrix [GO:0016363]; nuclear SCF ubiquitin ligase complex [GO:0043224]; nucleolus [GO:0005730]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | phosphoserine residue binding [GO:0050815]; U3 snoRNA binding [GO:0034511]; ubiquitin binding [GO:0043130] | PF16856;PF12937;PF00400; | 1.20.1280.50;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11080155}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07845 | ACTP2_STIHL | ALAGTIIAGASLTFQVLDKVLEELGKVSRKIAVGIDNESGGTWTALNAYFRSGTTDVILPEFVPNTKALLYSGRKDTGPVATGAVAAFAYYMSSGNTLGVMFSVPFDYNWYSNWWDVKIYSGKRRADQGMYEDLYYGNPYRGDNGWHEKNLGYGLRMKGIMTSAGEAKMQIKISR | null | null | cytolysis in another organism [GO:0051715]; monoatomic cation transport [GO:0006812]; pore complex assembly [GO:0046931] | extracellular region [GO:0005576]; nematocyst [GO:0042151]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930] | channel activity [GO:0015267]; identical protein binding [GO:0042802]; toxin activity [GO:0090729] | PF06369; | 2.60.270.20; | Actinoporin family, Sea anemone subfamily | null | SUBCELLULAR LOCATION: Secreted. Nematocyst {ECO:0000269|PubMed:16432881}. Target cell membrane {ECO:0000269|PubMed:17573423}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000269|PubMed:17573423}. | null | null | null | null | null | FUNCTION: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and ... | Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus) |
P07846 | DHSO_SHEEP | AKPAAENLSLVVHGPGDLRLENYPIPEPGPNEVLLKMHSVGICGSDVHYWQGRIGDFVVKKPMVLGHEASGTVVKVGSLVRHLQPGDRVAIQPGAPRQTDEFCKIGRYNLSPTIFFCATPPDDGNLCRFYKHNANFCYKLPDNVTFEEGALIEPLSVGIHACRRAGVTLGNKVLVCGAGPIGLVNLLAAKAMGAAQVVVTDLSASRLSKAKEVGADFILEISNESPEEIAKKVEGLLGSKPEVTIECTGVETSIQAGIYATHSGGTLVLVGLGSEMTSVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVT... | 1.1.1.-; 1.1.1.14; 1.1.1.9 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21543846}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21543846}; | flagellated sperm motility [GO:0030317]; fructose biosynthetic process [GO:0046370]; sorbitol catabolic process [GO:0006062] | mitochondrial membrane [GO:0031966]; motile cilium [GO:0031514]; protein-containing complex [GO:0032991] | D-xylulose reductase activity [GO:0046526]; L-iditol 2-dehydrogenase activity [GO:0003939]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q64442}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64442}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q64442}. Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagell... | CATALYTIC ACTIVITY: Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH; Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140, ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9; Evidence={ECO:0000269|PubMed:1459146}; CATALYTIC ACTIVITY: Reaction=L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 mM for D-sorbitol (at pH 7.4) {ECO:0000269|PubMed:1459146}; KM=0.9 mM for xylitol (at pH 7.4) {ECO:0000269|PubMed:1459146}; KM=3.3 mM for L-iditol (at pH 7.4) {ECO:0000269|PubMed:1459146}; KM=51 mM for ribitol (at pH 7.4) {ECO:0000269|PubMed:1459146}; KM=145 mM... | null | null | null | FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with xylitol, L-iditol and D-sorbitol (D-glucitol) as substrates, leading to the C2-oxidized products D-xylulose, L-sorbose and D-fructose, respectively (PubMed:1459146). Is a key enzyme i... | Ovis aries (Sheep) |
P07857 | SCP2_BOVIN | MSLVASQSPLRNRVFVVGVGMTKFTKPGVENRDYPDLAKEAGQKALADAQIPYSAVEQACIGYVYGDSTSGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMARQLIQGGLADCVLALGFEKMVKGPIAVNIQDKANPIDKHIEVMVNKYGLSPSPVAPQMFGNAGKEHMEKYGTTLEHFAKIGWKNHKHSVNNPYSQFQKEYSLDEVMTSRKIFDFLTVLQCCPTSDGAAAAILASEAFVQKHNLKPKAVEILAQEMVTDMPSSFEGKSIIKMVGFDMSKEAARRCYEKSGLRPSDIDVIELHDCFSANELITYEALGL... | 2.3.1.155; 2.3.1.16; 2.3.1.176 | null | bile acid metabolic process [GO:0008206]; fatty acid beta-oxidation [GO:0006635]; intracellular cholesterol transport [GO:0032367]; lipid hydroperoxide transport [GO:1901373]; positive regulation of intracellular cholesterol transport [GO:0032385]; regulation of phospholipid biosynthetic process [GO:0071071] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; phosphatidylcholine transfer activity [GO:0120019]; propanoyl-CoA C-acyltransferase activity [GO:0033814]; propionyl-CoA C2-trimethyltridec... | PF02036;PF02803;PF00108; | 3.40.47.10;3.30.1050.10; | null | PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about 15 kDa, is processed into its mature form (SCP2) by proteolytic cleavage of a 20 residue leader sequence after translocation into peroxisomes. {ECO:0000250|UniProtKB:O62742}. | SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000250|UniProtKB:P22307}. Mitochondrion {ECO:0000250|UniProtKB:P22307}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P32020}. Mitochondrion {ECO:0000250|UniProtKB:P32020}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {... | CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; Evidence={ECO:0000250|UniProtKB:P22307}; PhysiologicalDirec... | null | null | null | null | FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (By similarity). Also a... | Bos taurus (Bovine) |
P07858 | CATB_HUMAN | MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCGTFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCG... | 3.4.22.1 | null | cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; epithelial cell differentiation [GO:0030855]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; regulation of apoptotic process [GO:0042981]; symbion... | apical plasma membrane [GO:0016324]; collagen-containing extracellular matrix [GO:0062023]; endolysosome lumen [GO:0036021]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; ... | collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; peptidase activity [GO:0008233]; proteoglycan binding [GO:0043394] | PF00112;PF08127; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:16733801}. Melanosome {ECO:0000269|PubMed:17081065}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.; EC=3.4.... | null | null | null | null | FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:12220505). Cleaves matrix extracellular phosphoglycoprotein MEPE (PubMed:12220505). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has a... | Homo sapiens (Human) |
P07860 | RPSF_BACSU | MDVEVKKNGKNAQLKDHEVKELIKQSQNGDQQARDLLIEKNMRLVWSVVQRFLNRGYEPDDLFQIGCIGLLKSVDKFDLTYDVRFSTYAVPMIIGEIQRFIRDDGTVKVSRSLKELGNKIRRAKDELSKTLGRVPTVQEIADHLEIEAEDVVLAQEAVRAPSSIHETVYENDGDPITLLDQIADNSEEKWFDKIALKEAISDLEEREKLIVYLRYYKDQTQSEVAERLGISQVQVSRLEKKILKQIKVQMDHTDG | null | null | DNA-templated transcription initiation [GO:0006352]; sporulation resulting in formation of a cellular spore [GO:0030435] | null | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04542;PF04539;PF04545; | 1.20.120.1810;1.10.10.10; | Sigma-70 factor family | null | null | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes (PubMed:8759874). Interaction with SpoIIAB inhibits sigma-F activity throughout the cell befo... | Bacillus subtilis (strain 168) |
P07861 | NEP_RAT | MGRSESQMDITDINAPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDASAEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGQPLLTLLPDIYGWPVASQNWEQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQRLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEINGKP... | 3.4.24.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08473}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473}; | amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; amyloid-beta metabolic process [GO:0050435]; bradykinin catabolic process [GO:0010815]; cellular response to cytokine stimulus [GO:0071345]; cellular response to UV-A [GO:0071492]; cellular response to UV-B [GO:00714... | axon [GO:0030424]; brush border [GO:0005903]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection terminus [GO:0044306]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; presynaps... | cardiolipin binding [GO:1901612]; endopeptidase activity [GO:0004175]; exopeptidase activity [GO:0008238]; metalloendopeptidase activity [GO:0004222]; oligopeptidase activity [GO:0070012]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; phosphatidylserine binding [GO:0001786]; protein homodimerization ac... | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000250|UniProtKB:P08473}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000250|UniProtKB:P08473}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08473}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:2703483}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9); Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:... | null | null | null | null | FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:2966343). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:2966343). Catalyzes cleavage of bradykinin, substance P a... | Rattus norvegicus (Rat) |
P07862 | DDLB_ECOLI | MTDKIAVLLGGTSAEREVSLNSGAAVLAGLREGGIDAYPVDPKEVDVTQLKSMGFQKVFIALHGRGGEDGTLQGMLELMGLPYTGSGVMASALSMDKLRSKLLWQGAGLPVAPWVALTRAEFEKGLSDKQLAEISALGLPVIVKPSREGSSVGMSKVVAENALQDALRLAFQHDEEVLIEKWLSGPEFTVAILGEEILPSIRIQPSGTFYDYEAKYLSDETQYFCPAGLEASQEANLQALVLKAWTTLGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGMSFSQLVVRILELAD | 6.3.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytosol [GO:0005829] | ATP binding [GO:0005524]; D-alanine-D-alanine ligase activity [GO:0008716]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF07478;PF01820; | 3.40.50.20;3.30.1490.20;3.30.470.20; | D-alanine--D-alanine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4; Evidence={ECO:0000269|PubMed:1554356}; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Cell wall formation. | Escherichia coli (strain K12) |
P07864 | LDHC_HUMAN | MSTVKEQLIEKLIEDDENSQCKITIVGTGAVGMACAISILLKDLADELALVDVALDKLKGEMMDLQHGSLFFSTSKITSGKDYSVSANSRIVIVTAGARQQEGETRLALVQRNVAIMKSIIPAIVHYSPDCKILVVSNPVDILTYIVWKISGLPVTRVIGSGCNLDSARFRYLIGEKLGVHPTSCHGWIIGEHGDSSVPLWSGVNVAGVALKTLDPKLGTDSDKEHWKNIHKQVIQSAYEIIKLKGYTSWAIGLSVMDLVGSILKNLRRVHPVSTMVKGLYGIKEELFLSIPCVLGRNGVSDVVKINLNSEEEALFKKSA... | 1.1.1.27 | null | ATP biosynthetic process [GO:0006754]; flagellated sperm motility [GO:0030317]; lactate biosynthetic process from pyruvate [GO:0019244]; lactate metabolic process [GO:0006089]; lactate oxidation [GO:0019516]; pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; nucleus [GO:0005634]; oxidoreductase complex [GO:1990204] | L-lactate dehydrogenase activity [GO:0004459] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; | null | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. | null | null | FUNCTION: Possible role in sperm motility. | Homo sapiens (Human) |
P07866 | LTE1_YEAST | MEIFSQKDYYPTPSSNVISYESDCVSKPVNSADLPALIVHLSSPLEGVDYNASADFFLIYRNFITPQDLHDLLIYRFRWCIREITTNAAKAKRRRIGEVALVRTFVLLRHSILNYFVQDFLPNITLRLRLIEFLNDKHIEQYPKIISSCIINLKKNWVHCSKLVWENIELNEPDKLDFDAWLHYSLKDFTQLESLHKRGSRLSIYARQSFASPDFRNQSVLSLYKTSDVFRLPEKLQSSNSSKNQRSPSMLLFPDNTSNVYSKHRIAKEPSVDNESEDMSDSKQKISHLSKVTLVSTLMKGVDYPSSYAVDKIMPPTPAK... | null | null | asymmetric protein localization to new mitotic spindle pole body [GO:0061510]; cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of exit from mitosis [GO:0031536]; Ras protein signal transduction [GO:0007265]; vesicle-mediated transport [GO:0016192] | cellular bud [GO:0005933]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF00617;PF00618; | 1.10.840.10;1.20.870.10; | LTE1 family | PTM: Phosphorylated by CDC28 in a cell cycle-dependent manner and in response to nocodazole. Dephosphorylion by CDC14 triggers LTE1 release from bud cortex during the exit of mitosis. {ECO:0000269|PubMed:11493673, ECO:0000269|PubMed:12234925, ECO:0000269|PubMed:12432084, ECO:0000269|PubMed:12498684}. | SUBCELLULAR LOCATION: Cytoplasm. Bud. Note=The localization to the bud requires interaction with KEL1, as well as the presence of septins, CDC42, CLA4 and RAS2. | null | null | null | null | null | FUNCTION: GDP-GTP exchange factor for TEM1, a Ras-like protein, component of the mitotic exit network (MEN). Activation of TEM1 by LTE1 in the bud ultimately leads to activation of CDC15 followed by the release of CDC14 from the nucleolus, which then inactivates cyclin-dependent kinases (CDKs) activity by several mecha... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07867 | LIPC_RAT | MGNHLQISVSLVLCIFIQSSACGQGVGTEPFGRNLGATEERKPLQKPEIRFLLFKDESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLLETWIWKIVGALKSRQSQPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMGGKRKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTINCAHERSVHLFIDSLQHSNLQNTGFQCSNMDSFSQGLCLNCKKG... | 3.1.1.3; 3.1.1.32; 3.1.1.5 | null | aflatoxin metabolic process [GO:0046222]; cellular response to hormone stimulus [GO:0032870]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; chylomicron remnant clearance [GO:0034382]; chylomicron remodeling [GO:0034371]; circadian rhythm [GO:000762... | cell surface [GO:0009986]; early endosome [GO:0005769]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; late endosome [GO:0005770]; microvillus [GO:0005902] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; acetylesterase activity [GO:0008126]; acylglycerol lipase activity [GO:0047372]; acyltransferase activity [GO:0016746]; apolipoprotein binding [GO:0034185]; chylomicron binding [GO:0035478]; heparan sulfate proteoglycan binding [GO:0043395]; heparin b... | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315, ECO:0000269|PubMed:1865764, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:7074125}; KM=0.16 mM for 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine {ECO:0000269|PubMed:7074125}; Vmax=144 umol/min/mg enzyme with 1-oleoyl-sn-glycerol as substrate {ECO:0000269|PubMed:1865764... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:7074125}; | null | FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein pa... | Rattus norvegicus (Rat) |
P07871 | THIKB_RAT | MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIG... | 2.3.1.155; 2.3.1.16; 2.3.1.9 | null | fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; phenylacetate catabolic process [GO:0010124] | peroxisome [GO:0005777] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10064897}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000250|UniProtKB:P09110}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000269|PubMed:10064897, ECO:0000269|PubMed:2882519}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for acetoacetyl-CoA {ECO:0000269|PubMed:10064897}; KM=8.2 uM for 3-oxooctanoyl-CoA {ECO:0000269|PubMed:10064897}; KM=6.7 uM for 3-oxohexadecanoyl-CoA {ECO:0000269|PubMed:10064897}; KM=3.2 uM for 3-oxohexadecanedioyl-CoA {ECO:0000269|PubMed:10064897}; Vmax=24.4... | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:10064897, ECO:0000269|PubMed:2882519}. | null | null | FUNCTION: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) (PubMed:10064897, PubMed:2882519). Plays an important role in fatty acid peroxisomal beta-oxidation (PubMed:10064897, PubMed:2882519). Catalyzes the cleavage of short, medium, long, and very long straight chain 3-... | Rattus norvegicus (Rat) |
P07872 | ACOX1_RAT | MNPDLRKERASATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREYGISDPEEIMWFKKLYLANFVEPVGLNYSMFIPTLLNQGTTAQQEKWMRPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITQGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGNAAQSLSKACTIAIRYSAVRRQSEIKQSEPEPQ... | 1.3.3.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11872165, ECO:0000269|PubMed:16672280}; | ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; fatty acid catabolic process [GO:0009062]; fatty acid oxidation [GO:0019395]; generation of precursor metabolites and energy [GO:0006091]; hydrogen peroxide biosynthetic process [GO:0050665]; lipid homeostasis [... | cytoplasm [GO:0005737]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; palmitoyl-CoA oxidase activity [GO:0016401]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803] | PF01756;PF02770;PF14749; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA oxidase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11872165}. | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:16672280, ECO:0000269|PubMed:7503725, ECO:0000305|PubMed:1400324, ECO:0000305|PubMed:7462191}; ... | null | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. | null | null | FUNCTION: Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids. Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, an... | Rattus norvegicus (Rat) |
P07874 | ALGA_PSEAE | MIPVILSGGSGSRLWPLSRKQYPKQFLALTGDDTLFQQTIKRLAFDGMQAPLLVCNKEHRFIVQEQLEAQNLASQAILLEPFGRNTAPAVAIAAMKLVAEGRDELLLILPADHVIEDQRAFQQALALATNAAEKGEMVLFGIPASRPETGYGYIRASADAQLPEGVSRVQSFVEKPDEARAREFVAAGGYYWNSGMFLFRASRYLEELKKHDADIYDTCLLALERSQHDGDLVNIDAATFECCPDNSIDYAVMEKTSRACVVPLSAGWNDVGSWSSIWDVHAKDANGNVTKGDVLVHDSHNCLVHGNGKLVSVIGLEDIV... | 2.7.7.13; 5.3.1.8 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:1846611}; Note=Co(2+) (for PMI). {ECO:0000269|PubMed:1846611}; | alginic acid biosynthetic process [GO:0042121]; GDP-mannose biosynthetic process [GO:0009298] | null | GTP binding [GO:0005525]; mannose-1-phosphate guanylyltransferase (GTP) activity [GO:0004475]; mannose-6-phosphate isomerase activity [GO:0004476] | PF01050;PF00483; | 2.60.120.10; | Mannose-6-phosphate isomerase type 2 family | null | null | CATALYTIC ACTIVITY: Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate; Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527; EC=5.3.1.8; Evidence={ECO:0000269|PubMed:1846611}; CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose; Xref=Rhea:RHEA:15229, ChE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.03 mM for D-mannose 6-phosphate {ECO:0000269|PubMed:1846611}; KM=20.5 uM for D-mannose 1-phosphate {ECO:0000269|PubMed:1846611}; KM=29.5 uM for GTP {ECO:0000269|PubMed:1846611}; KM=14.2 uM for GDP-D-mannose {ECO:0000269|PubMed:1846611}; Vmax=830 nmol/min/mg enzym... | PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.; PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for PMI activity, and 7.6 for GMP activity. {ECO:0000269|PubMed:1846611}; | null | FUNCTION: Produces a precursor for alginate polymerization. The alginate layer provides a protective barrier against host immune defenses and antibiotics. {ECO:0000269|PubMed:1846611}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P07882 | CEL_RAT | MGRLEVLFLGLTCCLAAACAAKLGAVYTEGGFVEGVNKKLSLLGGDSVDIFKGIPFATAKTLENPQRHPGWQGTLKATDFKKRCLQATITQDDTYGQEDCLYLNIWVPQGRKQVSHDLPVMVWIYGGAFLMGSGQGANFLKNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNFGLRDQHMAIAWVKRNIAAFGGDPDNITIFGESAGAASVSLQTLSPYNKGLIRRAISQSGVALSPWAIQENPLFWAKTIAKKVGCPTEDTAKMAGCLKITDPRALTLAYRLPLKSQEYPIVHYLAFIPVVDGDFIPDDP... | 3.1.1.13; 3.1.1.3; 3.1.1.6 | null | ceramide catabolic process [GO:0046514]; chemical synaptic transmission [GO:0007268]; intestinal cholesterol absorption [GO:0030299]; modulation of chemical synaptic transmission [GO:0050804]; neuron cell-cell adhesion [GO:0007158]; pancreatic juice secretion [GO:0030157]; postsynaptic membrane assembly [GO:0097104]; p... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; postsynaptic membrane [GO:0045211]; protein-containing complex [GO:0032991]; zymogen granule [GO:0042588] | acetylesterase activity [GO:0008126]; glycosphingolipid binding [GO:0043208]; lysophospholipase activity [GO:0004622]; neurexin family protein binding [GO:0042043]; protein-containing complex binding [GO:0044877]; retinyl-palmitate esterase activity [GO:0050253]; signaling receptor activity [GO:0038023]; sterol esteras... | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19835}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P19835}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFA) (PubMed:1999399, PubMed:2211595). Preferentially hydrolyzes FAHFAs with the ester bond further away from the ca... | Rattus norvegicus (Rat) |
P07884 | MOD5_YEAST | MLKGPLKGCLNMSKKVIVIAGTTGVGKSQLSIQLAQKFNGEVINSDSMQVYKDIPIITNKHPLQEREGIPHHVMNHVDWSEEYYSHRFETECMNAIEDIHRRGKIPIVVGGTHYYLQTLFNKRVDTKSSERKLTRKQLDILESTDPDVIYNTLVKCDPDIATKYHPNDYRRVQRMLEIYYKTGKKPSETFNEQKITLKFDTLFLWLYSKPEPLFQRLDDRVDDMLERGALQEIKQLYEYYSQNKFTPEQCENGVWQVIGFKEFLPWLTGKTDDNTVKLEDCIERMKTRTRQYAKRQVKWIKKMLIPDIKGDIYLLDATDL... | 2.5.1.75 | null | tRNA modification [GO:0006400] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634] | AMP dimethylallyltransferase activity [GO:0009824]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tRNA binding [GO:0000049]; tRNA dimethylallyltransferase activity [GO:0052381] | PF01715; | 1.10.20.140;3.30.160.60;3.40.50.300; | IPP transferase family | null | SUBCELLULAR LOCATION: Note=[MOD+] forms multicytoplasmic aggregates that do not colocalize to either mitochondria or nucleus. {ECO:0000269|PubMed:22517861}.; SUBCELLULAR LOCATION: [Isoform I]: Cytoplasm {ECO:0000269|PubMed:1850093, ECO:0000269|PubMed:8139535}. Mitochondrion {ECO:0000269|PubMed:1850093, ECO:0000269|PubM... | CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75; Evidence={ECO:0000269|PubMed:... | null | null | null | null | FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in the anticodon loop on a specific subset of tRNAs both in the cytosol and the mitochondrion, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). This modification optimizes the codon:anticodon fit in the ribosome an... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07895 | SODM_RAT | MLCRAACSAGRRLGPAASTAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHATYVNNLNVTEEKYHEALAKGDVTTQVALQPALKFNGGGHINHSIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVSQRYIVCKK | 1.15.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P04179}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P04179}; | acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0003069]; apoptotic mitochondrial changes [GO:0008637]; cellular response to ethanol [GO:0071361]; cellular response to oxidative stress [GO:0034599]; detection of oxygen [GO:0003032]; erythrophore differentiation [GO:004... | mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739] | DNA binding [GO:0003677]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; superoxide dismutase activity [GO:0004784] | PF02777;PF00081; | 1.10.287.990;3.55.40.20; | Iron/manganese superoxide dismutase family | PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity. {ECO:0000269|PubMed:12791589, ECO:0000269|PubMed:16399855}.; PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).... | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:12791589}. | Rattus norvegicus (Rat) |
P07896 | ECHP_RAT | MAEYLRLPHSLAMIRLCNPPVNAVSPTVIREVRNGLQKAGSDHTVKAIVICGANGNFCAGADIHGFSAFTPGLALGSLVDEIQRYQKPVLAAIQGVALGGGLELALGCHYRIANAKARVGLPEVTLGILPGARGTQLLPRVVGVPVALDLITSGKYLSADEALRLGILDAVVKSDPVEEAIKFAQKIIDKPIEPRRIFNKPVPSLPNMDSVFAEAIAKVRKQYPGVLAPETCVRSIQASVKHPYEVGIKEEEKLFMYLRASGQAKALQYAFFAEKSANKWSTPSGASWKTASAQPVSSVGVLGLGTMGRGIAISFARVGI... | 1.1.1.35; 4.2.1.17; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | cytosol [GO:0005829]; peroxisome [GO:0005777] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; enzyme binding [GO:0019899]; intramolecular oxidoreductase activity, transposing C=C bonds [GO:0016863]; long-chain-3-hydroxyacyl-CoA dehydrogenase activity [GO:... | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | PTM: Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-345. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity). {ECO:0000250|UniProtK... | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11781327}. | 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:0000305|PubMed:2303409}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16106; Evidence={ECO:0000305|PubMed:2303409}; CATALYTIC ... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:12106015, ECO:0000269|PubMed:2303409}. | null | null | FUNCTION: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities (PubMed:12106015, PubMed:2303409, PubMed:23351063). Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (PubM... | Rattus norvegicus (Rat) |
P07897 | PGCA_RAT | MTTLLLVFVTLRVIAAVISEEVPDHDNSLSVSIPQPSPLKALLGTSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAIPSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRTVGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGG... | null | null | cartilage condensation [GO:0001502]; cell adhesion [GO:0007155]; cellular response to growth factor stimulus [GO:0071363]; central nervous system development [GO:0007417]; chondroblast differentiation [GO:0060591]; chondrocyte development [GO:0002063]; collagen fibril organization [GO:0030199]; glial cell differentiati... | basement membrane [GO:0005604]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; perineuronal net [GO:0072534]; perisynaptic extracellular matrix [GO:0098966]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; hyaluronic acid binding [GO:0005540] | PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides. {ECO:0000269|PubMed:3693371}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage. | Rattus norvegicus (Rat) |
P07898 | PGCA_CHICK | MTTLLLVFVCLQAITTAASAELSDSSDGLEVKIPEQSPLRVVLGSSLNIPCYFNIPEEEDTNALLTPRIKWSKLSNGTEIVLLVATGGKIRLNAEYREVISLPNYPAIPTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGVVFHYRAISTRYTLNFERAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHLPRERCYGDKDEFPGVRTYGVRETDETYDVYCYAEQMQGKVFYATSPEKFTFQEAFDKCHSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVG... | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501] | extracellular space [GO:0005615]; perineuronal net [GO:0072534]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; hyaluronic acid binding [GO:0005540] | PF00008;PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;2.10.25.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides. {ECO:0000269|PubMed:2365711}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage. | Gallus gallus (Chicken) |
P07900 | HS90A_HUMAN | MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDW... | 3.6.4.10 | null | activation of innate immune response [GO:0002218]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to heat [GO:0034605]; cellular response to virus [GO:0098586]; chaperone-mediated autophagy [GO:0061684]; chaperone-mediated protein complex assembly [GO:0051131]; mitochondrial transport [GO:0006839... | apical plasma membrane [GO:0016324]; axonal growth cone [GO:0044295]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic growth cone [GO:0044294]; endocyti... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; CTP binding [GO:0002135]; dATP binding [GO:0032564]; disordered domain specific binding [GO:0097718]; DNA polymerase binding [GO:0070182]; GTP binding [GO:0005525]; GTPase binding [GO:0051020]; histone ... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from th... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome {ECO:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:11276205}. Mitochondrion {ECO:0000269|PubMed:25609812}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage I... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000269|PubMed:12526792}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for ATP {ECO:0000269|PubMed:18400751}; | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This... | Homo sapiens (Human) |
P07901 | HS90A_MOUSE | MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPSKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEEKEEEKEKEEKESDDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTND... | 3.6.4.10 | null | activation of innate immune response [GO:0002218]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to heat [GO:0034605]; cellular response to virus [GO:0098586]; chaperone-mediated protein complex assembly [GO:0051131]; neuron migration [GO:0001764]; nitric oxide biosynthetic process [GO:0006809];... | apical plasma membrane [GO:0016324]; axonal growth cone [GO:0044295]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic growth cone [GO:0044294]; melanoso... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; CTP binding [GO:0002135]; dATP binding [GO:0032564]; disordered domain specific binding [GO:0097718]; DNA polymerase binding [GO:0070182]; GTP binding [GO:0005525]; GTPase binding [GO:0051020]; histone ... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000250|UniProtKB:P07900}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from t... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22431752}. Cytoplasm {ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:22431752, ECO:0000269|PubMed:27496612, ECO:0000269|PubMed:27686098}. Melanosome {ECO:0000250|UniProtKB:P07900}. Cell membrane {ECO:0000250|UniProtKB:P07900}. Mitochondrion {ECO:0000250|UniProtKB:P0790... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P07900}; | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This... | Mus musculus (Mouse) |
P07902 | GALT_HUMAN | MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHA... | 2.7.7.12 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27005423}; Note=Binds 2 zinc ions per subunit. {ECO:0000305|PubMed:27005423}; | galactose catabolic process [GO:0019388]; galactose catabolic process via UDP-galactose [GO:0033499]; galactose metabolic process [GO:0006012]; UDP-glucose metabolic process [GO:0006011] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794] | UDP-glucose:hexose-1-phosphate uridylyltransferase activity [GO:0008108]; zinc ion binding [GO:0008270] | PF02744;PF01087; | 3.30.428.10; | Galactose-1-phosphate uridylyltransferase type 1 family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989, ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=2.7.7.12; Evidence={ECO:0000269|PubMed:22461411, ECO:0000269|PubMed:27005423}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.25 mM for alpha-D-galactose 1-phosphate (at pH 8.7) {ECO:0000269|PubMed:22461411}; KM=0.43 mM for UDP-glucose (at pH 8.7) {ECO:0000269|PubMed:22461411}; Vmax=48 umol/min/mg enzyme {ECO:0000269|PubMed:22461411}; | PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000269|PubMed:22461411, ECO:0000269|PubMed:27005423}. | null | null | FUNCTION: Plays an important role in galactose metabolism. {ECO:0000269|PubMed:22461411, ECO:0000269|PubMed:27005423}. | Homo sapiens (Human) |
P07903 | ERCC1_MOUSE | MDPGKDEESRPQPSGPPTRRKFVIPLEEEEVPCAGVKPLFRSSRNPTIPATSAHVAPQTYAEYAITQPPGGAGATVPTGSEPAAGENPSQTLKTGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGEVIPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRATECLTTVKSVNKTDSQTLLATFGSLEQLFTASREDLALCPGLGPQKARRLFEVLHEPFLKVPR | null | null | cell development [GO:0048468]; cell population proliferation [GO:0008283]; chromosome organization [GO:0051276]; determination of adult lifespan [GO:0008340]; DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair vi... | chromosome, telomeric region [GO:0000781]; ERCC4-ERCC1 complex [GO:0070522]; nucleoplasm [GO:0005654]; nucleotide-excision repair complex [GO:0000109]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634] | 3' overhang single-stranded DNA endodeoxyribonuclease activity [GO:1990599]; damaged DNA binding [GO:0003684]; promoter-specific chromatin binding [GO:1990841]; single-stranded DNA binding [GO:0003697]; TFIID-class transcription factor complex binding [GO:0001094] | PF14520;PF03834; | 3.40.50.10130;1.10.150.20; | ERCC1/RAD10/SWI10 family | PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Deubiquitinated by USP45. {ECO:0000250|UniProtKB:P07992}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07992}. | null | null | null | null | null | FUNCTION: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, whic... | Mus musculus (Mouse) |
P07909 | ROA1_DROME | MVNSNQNQNGNSNGHDDDFPQDSITEPEHMRKLFIGGLDYRTTDENLKAHFEKWGNIVDVVVMKDPRTKRSRGFGFITYSHSSMIDEAQKSRPHKIDGRVVEPKRAVPRQDIDSPNAGATVKKLFVGALKDDHDEQSIRDYFQHFGNIVDINIVIDKETGKKRGFAFVEFDDYDPVDKVVLQKQHQLNGKMVDVKKALPKQNDQQGGGGGRGGPGGRAGGNRGNMGGGNYGNQNGGGNWNNGGNNWGNNRGGNDNWGNNSFGGGGGGGGGYGGGNNSWGNNNPWDNGNGGGNFGGGGNNWNNGGNDFGGYQQNYGGGPQR... | null | null | compound eye morphogenesis [GO:0001745]; female germ-line stem cell population maintenance [GO:0036099]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of RNA splicing [GO:0033119]; oogenesis [GO:0048477]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of trans... | catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]; polytene chromosome puff [GO:0005703]; ribonucleoprotein complex [GO:1990904] | mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; poly(G) binding [GO:0034046]; sequence-specific DNA binding [GO:0043565] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: This protein is a component of ribonucleosomes. | Drosophila melanogaster (Fruit fly) |
P07910 | HNRPC_HUMAN | MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDLQAIKKELTQIKQKVDSLLENLEKIEKEQSKQAVEMKNDKSEEEQSSSSVKKDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEGEDDRDSANGEDDS | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; chromatin remodeling [GO:0006338]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of telomere maintenance via telomerase [GO:0032211]; osteoblast differentiation [GO:0001649]; RNA splicing [GO:0008380] | actin cytoskeleton [GO:0015629]; catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spliceosomal co... | identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; nucleosomal DNA binding [GO:0031492]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034] | PF00076; | 3.30.70.330; | RRM HNRPC family, RALY subfamily | PTM: Phosphorylated on Ser-260 and Ser-299 in resting cells. Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser stretch at position 238 in response to hydrogen peroxide. {ECO:0000269|PubMed:12564933}.; PTM: Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000269|PubMed:15082759}.; PTM: Ubiquitina... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37599448}. Note=Component of ribonucleosomes. | null | null | null | null | null | FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tet... | Homo sapiens (Human) |
P07911 | UROM_HUMAN | MGQPSLTWMLMVVVASWFITTAATDTSEARWCSECHSNATCTEDEAVTTCTCQEGFTGDGLTCVDLDECAIPGAHNCSANSSCVNTPGSFSCVCPEGFRLSPGLGCTDVDECAEPGLSHCHALATCVNVVGSYLCVCPAGYRGDGWHCECSPGSCGPGLDCVPEGDALVCADPCQAHRTLDEYWRSTEYGEGYACDTDLRGWYRFVGQGGARMAETCVPVLRCNTAAPMWLNGTHPSSDEGIVSRKACAHWSGHCCLWDASVQVKACAGGYYVYNLTAPPECHLAYCTDPSSVEGTCEECSIDEDCKSNNGRWHCQCKQD... | null | null | antibacterial innate immune response [GO:0140367]; apoptotic signaling pathway [GO:0097190]; autophagy [GO:0006914]; cellular defense response [GO:0006968]; cellular response to unfolded protein [GO:0034620]; chaperone-mediated protein folding [GO:0061077]; citric acid secretion [GO:0046720]; collecting duct developmen... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of membrane [GO:0019898]; Golgi lume... | calcium ion binding [GO:0005509]; IgG binding [GO:0019864] | PF12947;PF07645;PF00100; | 2.10.25.10;2.60.40.4100;2.60.40.3210; | null | PTM: N-glycosylated (PubMed:19005207, PubMed:26673890, PubMed:26811476, PubMed:32815518, PubMed:33196145). N-glycan heterogeneity at Asn-232: Hex7HexNAc6 (major) and dHex1Hex7HexNAc6 (minor); at Asn-322: dHex1Hex6HexNAc5 (minor), dHex1Hex7HexNAc6 (major) and dHex1Hex8HexNAc7 (minor); at Asn-396: Hex6HexNAc5 (major), dH... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:22776760, ECO:0000269|PubMed:23988501, ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:7028707}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2249987}. Basolateral cell membrane {ECO:0000269|PubMed:7028707}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2249... | null | null | null | null | null | FUNCTION: [Uromodulin]: Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability (Probable). May serve as a receptor... | Homo sapiens (Human) |
P07913 | TDH_ECOLI | MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMAELGMTEGFDVGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDD... | 1.1.1.103 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:2007567, ECO:0000305|PubMed:9784233}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:2007567}; Name=Cd(2+); Xref=ChEBI:CHEBI:48775; Evidence={ECO:0000269|PubMed:2007567}; Note=Binds 2 Zn(2+) i... | L-serine biosynthetic process [GO:0006564]; L-threonine catabolic process to glycine [GO:0019518]; threonine catabolic process [GO:0006567] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | cadmium ion binding [GO:0046870]; ferrous iron binding [GO:0008198]; L-threonine 3-dehydrogenase activity [GO:0008743]; manganese ion binding [GO:0030145]; oxidoreductase activity [GO:0016491]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}. | CATALYTIC ACTIVITY: Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948; EC=1.1.1.103; Evidence={ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:6780553}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.43 mM for L-threonine (at 37 degrees Celsius and pH 8.4) {ECO:0000269|PubMed:6780553}; KM=0.19 mM for NAD(+) (at 37 degrees Celsius and pH 8.4) {ECO:0000269|PubMed:6780553}; Vmax=57 umol/min/mg enzyme for the NAD(+) oxidation of L-threonine {ECO:0000269|PubMed:67... | PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00627}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.3. At pH 9.0 and 11.0, the activity is 35% and only 6%, respectively, of the optimal level. {ECO:0000269|PubMed:6780553}; | null | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). {ECO:0000269|PubMed:6780553}. | Escherichia coli (strain K12) |
P07914 | BAIA1_CLOSV | MKLVQDKITIITGGTRGIGFAAAKLFIENGAKVSIFGETQEEVDTALAQLKELYPEEEVLGFAPDLTSRDAVMAAVGTVAQKYGRLDVMINNAGITMNSVFSRVSEEDFKNIMDINVNGVFNGAWSAYQCMKDAKQGVIINTASVTGIYGSLSGIGYPTSKAGVIGLTHGLGREIIRKNIRVVGVAPGVVDTDMTKGLPPEILEDYLKTLPMKRMLKPEEIANVYLFLASDLASGITATTISVDGAYRP | 1.1.1.395 | null | bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; protein homotetramerization [GO:0051289]; response to bile acid [GO:1903412] | null | 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase activity [GO:0033792]; bile acid binding [GO:0032052]; NAD+ binding [GO:0070403]; steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0033764] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a 3alpha-hydroxy bile acid CoA + NAD(+) = a 3-oxo bile acid CoA + H(+) + NADH; Xref=Rhea:RHEA:55380, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:138842, ChEBI:CHEBI:138843; EC=1.1.1.395; Evidence={ECO:0000269|PubMed:23836456}; CATALYTIC ACTIVITY: Reaction=choloyl-Co... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=106 uM for choloyl-CoA (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:23836456}; KM=53 uM for chenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:23836456}; KM=22 uM for lithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius) {ECO:00002... | PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000303|PubMed:16299351, ECO:0000305|PubMed:23836456}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: The direction of reaction is pH dependent in vitro. At pH 7.3, clearly the reduction reaction is preferred with an order of magnitude higher velocity than the oxidation reaction. At pH 8.7, the velocities of the oxidation and reduction reaction are comparable. At pH 9.9 th... | null | FUNCTION: Involved in the multi-step bile acid 7alpha-dehydroxylation pathway that transforms primary bile acids to secondary bile acids in the human gut (PubMed:16299351, PubMed:23836456). Catalyzes the oxidation of C3-hydroxyl group of CoA conjugated bile acids generating a C3-oxo bile acid intermediate. Can use chol... | Clostridium scindens (strain JCM 10418 / VPI 12708) |
P07919 | QCR6_HUMAN | MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidative phosphorylation [GO:0006119] | mitochondrial inner membrane [GO:0005743]; mitochondrial respirasome [GO:0005746]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02320; | 1.10.287.20; | UQCRH/QCR6 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00127}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00127}; Intermembrane side {ECO:0000250|UniProtKB:P00127}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Homo sapiens (Human) |
P07926 | AT5G2_BOVIN | MYTCAKFVSTPSLIRRTSTVLSRSLSAVVVRRPETLTDESHSSLAVVPRPLTTSLTPSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | null | null | proton motive force-driven ATP synthesis [GO:0015986] | mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276] | lipid binding [GO:0008289]; proton transmembrane transporter activity [GO:0015078] | PF00137; | 1.20.20.10; | ATPase C chain family | PTM: Trimethylated by ATPSCKMT at Lys-111. Methylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. {ECO:0000250|UniProtKB:Q06055}. | SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Bos taurus (Bovine) |
P07934 | PHKG1_MOUSE | MTRDDALPDSHSAQTFYENYEPKEILGRGVSSVVRRCIHKPTCQEYAVKIIDITGGGSFSSEEVQELREATLKEVDILQKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLTEKETRKIMRALLEVICTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLQPGEKLREVCGTPSYLAPEIIQCSMDDGHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMDGKYQFGSPEWDDYSDTVKDLVSRFLVVQPQDRCSAEEALAHPFFQEYVVEEVRHFSPRGKFKVICLTVLASVKIYY... | 2.7.11.1; 2.7.11.19; 2.7.11.26 | null | glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; phosphorylation [GO:0016310] | phosphorylase kinase complex [GO:0005964] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; phosphorylase kinase activity [GO:0004689]; protein serine kinase activity [GO:0106310]; tau-protein kinase activity [GO:0050321] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.; EC=2.7.11.19; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:3061... | null | null | null | null | FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P07936 | NEUM_RAT | MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKDEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAAKAAQPPTETAESSQAEEEKEAVDEAKPKESARQDEGKEDPEADQEHA | null | null | astrocyte differentiation [GO:0048708]; axon choice point recognition [GO:0016198]; axon guidance [GO:0007411]; axon regeneration [GO:0031103]; cell fate commitment [GO:0045165]; nervous system development [GO:0007399]; radial glial cell differentiation [GO:0060019]; regulation of filopodium assembly [GO:0051489]; regu... | axon [GO:0030424]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; GABA-ergic synapse [GO:0098982]; growth cone [GO:0030426]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presyna... | calmodulin binding [GO:0005516]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786] | PF00612;PF06614;PF10580; | 1.20.5.190; | Neuromodulin family | PTM: Phosphorylated (PubMed:1533624, PubMed:8454596, Ref.13). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (PubMed:1533624, PubMed:8454596, Ref.13). {ECO:0000269|PubMed:1533624, ECO:0000269|PubMed:8454596, ECO:0000269|Ref.13}.; PTM: Palmitoyl... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone {ECO:0000269|PubMed:10982410}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral me... | null | null | null | null | null | FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction (By similarity). {ECO:0000250|UniProtKB:P17677}. | Rattus norvegicus (Rat) |
P07942 | LAMB1_HUMAN | MGLLQLLAFSFLALCRARVRAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLP... | null | null | basement membrane assembly [GO:0070831]; cell adhesion [GO:0007155]; endodermal cell differentiation [GO:0035987]; neuron projection development [GO:0031175]; neuronal-glial interaction involved in cerebral cortex radial glia guided migration [GO:0021812]; odontogenesis [GO:0042476]; positive regulation of cell adhesio... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-1 complex [GO:0005606]; laminin-10 complex [GO:0043259]; laminin-2 complex [GO... | extracellular matrix structural constituent [GO:0005201]; structural molecule activity [GO:0005198] | PF00053;PF21199;PF00055; | 2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It ... | Homo sapiens (Human) |
P07943 | ALDR_RAT | MASHLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVCALMSCAKHKDYPFHAEV | 1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54 | null | cellular hyperosmotic salinity response [GO:0071475]; cellular response to methylglyoxal [GO:0097238]; cellular response to peptide [GO:1901653]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; epithelial cell maturation [GO:0002070]; fructose biosynthetic process [GO:0046370]; ... | cytosol [GO:0005829]; extracellular space [GO:0005615]; mast cell granule [GO:0042629]; paranodal junction [GO:0033010]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane bounded cell projection cytoplasm [GO:0032838]; Schmidt-Lanterman incisure [GO:0043220]; Schwann cell microvillus [GO:0097454] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase activity [GO:0018505]; glyceraldehyde oxidoreductase activity [GO:0043795]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; L-glucuronate reductase activi... | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21; Evidence={ECO:0000250|UniProtKB:P15121}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.; FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displa... | Rattus norvegicus (Rat) |
P07947 | YES_HUMAN | MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQE... | 2.7.10.2 | null | cell differentiation [GO:0030154]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway i... | actin filament [GO:0005884]; centrosome [GO:0005813]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme activity by blocking CSK-mediated inhibition. {ECO:0000269|PubMed:11901164, ECO:0000269|PubMed:9281320, ECO:0000269|PubMed:9794236}.; PTM: Palmitoylation at Cys-3 promotes membra... | SUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytosol. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphoryl... | Homo sapiens (Human) |
P07948 | LYN_HUMAN | MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITE... | 2.7.10.2 | null | adaptive immune response [GO:0002250]; B cell homeostasis [GO:0001782]; B cell receptor signaling pathway [GO:0050853]; C-X-C chemokine receptor CXCR4 signaling pathway [GO:0038159]; cellular response to extracellular stimulus [GO:0031668]; cellular response to heat [GO:0034605]; cellular response to retinoic acid [GO:... | adherens junction [GO:0005912]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glutamatergic s... | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; gamma-tubulin binding [GO:0043015]; glycosphingolipid binding [GO:0043208]; integrin binding [GO:0005178]; kinase activity [GO:0016301]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol ... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent. {ECO:0000269|PubMed:16920712, ECO:0000269|PubMed:20534535}.; PTM: Autophosphorylated (PubMed:18056483, PubMed:18070987, PubMed:7935444, PubMed:9171348, PubMed:9341198). Phosphorylated on tyrosine residues in response to KIT signalin... | SUBCELLULAR LOCATION: Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The traffick... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Fu... | Homo sapiens (Human) |
P07949 | RET_HUMAN | MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLP... | 2.7.10.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11445581, ECO:0000269|PubMed:25242331, ECO:0000269|PubMed:31535977, ECO:0000269|PubMed:9575150}; | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; axon guidance [GO:0007411]; cellular response to retinoic acid [GO:0071300]; embryonic epithelial tube formation [GO:0001838]; enteric nervous system development [GO:0048484]; glial cell-derived neurotrophic factor receptor s... | axon [GO:0030424]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; protein tyrosine kinase activity [GO:0004713]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00028;PF07714;PF17756;PF17812;PF17813; | 2.60.40.60;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. {ECO:0000269|PubMed:11061555, ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:20117004, ECO:0000269|PubMed:24560924, ECO:0000269|PubMed:28846099}.; PTM: Proteolytically cleaved by caspase-3. The soluble RET kin... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19823924, ECO:0000269|PubMed:21994944, ECO:0000269|PubMed:23333276, ECO:0000269|PubMed:28953886, ECO:0000269|PubMed:9575150}; Single-pass type I membrane protein {ECO:0000269|PubMed:19823924}. Endosome membrane {ECO:0000269|PubMed:19823924, ECO:0000269|PubMed:2333... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (PubMed:20064382, PubMed:20616503, PubMed:2070252... | Homo sapiens (Human) |
P07951 | TPM2_HUMAN | MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL | null | null | actin filament organization [GO:0007015]; muscle contraction [GO:0006936]; regulation of ATP-dependent activity [GO:0043462] | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytosol [GO:0005829]; muscle thin filament tropomyosin [GO:0005862] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; structural constituent of muscle [GO:0008307] | PF00261; | 1.20.5.170;1.20.5.340; | Tropomyosin family | PTM: Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is required for ADRB2 internalization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P58775}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P58775}. | null | null | null | null | null | FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in sta... | Homo sapiens (Human) |
P07952 | PMGE_RABIT | MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREKMALNHGEEQVRIWRRSYNVTPPPIEESHPYYHEIYSDRRYRVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTVLISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKRAEK | 5.4.2.11; 5.4.2.4 | null | defense response to protozoan [GO:0042832]; erythrocyte development [GO:0048821]; establishment of blood-brain barrier [GO:0060856]; glycolytic process [GO:0006096]; neuroinflammatory response [GO:0150076]; oxygen transport [GO:0015671] | null | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4; Evidence={ECO:0000250|UniProtKB:P07738}; CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=... | null | null | null | null | FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. {ECO:0000250|UniProtKB:P07738}. | Oryctolagus cuniculus (Rabbit) |
P07953 | F261_RAT | MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYRNYEFFRPDNTEAQLIRKQCALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPEIIAENIKQVKLGSPDYIDCDQEKVLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTPRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLKVWTSHMKRTIQTAEALGVPY... | 2.7.1.105; 3.1.3.46 | null | animal organ regeneration [GO:0031100]; carbohydrate phosphorylation [GO:0046835]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; response to cAMP [GO:0051591]; response to glucagon [... | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex [GO:0043540]; cytosol [GO:0005829] | 6-phosphofructo-2-kinase activity [GO:0003873]; ATP binding [GO:0005524]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900] | PF01591;PF00300; | 3.40.50.300;3.40.50.1240; | Phosphoglycerate mutase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence={ECO:0000269|PubMed:2848802}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290;... | null | null | null | null | FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:2848802}. | Rattus norvegicus (Rat) |
P07954 | FUMH_HUMAN | MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDA... | 4.2.1.2 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; fumarate metabolic process [GO:0006106]; homeostasis of number of cells within a tissue [GO:0048873]; malate metabolic process [GO:0006108]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of double-strand break repair via no... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; tricarboxylic acid cycle enzyme complex [GO:0045239] | fumarate hydratase activity [GO:0004333]; histone binding [GO:0042393] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Fumarase subfamily | PTM: [Isoform Cytoplasmic]: Phosphorylation at Thr-236 by PRKDC in response to DNA damage promotes translocation to the nucleus and recruitment to DNA double-strand breaks (DSBs). {ECO:0000269|PubMed:26237645}. | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:27037871}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:22509282, ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:27037871}. Nucleus {ECO:0000269|PubMed:20231875, ECO:000... | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:30761759, ECO:0000305|PubMed:30718813}; CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:1246... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for L-malate (at pH 8.5) {ECO:0000269|PubMed:30761759}; KM=0.2 mM for fumarate (at pH 8.5) {ECO:0000269|PubMed:30761759}; Note=kcat is 280 sec(-1) with L-malate (at pH 8.5) (PubMed:30761759). kcat is 170 sec(-1) with fumarate (at pH 8.5) (PubMed:30761759). {... | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000250|UniProtKB:P10173}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:30761759}; | null | FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:30761759). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). {ECO:0000269|PubMed:30761759, ECO:0000305}.; FUNCT... | Homo sapiens (Human) |
P07975 | HEMA_INCJH | MFFSLLLVLGLTEAEKIKICLQKQVNSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWIGFGDSRTDKSNSAFPRSADVSAKTADKFRFLSGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHAAINCYRKNWTDIKLNFQKNIYELASQSHCMSLVNALDKTIPLQVTAGTAGNCNNSFLKNPALYTQEVKPSENKCGKENLAFFTLPTQFGTYECKLHLVASCYFIYDSKEVYNKRGCDNYFQVIYDSFGKVVGGLDNRVSPYTGNSGDTPTMQCDMLQLKPGRYSVRSSPRFLLMPERSYCFDMK... | 3.1.1.53 | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789]; sialate 4-O-acetylesterase activity [GO:0106331]; sialate 9-O-acetylesterase activity [GO:0106330] | PF03996;PF02710;PF08720; | 2.20.70.20;3.90.20.10; | Influenza viruses hemagglutinin family | PTM: In natural infection, inactive HEF is matured into HEF1 and HEF2 outside the cell by one or more trypsin-like, arginine-specific endoprotease. {ECO:0000255|HAMAP-Rule:MF_04072}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; Evidence={ECO:0000255|HAMAP-Rule:MF_04072}; CATALYTIC ACTIVITY: Reaction=H2O + N-ace... | null | null | null | null | FUNCTION: Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell c... | Influenza C virus (strain C/Johannesburg/1/1966) |
P07978 | PRM2_MOUSE | MVRYRMRSPSEGPHQGPGQDHEREEQGQGQGLSPERVEDYGRTHRGHHHHRHRRCSRKRLHRIHKRRRSCRRRRRHSCRHRRRHRRGCRRSRRRRRCRCRKCRRHHH | null | null | chromosome condensation [GO:0030261]; nucleus organization [GO:0006997]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283] | male germ cell nucleus [GO:0001673]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | cadmium ion binding [GO:0046870]; DNA binding [GO:0003677]; zinc ion binding [GO:0008270] | PF00841; | null | Protamine P2 family | PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis (PubMed:28366643). Transition proteins (TNP1 and TNP2) are required for processing (PubMed:28366643). {ECO:0000269|PubMed:28366643}. | SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000269|PubMed:28366643}. | null | null | null | null | null | FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. {ECO:0000269|PubMed:12620939, ECO:0000269|PubMed:28366643}. | Mus musculus (Mouse) |
P07981 | GUN1_HYPJE | MAPSVTLPLTTAILAIARLVAAQQPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASA... | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248] | PF00734;PF00840; | 2.70.100.10; | Glycosyl hydrolase 7 (cellulase C) family | PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at this site. {ECO:0000250|UniProtKB:A0A024SNB7}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|Ref.2}; | null | null | null | null | FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose (PubMed:2948877). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substra... | Hypocrea jecorina (Trichoderma reesei) |
P07982 | GUN2_HYPJE | MNKSVAPLLLAASILYGGAVAQQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCIPGATTITTSTRPPSGPTTTTRATSTSSSTPPTSSGVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNEDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTH... | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248] | PF00734;PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:3384334}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:3356188, ECO:0000269|PubMed:3384334}; | null | null | null | null | FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose (PubMed:3384334). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substra... | Hypocrea jecorina (Trichoderma reesei) |
P07986 | GUX_CELFI | MPRTTPAPGHPARGARTALRTTRRRAATLVVGATVVLPAQAATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGDGPPQDSAFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCVGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQACMQVTRCQGVTVWGITDKY... | 3.2.1.8; 3.2.1.91 | null | cellulose catabolic process [GO:0030245]; xylan catabolic process [GO:0045493] | null | cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; endo-1,4-beta-xylanase activity [GO:0031176]; polysaccharide binding [GO:0030247] | PF00553;PF00331; | 2.60.40.290;3.20.20.80; | Glycosyl hydrolase 10 (cellulase F) family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; | null | null | null | null | FUNCTION: Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity.; FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cel... | Cellulomonas fimi |
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