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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0DMA9 | APOA1_PHYMC | MKALVLTLAVLFFTGSQAQHFWQQDDPQSSWDRVKDFATVYVDAIKDSGRDYVAQFEASALGKQLNLKLLDNWDSLTSTFAKVREQLGPVTQEFWDNLEKETESLRQEMNKDLEEVKQKVQPYLDEFKRKWQEELQIYRQKVAPLGEELREGARQKVQELQDKLTPLAEEMRDRARAHVETLRQQLAPYSDDLRQRMATRFEVLKEGGGSLAEYHAKASEQLKALGEKAKPALEDLRQGLLPVLESLKVSILAAIDEASKKLNAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Physeter macrocephalus (Sperm whale) (Physeter catodon) |
P0DMB4 | PA11_VESAF | MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLIGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPV... | 3.1.1.32 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular space [GO:0005615] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; toxin activity [GO:0090729] | PF00151; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | PTM: Not glycosylated. {ECO:0000269|PubMed:23159790}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23159790}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:23159790}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses its activity after heat treatment. {ECO:0000269|PubMed:23159790}; | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (3.6 U/ml) (PubMed:23159790). May act as an allergen and induce hemolytic activity (By similarity). In vivo, a mixture of this protein and Ves a 1.02 is able to paralyze crickets (PubMed:23159790). {ECO:0000250|UniProtKB:P0DMB7, EC... | Vespa affinis (Lesser banded hornet) |
P0DMB5 | PA12_VESAF | MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLVGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNQCVCVGLNAKTYPKTGSFYVPV... | 3.1.1.32 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular space [GO:0005615] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | PF00151; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | PTM: Not glycosylated. {ECO:0000269|PubMed:23159790}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23159790}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:23159790}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses its activity after heat treatment. {ECO:0000269|PubMed:23159790}; | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (6.3 U/ml) (PubMed:23159790). May act as an allergen and induce hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB7, ECO:0000269|PubMed:23159790}. | Vespa affinis (Lesser banded hornet) |
P0DMB6 | PA11_VESVE | GLLPKVKLVPEQISFILSTRENR | 3.1.1.32; 3.1.1.5 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; lysophospholipase activity [GO:0004622]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | null | null | AB hydrolase superfamily, Lipase family | PTM: Contains six disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484737}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:10484737}; Physiologica... | null | PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:10484737}. | null | null | FUNCTION: Catalyzes the hydrolysis of glycerophospholipids such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) and has a moderate activity to hydrolyze lysoglycerophospholipids such as lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine), but is unable to hydrolyze sphingomyelin. Liberates the ... | Vespa velutina (Asian yellow-legged hornet) |
P0DMB7 | PA12A_VESVE | FNPCPYSDDTVKMIILTRENKKHDF | 3.1.1.32; 3.1.1.5 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; lysophospholipase activity [GO:0004622]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | null | null | AB hydrolase superfamily, Lipase family | PTM: Contains six disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484737}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:10484737}; Physiologica... | null | PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:10484737}. | null | null | FUNCTION: Catalyzes the hydrolysis of glycerophospholipids such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) and has a moderate activity to hydrolyze lysoglycerophospholipids such as lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine), but is unable to hydrolyze sphingomyelin. In addition to... | Vespa velutina (Asian yellow-legged hornet) |
P0DMB8 | PA12B_VESVE | FNPCPYSDDTVKMIILTRENKKHDF | 3.1.1.32; 3.1.1.5 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; lysophospholipase activity [GO:0004622]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | null | null | AB hydrolase superfamily, Lipase family | PTM: Contains six disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484737}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:10484737}; Physiologica... | null | PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:10484737}. | null | null | FUNCTION: Catalyzes the hydrolysis of glycerophospholipids such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) and has a moderate activity to hydrolyze lysoglycerophospholipids such as lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine), but is unable to hydrolyze sphingomyelin. In addition to... | Vespa velutina (Asian yellow-legged hornet) |
P0DMC2 | ELA_DANRE | MRFFHPLYLLLLLLTVLVLISADKHGTKHDFLNLRRKYRRHNCPKKRCLPLHSRVPFP | null | null | adult heart development [GO:0007512]; angioblast cell migration from lateral mesoderm to midline [GO:0035479]; apelin receptor signaling pathway [GO:0060183]; cell migration involved in gastrulation [GO:0042074]; cell migration involved in mesendoderm migration [GO:0090134]; chordate embryonic development [GO:0043009];... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | apelin receptor binding [GO:0031704]; hormone activity [GO:0005179]; receptor ligand activity [GO:0048018] | null | null | Elabela/Toddler family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24407481}. Secreted, extracellular space {ECO:0000269|PubMed:24407481}. | null | null | null | null | null | FUNCTION: Endogenous ligand for the apelin receptor (aplnra and/or aplnrb) (PubMed:24316148, PubMed:24407481). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis (PubMed:24316148, PubMed:24407481, PubMed:2... | Danio rerio (Zebrafish) (Brachydanio rerio) |
P0DMC3 | ELA_HUMAN | MRFQQFLFAFFIFIMSLLLISGQRPVNLTMRRKLRKHNCLQRRCMPLHSRVPFP | null | null | adult heart development [GO:0007512]; angiogenesis [GO:0001525]; apelin receptor signaling pathway [GO:0060183]; cell migration involved in mesendoderm migration [GO:0090134]; coronary vasculature development [GO:0060976]; embryonic heart tube development [GO:0035050]; endoderm development [GO:0007492]; heart developme... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | apelin receptor binding [GO:0031704]; hormone activity [GO:0005179] | null | null | Elabela/Toddler family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24316148, ECO:0000269|PubMed:28137936}. Secreted, extracellular space {ECO:0000269|PubMed:28137936}. Note=Found in blood plasma (PubMed:28137936). Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA du... | null | null | null | null | null | FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (PubMed:25639753, PubMed:28137936). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis (PubMed:25639753, PubMed:28137936). Drives internalization... | Homo sapiens (Human) |
P0DMC4 | ELA_MOUSE | MRFQPLFWVFFIFAMSLLFISEQKPVNFPRRRKLYRHNCFRRRCIPLHSRVPFP | null | null | angiogenesis [GO:0001525]; apelin receptor signaling pathway [GO:0060183]; cell migration involved in mesendoderm migration [GO:0090134]; coronary vasculature development [GO:0060976]; embryonic heart tube development [GO:0035050]; endoderm development [GO:0007492]; heart development [GO:0007507]; mesendoderm migration... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | apelin receptor binding [GO:0031704]; hormone activity [GO:0005179] | null | null | Elabela/Toddler family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28663440}. Secreted, extracellular space {ECO:0000269|PubMed:28663440}. Note=Found in blood plasma (By similarity). Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA during pregnancy (PubMed:28663440... | null | null | null | null | null | FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (By similarity). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis (PubMed:28371822, PubMed:28663440, PubMed:28854362, PubMed:28890073). Drives ... | Mus musculus (Mouse) |
P0DMC5 | RCSC_ECOLI | MKYLASFRTTLKASRYMFRALALVLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFEPLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRNAPQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESKIKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAI... | 2.7.13.3 | null | cellular response to osmotic stress [GO:0071470]; phosphorelay signal transduction system [GO:0000160]; regulation of DNA-templated transcription [GO:0006355]; single-species biofilm formation [GO:0044010] | cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF02518;PF00512;PF09456;PF00072; | 1.10.287.130;3.40.50.10970;3.40.50.2300;3.30.565.10; | RcsC family | PTM: Autophosphorylated. Activation probably requires a transfer of a phosphate group from a His in the transmitter domain to an Asp in the receiver domain. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00979, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2404948}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00979, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2404948}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00979}; | null | null | null | null | FUNCTION: Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane-associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB. RcsC has also phosphatase activi... | Escherichia coli (strain K12) |
P0DMC7 | RCSB_ECOLI | MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITLIKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEKISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTLSPADKD | null | null | cellular stress response to acidic pH [GO:1990451]; DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; phosphorelay signal transduction system [GO:0000160]; positive regulation of cell projection organization [GO:0031346]; positive regulation of DNA-templated tran... | cytosol [GO:0005829]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802] | PF00196;PF00072; | 3.40.50.2300;1.10.10.10; | RcsB family | PTM: Phosphorylated and activated by RcsD. {ECO:0000305|PubMed:11309126}. | null | null | null | null | null | null | FUNCTION: Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic ... | Escherichia coli (strain K12) |
P0DMC9 | RCSA_ECOLI | MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSQRPSVVFINEDCFIHDASNSQRIKLIINQHPNTLFIVFMAIANVHFDEYLLVRKNLLISSKSIKPESLDDILGDILKKETTITSFLNMPTLSLSRTESSMLRMWMAGQGTIQISDQMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR | null | null | DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of capsule organization [GO:1901913]; response to stimulus [... | transcription regulator complex [GO:0005667] | DNA binding [GO:0003677] | PF00196; | 1.10.10.10; | RcsA family | PTM: Degraded by the Lon and the HslUV proteases (PubMed:14766922, PubMed:1999391). Interaction with RcsB protects RcsA from degradation (PubMed:1999391). {ECO:0000269|PubMed:1999391}. | null | null | null | null | null | null | FUNCTION: Component of the Rcs signaling system, which controls transcription of numerous genes. Binds, with RcsB, to the RcsAB box to regulate expression of genes involved in colanic acid capsule synthesis. {ECO:0000255|HAMAP-Rule:MF_00982, ECO:0000269|PubMed:10702265, ECO:0000269|PubMed:1999391}. | Escherichia coli (strain K12) |
P0DME0 | SETLP_HUMAN | MAPKRQSPLPLQKKKPRPPPALGLEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQDSEEILKVEQKYNKLRQPFFQKRSELIAKIPNFGVTTFVNHPQVSSLLGEEDEEALHYLTKVEVTEFEDIKSGYRIDFYFDENPYFENKVFSKEFHLNESGDPSSKSTKIKWKSGKDVTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELEEVIKDDIWPNPLQYYLVPDMDDEEGGEDDDDDDDDGDEGEEELEDIDEGDEDEGEEDEDDDEGEEGEEDEGEDD | null | null | endothelial cell differentiation [GO:0045446]; nucleosome assembly [GO:0006334]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393] | PF00956; | 1.20.5.1500;3.30.1120.90; | Nucleosome assembly protein (NAP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22869753}. Nucleus {ECO:0000269|PubMed:22869753}. Note=Translocated from the cytoplasm to the nucleus in protein-induced pluripotent stem (PiPS) endothelial cells. | null | null | null | null | null | FUNCTION: Plays a role as a transcriptional activator involved in the early stage of somatic cell reprogramming. Promotes the differentiation of protein-induced pluripotent stem (PiPS) cells into endothelial cells and the formation of vascular-like tubes (in vitro). Involved in the transcription induction of vascular e... | Homo sapiens (Human) |
P0DML2 | CSH1_HUMAN | MAPGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF | null | null | animal organ development [GO:0048513]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of growth [GO:0045927]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; response to nutrient level... | endoplasmic reticulum [GO:0005783]; endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; vesicle [GO:0031982] | growth factor activity [GO:0008083]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Produced only during pregnancy and is involved in stimulating lactation, fetal growth and metabolism. Does not interact with GHR but only activates PRLR through zinc-induced dimerization. {ECO:0000269|PubMed:16546209}. | Homo sapiens (Human) |
P0DML3 | CSH2_HUMAN | MAAGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF | null | null | animal organ development [GO:0048513]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of growth [GO:0045927]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; response to nutrient level... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; vesicle [GO:0031982] | growth factor activity [GO:0008083]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Produced only during pregnancy and is involved in stimulating lactation, fetal growth and metabolism. Does not interact with GHR but only activates PRLR through zinc-induced dimerization. {ECO:0000269|PubMed:16546209}. | Homo sapiens (Human) |
P0DML7 | APOE_BALAS | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPGWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEEQLGPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAVMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGSERSVSAIRERLGPLMEKGRGRAGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEIREQLEEVRAKVEEQGSQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Balaenoptera acutorostrata scammoni (North Pacific minke whale) (Balaenoptera davidsoni) |
P0DML8 | APOE_LIPVE | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGQEWPGWQDSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLAPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Lipotes vexillifer (Yangtze river dolphin) |
P0DML9 | APOE_ORCOR | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPRWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLGPIAQETQARVSKELQAAQARLASDMEDVRSRVAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRVRAATVGTLASQTLRERAEAWHQKLRGRMEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSPTSAPIENS | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20;1.20.5.1230; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Orcinus orca (Killer whale) (Delphinus orca) |
P0DMM0 | APOE_PHYMC | MKVLWVALVITLLAGCQAEEVKPAPEPEVQLGQEWPGWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEEQLGPVAQETQARVSKELQAAQARLASDMQDVRGRLAQYRSEVQAMMGHTTDELRDRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLDEVRAKVEEQGTQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH | null | null | AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; fatty acid homeostasis [GO:0055089]; G protein-coupled... | chylomicron remnant [GO:0034360]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotei... | amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid transporter activity [GO:0005319]; low-density lipoprotein particle receptor binding [GO:00507... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Physeter macrocephalus (Sperm whale) (Physeter catodon) |
P0DMM1 | APOE_TURTR | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPRWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLGPIAQETQARVSKELQAAQARLASDMEDVRSRVAQYRSEVQALMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLVVYRAGALEGSERSVSAIRERLGPLVEQGRVRAATVGTLASQTLRERAEAWHQKLRGRMEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATGPTSAPIENN | null | null | AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; fatty acid homeosta... | chylomicron remnant [GO:0034360]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotei... | amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipoprotein particle binding [GO:0071813]; low-density l... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) |
P0DMM5 | MCSB_GEOSE | MSFGKFFNTAVSAWMSQEGPNSDIVLSSRIRLARNIVDFRFPTLFSSEEAKQIVALFERAFVHRPYGEAGRFELLKMSELQPIEKRVLVEKHLISPHLAEDSPFGACLLSENEEISIMINEEDHIRIQCLFPGLQLAEALEAASELDDWIEGHVNYAFDERLGYLTSCPTNVGTGLRASVMMHLPALVLTQQINRIIPAINQLGLVVRGTYGEGSEALGNIFQISNQITLGKSEEDIVADLHTIVEQLIAQERAARQALVKTLGIQLEDKVFRSYGILANCRVIDSKEAAQCLSDVRLGIDLGYIKNVSRNILNELMILT... | 2.7.14.1 | null | phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; protein kinase activity [GO:0004672] | PF00217; | 3.30.590.10; | ATP:guanido phosphotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:30616, ChEBI:CHEBI:83226, ChEBI:CHEBI:456216; EC=2.7.14.1; Evidence={ECO:0000269|PubMed:19498169... | null | null | null | null | FUNCTION: Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventin... | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P0DMM9 | ST1A3_HUMAN | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL | 2.8.2.1 | null | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; cellular response to dopamine [GO:1903351]; dopamine catabolic process [GO:0042420]; dopamine metabolic process [GO:0042417]; ethanol catabolic process [GO:0006068]; flavonoid metabolic process [GO:0009812]; steroid metabolic process [GO:0008202]; su... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | amine sulfotransferase activity [GO:0047685]; aryl sulfotransferase activity [GO:0004062]; sulfate binding [GO:0043199]; sulfotransferase activity [GO:0008146] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8093002}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:8093002}; | null | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs. {ECO:0000269|PubMed:15358107, ECO:0000269|PubMed:8093002}. | Homo sapiens (Human) |
P0DMN0 | ST1A4_HUMAN | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL | 2.8.2.1 | null | catecholamine metabolic process [GO:0006584]; steroid metabolic process [GO:0008202]; sulfation [GO:0051923] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | aryl sulfotransferase activity [GO:0004062] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; | null | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs. | Homo sapiens (Human) |
P0DMN7 | DCAM1_MOUSE | MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNF... | 4.1.1.50 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.; | polyamine metabolic process [GO:0006595]; S-adenosylmethionine metabolic process [GO:0046500]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597] | cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; putrescine binding [GO:0019810] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | null | CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000250|UniProtKB:P17707}; | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. | null | null | FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000269|PubMed:22391449}. | Mus musculus (Mouse) |
P0DMQ6 | DHSO_CHICK | MAATGQNLAVVVHRAGDLRLENRPIPEPGPNEVLLRMHSVGICGSDVHYWQHGRIGDFVVKDPMVLGHEASGTVIKVGAGVTHLKPGDRVAIEPGVPRETDEFCKTGRYNLSPTIFFCATPPDDGNLCRYYKHSASYCYKLPDSVTFEEGALIEPLSVGIHACKRAGVTLGSRVFVSGSGPIGLVNVIIAKMMGAAAVVVTDLSASRLQTAKELGADFTIQIKNETPQEVAAKVESLLGCMPEITVECTGVQACIQASIYATRSGGTLVLVGLGPEMVTVPIVNAAVREVDIRGIFRYCNTWPVAISLLASKRINIKPLV... | 1.1.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P07846}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P07846}; | fructose biosynthetic process [GO:0046370]; fructose metabolic process [GO:0006000]; NADH oxidation [GO:0006116]; NADH regeneration [GO:0006735]; sorbitol biosynthetic process [GO:0006061]; sorbitol catabolic process [GO:0006062] | mitochondrial membrane [GO:0031966]; motile cilium [GO:0031514]; protein-containing complex [GO:0032991] | 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=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+); Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924, ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:15649778}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=210 uM for NAD(+) (at 25 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:15649778}; KM=3.2 mM for sorbitol (at 25 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:15649778}; KM=240 uM for NADH (at 25 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:15649778}; KM=1000... | null | null | null | FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is active with D-sorbitol (D-glucitol) as substrate, leading to the C2-oxidized product D-fructose (PubMed:15649778). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbi... | Gallus gallus (Chicken) |
P0DMS0 | PDX1_PLABE | MRDYADNDSILLKHGWCEMLKGGVIMDVKNVEQAKIAEKAGAIGVMILENIPSELRNTDGVARSVDPLKIEEIRKCISINVLAKVRIGHFVEAQILEELKVDMLDESEVLTMADEYNHINKHKFKTPFVCGCTNLGEALRRISEGASMIRTKGEAGTGNIIEAIKHIRTVNNEIKYLCSLDESEVYNFAKKLRAPIDLILLTRKLKRLPVVNFAAGGIATPADAAMCMQLGMDGVFVGSGIFESENPQKMASSIVMAVSNFNNPKILLNVSLGLGKAMHGNTKVSNKWKNKSEEDNS | 4.3.3.6 | null | amino acid metabolic process [GO:0006520]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615] | null | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity [GO:0036381] | PF01680; | 3.20.20.70; | PdxS/SNZ family | null | null | CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:5... | null | PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. | null | null | FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by Pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respecti... | Plasmodium berghei |
P0DMS2 | APOA1_CHILA | MKAVVLAVAVLFLTGSQARHFWQRDEPQTPWDRVKDFATVYVDAIKESGRDYVAQLETSVLGKHLNLKLLDNWDTLSTTFSKLRADLGPVTQEFWDNLEKDTEWLRQEMNKDLQEVKQKVQPYLDNFHKKMQEEMERYREKVGPLGTELREGARQKLQELQEKLTPLGEDLRDRAREHVDTLRTQLAPYSDDMRQRLTQRLEALRDSTTFADYQAKASEHLKTFSEKAKPALEDLRQGLLPVLESLKASILSSIDQATKQLTAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}... | Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera) |
P0DMS3 | APOA1_JACJA | MKAVVLALAVLFLTGSQARHFWQQDDPQSPWDRVKDFATVYVDAVKDSGRDYVSQFESSALGKQLNLHLLDNWDTLSNTVGRLREQLGPVTHEFWANLEKDTEWLRQEMNKDLEEVKVKVQPYLDDFQKKWQEEVERYREKVGPLGAELREGARQKLQELHEKLTPLGEDLRDRARVHVDALRTQLAPYSDQMRERLATRLAAIRDSPSLAVYHAKASEHLKTLSEKAKPALEDLRQGLMPVLENLKTTVLAAIDEASKKLNAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}... | Jaculus jaculus (Lesser Egyptian jerboa) |
P0DMS5 | APOA1_OCTDE | MKAVVLAVAVLFLTGSQARHFWQRDDPQTSWDRVRDFATVYVDAVKESGRDYVAQLEASLGKHLNLKLLDNWDTLSTTFSKLRSELGPVTQEFWDNLEKDTEWLRQEMNKDLVEVKEKVQPYLKNFQEKVQLELEHYRKKVEPLGTDLRDGARQKLQELQEKLTPLGEDLRDRARQHVDELRAQLGPYSDQMRQRLTQRLEALKDSASLAEYQAKAQEHLKTFSEKAKPALEDLRLGLLPVLESLKASFLSSIDEVSKKLSAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}... | Octodon degus (Degu) (Sciurus degus) |
P0DMS7 | IFNA3_ONCMY | MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLSLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIRKEIKRHLQRLDILAAQMY | null | null | defense response to virus [GO:0051607]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; response to exogenous dsRNA [GO:0043330]; type I interferon-mediated signaling pathway [GO:0060337] | cytosol [GO:0005829]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126] | PF00143; | 1.20.1250.10; | Alpha/beta interferon family | null | SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000305|PubMed:24244163}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:24244163}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:24244163}. | null | null | null | null | null | FUNCTION: Key player in antiviral response. Induces expression of TLRs, including that of TLR3, TLR9 and TLR8a1, and that of cytosolic pattern recognition receptors, including RIGI, IFIH1/MDA5 and DHX58/LGP2. Also induces MX1 and its own expression. In the presence of intracellular IFNAR2 (iIFNAR2) and IFNAR1B, intrace... | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) |
P0DMS8 | AA3R_HUMAN | MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE | null | null | activation of adenylate cyclase activity [GO:0007190]; G protein-coupled adenosine receptor signaling pathway [GO:0001973]; inflammatory response [GO:0006954]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of NF-kappaB transcri... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | G protein-coupled adenosine receptor activity [GO:0001609] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28309}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: [Isoform 2]: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase (PubMed:8234299). {ECO:0000269|PubMed:8234299}. | Homo sapiens (Human) |
P0DMS9 | TMIG3_HUMAN | MEGSPAGPIEQKEARWESSWEEQPDWTLGCLSPESQFRIPGLPGCILSFQLKVCFLPVMWLFILLSLALISDAMVMDEKVKRSFVLDTASAICNYNAHYKNHPKYWCRGYFRDYCNIIAFSPNSTNHVALRDTGNQLIVTMSCLTKEDTGWYWCGIQRDFARDDMDFTELIVTDDKGTLANDFWSGKDLSGNKTRSCKAPKVVRKADRSRTSILIICILITGLGIISVISHLTKRRRSQRNRRVGNTLKPFSRVLTPKEMAPTEQM | null | null | activation of adenylate cyclase activity [GO:0007190]; inflammatory response [GO:0006954]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; regulation of heart contraction [... | membrane [GO:0016020]; plasma membrane [GO:0005886] | transmembrane signaling receptor activity [GO:0004888] | null | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27886186}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: [Isoform 1]: Plays a suppressive role in osteosarcoma malignancy by inhibiting NF-kappa-B activity (PubMed:27886186). {ECO:0000269|PubMed:27886186}. | Homo sapiens (Human) |
P0DMT6 | APOE_ALLMI | MRVWTVLLGAVLLLAACQADVQDVETKVKAKWEETVEVFREYVNRLSLATDDITEQITSSQMGKEMDMLIKDXVAELHAYRKDVEERLGPQAVVMRERLHTDVTVLGERLRVDMEEAKTRVQQYLGEARQVAGQNLEDVRSRVGTYLRKLRKRLAKDTEELRRKLEAYSKEATQHLETVREDLEPLREKGQQRLETLQQALRDQGQRLREQLEVRAQEMRGSLDRAATQLQEWLEPFLEDIRTQMQGLLDKLQXKEQQ | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Alligator mississippiensis (American alligator) |
P0DMV8 | HS71A_HUMAN | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA... | null | null | ATP metabolic process [GO:0046034]; cellular heat acclimation [GO:0070370]; cellular response to heat [GO:0034605]; cellular response to oxidative stress [GO:0034599]; cellular response to steroid hormone stimulus [GO:0071383]; cellular response to unfolded protein [GO:0034620]; chaperone cofactor-dependent protein ref... | aggresome [GO:0016235]; blood microparticle [GO:0072562]; centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lum... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; cadherin binding [GO:0045296]; death receptor agonist activity [GO:0038177]; denatured prote... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and S... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Nucleus {ECO:0000269|PubMed:27137183}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27137183}. Secreted {ECO:0000250|UniProtKB:Q61696}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Homo sapiens (Human) |
P0DMV9 | HS71B_HUMAN | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA... | null | null | ATP metabolic process [GO:0046034]; cellular heat acclimation [GO:0070370]; cellular response to heat [GO:0034605]; cellular response to oxidative stress [GO:0034599]; cellular response to steroid hormone stimulus [GO:0071383]; chaperone cofactor-dependent protein refolding [GO:0051085]; mRNA catabolic process [GO:0006... | aggresome [GO:0016235]; blood microparticle [GO:0072562]; centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [G... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; enzyme binding [GO:0019899]; G protein-coupled receptor binding [GO:0001664]; heat shock pro... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and S... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27137183}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Homo sapiens (Human) |
P0DMW0 | HS71A_RAT | MAKKTAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVVNDGDKPKVQVNYKGENRSFYPEEISSMVLTKMKEIAEAYLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRGTLEPVEKA... | null | null | ATP metabolic process [GO:0046034]; binding of sperm to zona pellucida [GO:0007339]; cellular heat acclimation [GO:0070370]; cellular response to heat [GO:0034605]; cellular response to unfolded protein [GO:0034620]; chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated protein complex assembl... | aggresome [GO:0016235]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cell body [GO:0044297]; centriole [GO:0005814]; centrosome [GO:0005813]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615];... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; death receptor agonist activity [GO:0038177]; denatured protein binding [GO:0031249]; disord... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and S... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV8}. Nucleus {ECO:0000250|UniProtKB:P0DMV8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV8}. Secreted {ECO:0000250|UniProtKB:Q61696}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {... | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Rattus norvegicus (Rat) |
P0DMW1 | HS71B_RAT | MAKKTAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVVNDGDKPKVQVNYKGENRSFYPEEISSMVLTKMKEIAEAYLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRGTLEPVEKA... | null | null | ATP metabolic process [GO:0046034]; binding of sperm to zona pellucida [GO:0007339]; cellular heat acclimation [GO:0070370]; cellular response to heat [GO:0034605]; cellular response to unfolded protein [GO:0034620]; chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated protein complex assembl... | aggresome [GO:0016235]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cell body [GO:0044297]; centriole [GO:0005814]; centrosome [GO:0005813]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615];... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; death receptor agonist activity [GO:0038177]; denatured protein binding [GO:0031249]; disord... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and S... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV9}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV9}. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Rattus norvegicus (Rat) |
P0DMW2 | PYDC4_HUMAN | MVSSAQLDFNLQALLGQLSQDDLCKFKSLIRTVSLGNELQKIPQT | null | null | innate immune response [GO:0045087]; negative regulation of cell cycle [GO:0045786]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; negative regula... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | null | 1.10.533.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24871464}. Nucleus {ECO:0000269|PubMed:24871464}. Note=Targeted to the nucleus upon TNF-alpha treatment. {ECO:0000269|PubMed:24871464}. | null | null | null | null | null | FUNCTION: May function as a negative regulator of NF-kappa-B by preventing RELA/p65 phosphorylation at 'Ser-536', thereby inhibiting its transcriptional activity. Through NF-kappa-B regulation may control cytokine release upon Toll-like receptors activation and therefore play a role in modulation of innate immunity. Ma... | Homo sapiens (Human) |
P0DN38 | APOE_CAPHE | MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQGQSRAATLSTQAAQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVGDMQRQWAGLVEKVQLALHLSPTSPPSENH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Capra hircus aegagrus (Wild goat) (Capra aegagrus) |
P0DN39 | APOE_OVIMU | MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQSQSRAATLSTQVGQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKVQLALHLSPTSPPSENH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Ovis aries musimon (Mouflon) |
P0DN41 | APOE_BOSMU | MKVLWVAVVVALLAGCQADMEGELGPEEPLTTQQPRGKDSQPWEQALGRFWDYLRWVQTLSDQVQEELLNTQVIQELTALMEETMKEVKAYKEELEGQLGPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSLSAVRERFGPLVEQGQSRAATLSTLAGQPLLERAEAWRQKLHGRLEEVGVRAQDRLDKIRQQLEEVHAKVEEQGNQMRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKVQLALRPSPTSPPSENH | null | null | AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; fatty acid homeosta... | chylomicron remnant [GO:0034360]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotei... | amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipoprotein particle binding [GO:0071813]; low-density l... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Bos mutus grunniens (Wild yak) (Bos grunniens) |
P0DN83 | DWORF_MOUSE | MAEKESTSPHLIVPILLLVGWIVGCIIVIYIVFF | null | null | positive regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901896]; positive regulation of calcium ion import [GO:0090280]; positive regulation of calcium ion import into sarcoplasmic reticulum [GO:1902082]; positive regulation of cardiac muscle cell contraction [GO:0106134]; regulation of AT... | sarcoplasmic reticulum membrane [GO:0033017] | enzyme activator activity [GO:0008047] | null | null | null | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity (PubMed:26816378, PubMed:30299255). Does not directly stimulate SERCA pump activity (PubMed:26816378). Enhances sarcoplasmic reticulum C... | Mus musculus (Mouse) |
P0DN84 | DWORF_HUMAN | MAEKAGSTFSHLLVPILLLIGWIVGCIIMIYVVFS | null | null | positive regulation of calcium ion import into sarcoplasmic reticulum [GO:1902082]; regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901894]; regulation of slow-twitch skeletal muscle fiber contraction [GO:0031449] | sarcoplasmic reticulum membrane [GO:0033017] | enzyme activator activity [GO:0008047] | null | null | null | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0DN83}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity. Does not directly stimulate SERCA pump activity. Enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing ... | Homo sapiens (Human) |
P0DN86 | CGB3_HUMAN | MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ | null | null | apoptotic process [GO:0006915]; cell-cell signaling [GO:0007267]; female gamete generation [GO:0007292]; G protein-coupled receptor signaling pathway [GO:0007186]; hormone-mediated signaling pathway [GO:0009755]; ovulation [GO:0030728]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; pituitary gonadotropin complex [GO:0061696] | hormone activity [GO:0005179] | PF00007; | 2.10.90.10; | Glycoprotein hormones subunit beta family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16123088}. | null | null | null | null | null | FUNCTION: Beta subunit of the human chorionic gonadotropin (hCG). hCG is a complex glycoprotein composed of two glycosylated subunits alpha and beta which are non-covalently associated. The alpha subunit is identical to those in the pituitary gonadotropin hormones (LH, FSH and TSH). The beta subunits are distinct in ea... | Homo sapiens (Human) |
P0DO01 | DJA7A_ORYSJ | MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSE... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; response to heat [GO:0009408] | chloroplast thylakoid membrane [GO:0009535]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783] | ATP binding [GO:0005524]; heat shock protein binding [GO:0031072]; metal ion binding [GO:0046872]; unfolded protein binding [GO:0051082] | PF00226;PF01556;PF00684; | 1.10.287.110;2.10.230.10;2.60.260.20; | DnaJ family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26210810}. | null | null | null | null | null | FUNCTION: Plays pivotal roles in chloroplast development. Is essential for the regulation of chloroplast development and differentiation. {ECO:0000269|PubMed:26210810}. | Oryza sativa subsp. japonica (Rice) |
P0DO02 | DJA7B_ORYSJ | MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSE... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; response to heat [GO:0009408] | chloroplast thylakoid membrane [GO:0009535]; endoplasmic reticulum [GO:0005783] | ATP binding [GO:0005524]; heat shock protein binding [GO:0031072]; metal ion binding [GO:0046872]; unfolded protein binding [GO:0051082] | PF00226;PF01556;PF00684; | 1.10.287.110;2.10.230.10;2.60.260.20; | DnaJ family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26210810}. | null | null | null | null | null | FUNCTION: Plays pivotal roles in chloroplast development. Is essential for the regulation of chloroplast development and differentiation. {ECO:0000269|PubMed:26210810}. | Oryza sativa subsp. japonica (Rice) |
P0DO11 | FLZ17_ARATH | MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP | null | null | response to abscisic acid [GO:0009737]; response to cytokine [GO:0034097]; response to glucose [GO:0009749]; response to mannose [GO:1905582]; response to salt [GO:1902074]; response to starvation [GO:0042594]; response to sucrose [GO:0009744] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | metal ion binding [GO:0046872] | PF04570; | null | FLZ family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}. Cytoplasm {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}. Note=Shuttles from the cytoplasm to the nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}. | null | null | null | null | null | FUNCTION: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway. {ECO:0000269|PubMed:24600465}. | Arabidopsis thaliana (Mouse-ear cress) |
P0DO17 | VIT1_EUCGR | MADGANDGGNPGAEEQQRLLDQHKEAHFTAGEIVRDIIIGVSDGLTVPFALAAGLSGANASSSIVLTAGIAEVAAGAISMGLGGYLAAKSEADNYARELKREQEEIIRVPDTEAAEVAEILARYGIEPHEYGPVVNALRKKPQAWLDFMMKFELGLEKPDPKRALQSAFTIAIAYVLGGLVPLIPYMFIPVARKAVVASVILTLMALLIFGYAKGYFTDNKPFKSALQTALIGAIASAAAFGMAKAVQS | null | null | intracellular manganese ion homeostasis [GO:0030026]; intracellular sequestering of iron ion [GO:0006880] | vacuolar membrane [GO:0005774] | iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF01988; | null | CCC1 family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:30742036}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:30742036}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28487; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Vacuolar iron transporter involved in the transfer of iron ions from the cytosol to the vacuole for intracellular iron storage (PubMed:30742036). Can transport cobalt ions from the cytosol to the vacuole (PubMed:30742036). {ECO:0000269|PubMed:30742036}. | Eucalyptus grandis (Flooded gum) |
P0DO18 | LHR32_CHLRE | MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL | null | null | nonphotochemical quenching [GO:0010196]; photosynthesis, light harvesting in photosystem I [GO:0009768]; response to high light intensity [GO:0009644]; response to light stimulus [GO:0009416]; response to photooxidative stress [GO:0080183] | chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872] | PF00504; | 1.10.3460.10; | Light-harvesting chlorophyll a/b-binding (LHC) protein family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage (PubMed:19940928, PubMed:21267060, PubMed:23716695, PubMed:26817847, PubMed:27626383, PubMed:27693674... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P0DO19 | LHR31_CHLRE | MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL | null | null | nonphotochemical quenching [GO:0010196]; photosynthesis, light harvesting in photosystem I [GO:0009768]; response to high light intensity [GO:0009644]; response to light stimulus [GO:0009416]; response to photooxidative stress [GO:0080183] | chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872] | PF00504; | 1.10.3460.10; | Light-harvesting chlorophyll a/b-binding (LHC) protein family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage (PubMed:19940928, PubMed:21267060, PubMed:23716695, PubMed:26817847, PubMed:27626383, PubMed:27693674... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P0DO22 | V19H_CATRO | MELDECSPSIFIISFIFIAISIAILRRIRPKKTKALPPGPWKLPLIGNLHQFISRDSLPYKILRDLAQKHGPLMHLQLGEVSAVVASSPEMAKVITRTKDLEFADKPAIRAIRIVTYDYLDIAFNSYGKYWREMRKIFVQELLTPKRVRSFWSAREDVFSNLVKTINSANGKSINLTKLISSTTNSIINRVALGNVPYEREIFMELIKQLLTAAGGFKLVDLFPSYKIIHVLEGTERKLWKILGKIDKILDKVIDEHRENLLRTGKGSGENGQEDIVDILLKIEDGGELDHDIPFGNNNIKALLFDIISGGSDTSSTTID... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | indole alkaloid biosynthetic process [GO:0035835] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:I1TEM1}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(+)-vincadifformine + O2 + reduced [NADPH--hemoprotein reductase] = (+)-minovincinine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61040, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for (+)-vincadifformine (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31009114}; KM=1.4 uM for (+)-vincadifformine {ECO:0000269|PubMed:35660549}; KM=5.6 uM for (+)-vincadifformine (in the presence of 3uM (-)-vincadifformine) {ECO:0000269|PubMed:3566... | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}. | null | null | FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the hydroxylation of (+)-vincadiff... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
P0DO30 | ILIA_NEOS2 | MSQQRYPEPIAVIGSACRFPGASSSPSKLWSLLQEPRDVLKKFDPDRLNLKRFHHTNGDTHGATDVNNKSYLLEENTRLFDASFFGISPLEAAGMDPQQRLLLETVYESFEAAGVTLDQLKGSLTSVHVGVMTNDYSFIQLRDPETLSKYNATGTANSIMSNRISYVFDLKGPSETIDTACSSSLVALHHAAQGLLSGDCETAVVAGVNLIFDPSPYITESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGIVRGTGVNSDGQSSGITMPFAPAQSALIRQTYLRAGLDPIKDRPQYFECHGT... | 2.3.1.-; 6.3.2.- | null | fatty acid biosynthetic process [GO:0006633]; ilicicolin H biosynthetic process [GO:0140781]; methylation [GO:0032259] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; non-ribosomal peptide synthetase activity [GO:1904091]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyke... | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 8 AH2 + ATP + 4 H(+) + holo-[ACP] + L-tyrosine + 7 malonyl-CoA + 2 S-adenosyl-L-methionine = 8 A + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31216742}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:31216742). IliA assembles the backbone of ilicicolin H (PubMed:31216742)... | Neonectria sp. (strain DH2) |
P0DO35 | CP178_ORIVU | MDISISWVVIILLVLSYLILMEKWRAAKLPKNLPPGPPKLPVIGHLHLLGGGLPQHVLRGITQKYGPVAHVQLGEVSSVVLSSTEAARQAMKVLDPAFADRFVNIGSRIMWYDSEDIIFSRYNDHWRQIRKICVSELLSPKNVKSFGYIRQDEMARLIRLFESSEGAAINVSEEISKTVCTIVSRVAFGSVVKDQSLLLNLVKESLRMASGFELADLFPSSWLLNLLCFNKYRLWGMRRRLDNFLDGFLEEHRVKKSGEYGGEDIIDVLYRMQKDSQMKVPITNNGIKGFIYDVFSAGTDTSAATILWALSELMRNPEKM... | 1.14.14.-; 1.14.14.51 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | defense response to insect [GO:0002213]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV-C [GO:0010225]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (1S,5R)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17945, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15383, ChEBI:CHEBI:153... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37.2 uM for gamma-terpinene {ECO:0000269|Ref.1}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000250|UniProtKB:A0A165U5Z9}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7. {ECO:0000269|Ref.1}; | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:26156773, Ref.1). Catalyzes the C2- and C3-hydroxylation of gamma-terpin... | Origanum vulgare (Wild marjoram) |
P0DO38 | CP180_THYVU | MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCFNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIIDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKM... | 1.14.14.-; 1.14.14.51; 1.14.14.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV-C [GO:0010225]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(4R)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (1R,5S)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18957, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15382, ChEBI:CHEBI:153... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40.3 uM for gamma-terpinene {ECO:0000269|Ref.1}; KM=14.1 uM for (4R)-limonene {ECO:0000269|Ref.1}; KM=0.11 uM for (4S)-limonene {ECO:0000269|Ref.1}; Note=kcat is 1.24 sec(-1) with gamma-terpinene as substrate (Ref.1). kcat is 0.08 sec(-1) with (4R)-limonene as subs... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.4-6.8. {ECO:0000269|Ref.1}; | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (Ref.1). Catalyzes the C2-hydroxylation of gamma-terpinene to produce carvacrol ... | Thymus vulgaris (Thyme) |
P0DO39 | CP180_ORIVU | MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCVNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIVDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKM... | 1.14.14.-; 1.14.14.51; 1.14.14.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | defense response to insect [GO:0002213]; response to insect [GO:0009625]; response to water deprivation [GO:0009414]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=gamma-terpinene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = carvacrol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:67404, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:3440, ChEBI:CHEBI:10577, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEB... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | null | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:26156773, PubMed:30231481, Ref.1). Catalyzes the C2-hydroxylation of gam... | Origanum vulgare (Wild marjoram) |
P0DO41 | CP181_ORIVU | MDISISWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKL... | 1.14.14.-; 1.14.14.51; 1.14.14.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | response to insect [GO:0009625]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=alpha-terpinene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = carvacrol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:67412, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:3440, ChEBI:CHEBI:10334, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEB... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7. {ECO:0000269|Ref.1}; | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (Ref.1). Catalyzes the C2-hydroxylation of gamma-terpinene and alpha-terpinene t... | Origanum vulgare (Wild marjoram) |
P0DO42 | CP181_THYVU | MDISILWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSFGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKL... | 1.14.14.-; 1.14.14.51; 1.14.14.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=gamma-terpinene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = carvacrol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:67404, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:3440, ChEBI:CHEBI:10577, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEB... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7. {ECO:0000269|Ref.1}; | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (Ref.1). Catalyzes the C2-hydroxylation of gamma-terpinene and alpha-terpinene t... | Thymus vulgaris (Thyme) |
P0DO49 | U71K3_FRAAN | MKKAELVFIPAPGAGHLVSALQFGKRLLQRDDRISITVLAIKSAAPSSLGSYTEALVASESRLQLIDVPQAELPPLEFAKSPAKFFILNIENHVPNVREALTNYVSSKQDSVSIVGVVLDFFCVSMIHVVNEFNLPSYLFMTSNAGYLSFEFHFPAQDSRTGRPPKDSDPDWLVPGIVPPVPTKVLPVSLTDGSYYNYLGVASRFREAKGIIANTCVELETHAFNSFAEDQTTPPVYPVGPVLDLNDGQARSNLNQAQRDKIISWLDDQPEESVVFLCFGSMGSFTEAQVKEIALGLEQSGQRFLWSLRLTPPKGSKSLT... | 2.4.1.-; 2.4.1.358 | null | fruit ripening [GO:0009835] | null | UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2-acylphloroglucinol + UDP-alpha-D-glucose = a 2-acylphloroglucinol 1-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:56072, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:134386, ChEBI:CHEBI:141060; EC=2.4.1.358; Evidence={ECO:0000269|PubMed:26859691}; PhysiologicalDirection=left-to-right; X... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for 1-naphtol {ECO:0000269|PubMed:26859691}; KM=109 uM for kaempferol {ECO:0000269|PubMed:26859691}; KM=38 uM for quercetin {ECO:0000269|PubMed:26859691}; KM=284 uM for phloroglucinol {ECO:0000269|PubMed:26859691}; KM=24 uM for 2-acylphloroglucinol {ECO:00002... | null | null | null | FUNCTION: Glycosyltransferase that catalyzes the glucosylation of diverse hydroxycoumarins, naphthols, flavonoids, acylphloroglucinols, and pelargonidin (PubMed:26859691). Involved in fruit ripening by synthesizing acylphloroglucinol glucosides and anthocyanin (PubMed:26859691). {ECO:0000269|PubMed:26859691}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) |
P0DO55 | PAL1_FRIUN | MAHIGNGNGNGNGFANGNGNGNGAAGLCLHPDPLNWRAAADALTGSHLDEVRRMAAEFRKPVVRLEGASLSISQVAAVAAGREVKVELSEEARGRVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKEGGALQKELIRFLNAGIFGAGPEDGQTLPPTTTRAAMLVRVNTLLQGYSGIRFEILEAISSLLNHNVTPILPLRGTISSSGDLVPLSYIAGVLIGRPNSKSIGPDGTYVDATEAFRLAGISGGFFELQPKEGLAMVNGTAVGSGLASMVLFEANIIAVLAEVISAIFCEVMQGKPEFTDHLTHKLKHHPGQ... | 4.3.1.25 | null | cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559]; lignin biosynthetic process [GO:0009809]; protein homotetramerization [GO:0051289]; response to water deprivation [GO:0009414]; salicylic acid biosynthetic process [GO:0009697] | cytoplasm [GO:0005737] | phenylalanine ammonia-lyase activity [GO:0045548]; protein self-association [GO:0043621]; tyrosine ammonia-lyase activity [GO:0052883] | PF00221; | 1.20.200.10;1.10.275.10; | PAL/histidase family | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ser-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35643154}. | CATALYTIC ACTIVITY: Reaction=L-tyrosine = (E)-4-coumarate + NH4(+); Xref=Rhea:RHEA:24906, ChEBI:CHEBI:12876, ChEBI:CHEBI:28938, ChEBI:CHEBI:58315; EC=4.3.1.25; Evidence={ECO:0000269|PubMed:35643154}; CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=255.987 uM for L-phenylalanine {ECO:0000269|PubMed:35643154}; KM=1245.354 uM for L-tyrosine {ECO:0000269|PubMed:35643154}; Vmax=1.309 umol/min/mg enzyme with L-phenylalanine as substrate {ECO:0000269|PubMed:35643154}; Vmax=1.327 umol/min/mg enzyme with L-tyrosine a... | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9-8.5. {ECO:0000269|PubMed:35643154}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:35643154}; | FUNCTION: Key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton (By similarity). Can use L-phenylalanine (L-Phe) as substrate more efficiently than L-tyrosine (L-Tyr) (PubMed:35643154). Promotes dro... | Fritillaria unibracteata (Sichuan fritillary) |
P0DO56 | PS_PIPNI | MAPSSQLEFNVVRKQPELLPPAEPTPFEWKELSDIDDQDGLRLHISGFFIYPPSTMSNVGRDNVARDIRLGLSKAMVFYYPLAGRIREGPNRKLSVECTGEGIMYCEADADVRLEQFGDIGALSMPFPFMDKVMFETVDDGILGTPLMYFQSTRFICGGIVIAGCYNHAIADGLGFYMFMAAAAQLARGAASPTPLPVWQRERLLSRVPPRVTFIHHEYIHDTPKTETANPLDNEPWPLHSIFFTRVDVAALRAQLPGHLRKSATSFEIISACLWRCRTAALRFAPDELSRLIIAVNARTKFGPPLPQGYYGNSIMLPMV... | 2.3.1.145 | null | aromatic compound biosynthetic process [GO:0019438] | cytoplasm [GO:0005737] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; transferase activity [GO:0016740] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35634755}. Note=Localized at residual cytoplasmic structures in special cells of the fruit perisperm. {ECO:0000269|PubMed:35634755}. | CATALYTIC ACTIVITY: Reaction=(E,E)-piperoyl-CoA + piperidine = CoA + H(+) + piperine; Xref=Rhea:RHEA:14561, ChEBI:CHEBI:15378, ChEBI:CHEBI:28821, ChEBI:CHEBI:57287, ChEBI:CHEBI:57325, ChEBI:CHEBI:589779; EC=2.3.1.145; Evidence={ECO:0000269|PubMed:33833371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14562; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=342 uM for piperoyl-CoA {ECO:0000269|PubMed:33833371}; KM=7.6 mM for piperidine {ECO:0000269|PubMed:33833371}; Note=kcat is 1.01 sec(-1) with piperoyl-CoA as substrate (PubMed:33833371). kcat is 0.47 sec(-1) with piperidine as substrate (PubMed:33833371). {ECO:0000... | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:33833371}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:33833371}; | null | FUNCTION: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative,... | Piper nigrum (Black pepper) |
P0DO57 | PAS_PIPNI | MASSQLEFNVERKQPELLGPAEPTPYELKELSDIDDQDGVRLFLTAIFIYPPPTKTSMPTRKTDPASDIRRGLSKAMVYYYPFAGRIREGPNRKLSVDCTGEGIVFCEADADIRLDGLGDVEVLRPPYPFIDKMTLGEGSAILGAPLVYVQVTRFACGGFIITGRFNHVMADAPGFTMFMKAAADLARGATVPMPLPVWERERYRSRVPPRVTFAHHEYMHVDDPPPRPTSEPWSLHSAFFTKADVATLRAQLPADLRKAATSFDIITACMWRCRVSALQYGPDEVVRLIVAVNSRTKFDPPLTGYYGNGLMLPAAVTEA... | 2.3.1.-; 2.3.1.145 | null | aromatic compound biosynthetic process [GO:0019438] | cytoplasm [GO:0005737] | acyltransferase activity [GO:0016746]; transferase activity [GO:0016740] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35634755}. Note=Localized at residual cytoplasmic structures in special cells of the fruit perisperm. {ECO:0000269|PubMed:35634755}. | CATALYTIC ACTIVITY: Reaction=(E,E)-piperoyl-CoA + piperidine = CoA + H(+) + piperine; Xref=Rhea:RHEA:14561, ChEBI:CHEBI:15378, ChEBI:CHEBI:28821, ChEBI:CHEBI:57287, ChEBI:CHEBI:57325, ChEBI:CHEBI:589779; EC=2.3.1.145; Evidence={ECO:0000269|PubMed:33833371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14562; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for piperoyl-CoA {ECO:0000269|PubMed:33833371}; KM=8.69 mM for piperidine {ECO:0000269|PubMed:33833371}; Note=kcat is 0.35 sec(-1) with piperoyl-CoA as substrate (PubMed:33833371). kcat is 0.27 sec(-1) with piperidine as substrate (PubMed:33833371). {ECO:000... | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:33833371}. | null | null | FUNCTION: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative,... | Piper nigrum (Black pepper) |
P0DO58 | F3GT1_RHODL | MTKNISRDRHVAVLPFPFSSHAGRLLTLVRRLAAAAPNVTFSFYSTPKSIESLFSPAERVPGNVRPYAVPDGVPEGHVFSGEPVEHVNLYLTAVGEGESLRGVLKAAEAETGRRIGCVMSDAFMWFAGDLAEEMGVPWVPFMAGGANSITAHFYTDLIRETVGMHDIVGRENDIVKFIPGFSELRLGDLPTGVLFGNLESPFAIMLHKMGRALPKATAIAINSFEELDPDIIQDLKSKFKMILNVSPFSAISLPSSPPPPPTSYTDEYGCMPWLDNRKAASVAYIGFGTLATPPPVEIAALAEALEASGTPFLWSLKDNP... | 2.4.1.115; 2.4.1.294 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; cyanidin 3-O-glucoside biosynthetic process [GO:0033485]; positive regulation of anthocyanin biosynthetic process [GO:0031542] | null | anthocyanidin 3-O-glucosyltransferase activity [GO:0047213] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=cyanidin + UDP-alpha-D-galactose = cyanidin 3-O-beta-D-galactoside + H(+) + UDP; Xref=Rhea:RHEA:35631, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:71682, ChEBI:CHEBI:77935; EC=2.4.1.294; Evidence={ECO:0000269|PubMed:35651780}; PhysiologicalDirection=left-to-right; X... | null | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:35651780}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:35651780}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:35651780}; | FUNCTION: Flavonoid 3-O-glycosyltransferase involved in the biosynthesis of anthocyanins conferring flower red/pink colors, mainly anthocyanidin 3-O-glycosides (PubMed:35651780). Catalyzes the addition of UDP-sugar to the 3-OH of anthocyanidin, with a preference for UDP-galactose (UDP-Gal) as sugar donor and cyanidin a... | Rhododendron delavayi (Rhododendron) (Rhododendron arboreum subsp. delavayi) |
P0DO59 | F3GT6_RHODL | MTNSSKGRHVAVLPFPFSTHAAPILSIIRRLASAAPDVTFSFFSTPQSIQTLFPSENPENNIRPHAISDGVPEGFVFSGKHHEDINLFLAAGKESFEAGMKAAEAETGRRIDCVVSDAFMWFSCELAEEMGVPWVTLWVSGACSLAAHCYTDLIRETVGMHDTAGREDEIVKFVPGFSEVRLGDLPSGVVYGNLESPFSMMLYKMGQVLHKAAAVAINSFDELEPEPVKVLASKLKLLTCGPFNPISPPPSSNLDEYGCIPWLDRRKAASVAYIGFGTVATPPPVELAALAEALEASSTPFLWSLRDNPKQHLPEGFLKR... | 2.4.1.115; 2.4.1.294 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; cyanidin 3-O-glucoside biosynthetic process [GO:0033485]; positive regulation of anthocyanin biosynthetic process [GO:0031542] | null | anthocyanidin 3-O-glucosyltransferase activity [GO:0047213] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=cyanidin + UDP-alpha-D-galactose = cyanidin 3-O-beta-D-galactoside + H(+) + UDP; Xref=Rhea:RHEA:35631, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:71682, ChEBI:CHEBI:77935; EC=2.4.1.294; Evidence={ECO:0000269|PubMed:35651780}; PhysiologicalDirection=left-to-right; X... | null | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:35651780}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:35651780}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:35651780}; | FUNCTION: Flavonoid 3-O-glycosyltransferase involved in the biosynthesis of anthocyanins conferring flower red/pink colors, mainly anthocyanidin 3-O-glycosides (PubMed:35651780). Catalyzes the addition of UDP-sugar to the 3-OH of anthocyanidin, with a preference for UDP-galactose (UDP-Gal) as sugar donor and cyanidin a... | Rhododendron delavayi (Rhododendron) (Rhododendron arboreum subsp. delavayi) |
P0DO94 | APOE_MACNE | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEGQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Macaca nemestrina (Pig-tailed macaque) |
P0DO95 | APOE_RHIRO | MKVLWAALLVTFLAGCQAKVEQPVESEPEPELRQQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | AMPA glutamate receptor clustering [GO:0097113]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; fatty acid homeosta... | chylomicron remnant [GO:0034360]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotei... | amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipoprotein particle binding [GO:0071813]; low-density l... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana) |
P0DOA3 | APOE_CEBCA | MKVLWAALLVAFLAGCQGKVEQVVEPELEPELEPHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMEETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGTLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTTPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Cebus capucinus (White-faced sapajou) |
P0DOB6 | PFKA1_LACLL | MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGIEVYGINHGYAGMVAGDIFPLTSASVGDKIGRGGTFLYSARYPEFAQVEGQLAGIEQLKKFGIEGVVVIGGDGSYHGAMRLTEHGFPAVGLPGTIDNDIVGTDFTIGFDTAVSTVVDALDKIRDTSSSHNRTFVVEVMGRNAGDIALNAGIAAGADDISIPELEFKFENVVNNINKGYEKGKNHHIIIVAEGVMTGEEFATKLKEAGYKGDLRVSVLGHIQRGGSPTARDRVLASRMGARAVELLRDGIGGVAVGIRNEELVESPILGTAEEGALFSLTTEGGIKVNNP... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00339}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002] | 6-phosphofructokinase complex [GO:0005945]; cell surface [GO:0009986]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; mannan binding [GO:2001065]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Prokaryotic clade 'B1' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6218377}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for ATP {ECO:0000269|PubMed:6218377}; KM=0.25 mM for fructose 6-phosphate {ECO:0000269|PubMed:6218377}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00339}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-7.8. {ECO:0000269|PubMed:6218377}; | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6218377}. | Lactococcus lactis subsp. lactis (Streptococcus lactis) |
P0DOC3 | APOE_CAMDR | MKALWVALVVTLLAGCRAEVEPEPEPEVQLGQEQPEWQGSQPWELALGRLWDYLRWVQTLSDQVQEELLSTQVTQELTALMEETMKEVKAYKAELEEQLSPVAQETRARLSKELQAAQARLGTDMEDLRSRLAHYRNEVQAMLGQTTDELRNRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGAERSVSALRERLGPLVEQGRLGTATTSTLGSQPLRERAEAWGQKLRGRLEAVGARAQDRLDKMREQLEEVRAKVEEQASQMRLQAETFQARLKGWFQPLVEDLQRQWAGLVEKVQQLAVGTTPTPAASKNQ | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20;1.20.5.1230; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Camelus dromedarius (Dromedary) (Arabian camel) |
P0DOC5 | TX1B_HETMC | ECRYLFGGCKTTADCCKHLGCRTDLYYCAWDGTF | null | null | modulation of voltage-gated sodium channel activity in another organism [GO:0044488] | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 09 (HaTx) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27281198}. | null | null | null | null | null | FUNCTION: Gating-modifier toxin that potently and selectively acts on Nav1.1/SCN1A and Nav1.3/SCN3A (PubMed:32335140). It enhances hNav1.1/SCN1A currents and delays fast inactivation of the channel (EC(50)=11.6 nM), leading to a sustained current (PubMed:32335140). Similar effects are observed at Nav1.3/SCN3A (EC(50)=1... | Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider) |
P0DOC6 | CS13A_LEPSD | MGNLFGHKRWYEVRDKKDFKIKRKVKVKRNYDGNKYILNINENNNKEKIDNNKFIRKYINYKKNDNILKEFTRKFHAGNILFKLKGKEGIIRIENNDDFLETEEVVLYIEAYGKSEKLKALGITKKKIIDEAIRQGITKDDKKIEIKRQENEEEIEIDIRDEYTNKTLNDCSIILRIIENDELETKKSIYEIFKNINMSLYKIIEKIIENETEKVFENRYYEEHLREKLLKDDKIDVILTNFMEIREKIKSNLEILGFVKFYLNVGGDKKKSKNKKMLVEKILNINVDLTVEDIADFVIKELEFWNITKRIEKVKKVNNE... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27256883}; Note=ssRNA target cleavage requires Mg(2+), weak target cleavage is seen with Mn(2+) and Ca(2+). {ECO:0000269|PubMed:27256883}; | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | null | null | CRISPR-associated endoribonuclease Cas13a family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements (spacers) and target... | Leptotrichia shahii (strain DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37) |
P0DOC7 | NPS4L_DANRE | MSCGDSGIRRILRASKRFRSTKGASKARRDQMNSEIRNLRALLPISPEHRLSYLHSMSITCTYIRKSVELRGVCEESTVFSAVNGCVPQDCALQDCALQECVLQECVLQECVLQECVLQALPGFIVAFTTDGKLLYVSENVHEYLGLSMVDVLQSDSFFDMLDRSDVEAVRSVLADASPSGERWVVCRMLVSKAMRLRSSCCPLLVRIRLRDGVCVSLCRPTADRLPARNADFHTHHSADMRLASASSSVLFHLGFSADELIGRSWYELLHPDDLRHAADRHAAILAAATADAEMLIRVQCKDLSWVWMYTHASATAERD... | null | null | blood vessel development [GO:0001568]; definitive hemopoiesis [GO:0060216]; endocardium development [GO:0003157]; endothelial cell development [GO:0001885]; endothelial cell differentiation [GO:0045446]; heart development [GO:0007507]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell ... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF14598; | 3.30.450.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcription factor specifically expressed in endothelial and hematopoietic precursor cells that acts as a key regulator of the endothelial differentiation cascade. Acts as an early-response transcription factor that regulates the expression of early regulators of endothelial and haematopoietic differentiati... | Danio rerio (Zebrafish) (Brachydanio rerio) |
P0DOE4 | SH_HRSS2 | MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT | null | null | protein complex oligomerization [GO:0051259] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | chloride channel activity [GO:0005254]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; sodium channel activity [GO:0005272] | PF03579; | null | Orthopneumovirus small hydrophobic protein family | PTM: Four species of SH have been detected in infected cell cytoplasm: a 7.5 kDa non-glycosylated form (SH0), a 13-15 kDa form that contains one or two N-linked carbohydrate side chains of the high-mannose type (SHg), a 21-30 kDa polylactosaminoglycan-modified form of the protein (SHp), and the isoform generated by alt... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P0DOE5}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DOE5}. Host cell membrane {ECO:0000250|UniProtKB:P0DOE5}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DOE5}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P0DOE5};... | null | null | null | null | null | FUNCTION: Viroporin that forms a homopentameric ion channel displaying low ion selectivity. May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infected cells and may facilitate virus release by modifying the secretory... | Human respiratory syncytial virus A (strain S-2) (HRSV-S2) |
P0DOE5 | SH_HRSVA | MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT | null | null | protein complex oligomerization [GO:0051259]; symbiont-mediated suppression of host apoptosis [GO:0033668] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; monoatomic cation channel activity [GO:0005261] | PF03579; | null | Orthopneumovirus small hydrophobic protein family | PTM: Four species of SH have been detected in infected cell cytoplasm: a 7.5 kDa non-glycosylated form (SH0), a 13-15 kDa form that contains one or two N-linked carbohydrate side chains of the high-mannose type (SHg), a 21-30 kDa polylactosaminoglycan-modified form of the protein (SHp), and the isoform generated by alt... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:2649692}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:2649692}; Single-pass type II membrane protein {ECO:0000305}. Host Golgi apparatus membrane {ECO:0000269|PubMed:15105532, ECO:0000269|PubMed:23229815}; Single-pa... | null | null | null | null | null | FUNCTION: Viroporin that forms a homopentameric ion channel displaying low ion selectivity (PubMed:18369195, PubMed:22621926, PubMed:25100835, PubMed:27817112). May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infec... | Human respiratory syncytial virus A (strain A2) |
P0DOE7 | MATRX_HRSVA | METYVNKLHEGSTYTAAVQYNVLEKDDDPASLTIWVPMFQSSMPADLLIKELANVNILVKQISTPKGPSLRVMINSRSAVLAQMPSKFTICANVSLDERSKLAYDVTTPCEIKACSLTCLKSKNMLTTVKDLTMKTLNPTHDIIALCEFENIVTSKKVIIPTYLRSISVRNKDLNTLENITTTEFKNAITNAKIIPYSGLLLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATRFAIKPMED | null | null | virion assembly [GO:0019068] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; viral tegument [GO:0019033] | structural constituent of virion [GO:0039660] | PF03393; | 2.70.20.30; | Pneumovirinae M protein family | PTM: Phosphorylation is important for oligomerization. {ECO:0000269|PubMed:24672034}. | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24672034}. Host cytoplasm {ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:19297465, ECO:0000269|PubMed:24672034, ECO:0000269|PubMed:29028839, ECO:0000269|PubMed:37712706}. Host nucleus {ECO:0000269|PubMed:12827470, ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:1617140... | null | null | null | null | null | FUNCTION: Plays a crucial role in virus assembly into filaments and budding (PubMed:23903836, PubMed:24672034, PubMed:25673702, PubMed:27654298). Early in infection, localizes in the nucleus where it inhibits host cell transcription through direct binding to host chromatin (PubMed:12827470, PubMed:34685766). Later in i... | Human respiratory syncytial virus A (strain A2) |
P0DOE9 | NS1_HRSVA | MGSNSLSMIKVRLQNLFDNDEVALLKITCYTDKLIHLTNALAKAVIHTIKLNGIVFVHVITSSDICPNNNIVVKSNFTTMPVLQNGGYIWEMMELTHCSQPNGLLDDNCEIKFSKKLSDSTMTNYMNQLSELLGFDLNP | null | null | symbiont-mediated suppression of host adaptive immune response [GO:0039504]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via... | host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025] | null | PF03438; | null | Pneumovirus non-structural protein 1 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:22383950}. Host mitochondrion {ECO:0000269|PubMed:22383950, ECO:0000269|PubMed:23877405}. Host nucleus {ECO:0000269|PubMed:21795342}. Note=Most NS1 resides in the mitochondria as a heteromer with NS2. {ECO:0000269|PubMed:21795342, ECO:0000269|PubMed:23877405}. | null | null | null | null | null | FUNCTION: Plays a major role in antagonizing the type I IFN-mediated antiviral response by degrading or inhibiting multiple cellular factors required for either IFN induction or response pathways (PubMed:15047850). Acts cooperatively with NS2 to repress activation and nuclear translocation of host IFN-regulatory factor... | Human respiratory syncytial virus A (strain A2) |
P0DOF0 | X_BDVV | MSSDLRLTLLELVRRLNGNATIESGRLPGGRRRSPDTTTGTTGVTKTTEGPKECIDPTSRPAPEGPQEEPLHDLRPRPANRKGAAVE | null | null | symbiont-mediated suppression of host apoptosis [GO:0033668] | host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025] | null | PF06515; | null | null | PTM: Phosphorylated. | SUBCELLULAR LOCATION: Host nucleus. Host mitochondrion {ECO:0000269|PubMed:19211764, ECO:0000269|PubMed:23702035, ECO:0000269|PubMed:26700735}. | null | null | null | null | null | FUNCTION: Plays an essential role in the inhibition of host apoptosis. Mediates host mitochondria-mediated apoptosis through interaction with the mitochondrial antiviral signaling protein/MAVS and thereby promotes viral persistence in host central nervous system. Within the host nucleus, regulates viral RNA synthesis a... | Borna disease virus (strain V) (BDV) |
P0DOF5 | M2_I72A2 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Udorn/307/1972 H3N2) |
P0DOF8 | M2_I72A8 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Udorn/1972 H3N2) |
P0DOH7 | POLS_JAEV1 | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAVLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | protein dimerization activity [GO:0046983]; structural molecule activity [GO:0005198] | PF01003;PF21659;PF02832;PF00869;PF01004;PF00948;PF01570; | 1.10.10.930;1.20.1280.260;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | 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-med... | SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membr... | null | 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... | Japanese encephalitis virus (strain SA-14) (JEV) |
P0DOH8 | POLS_JAEVJ | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIAYAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAATLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | protein dimerization activity [GO:0046983]; structural molecule activity [GO:0005198] | PF01003;PF21659;PF02832;PF00869;PF01004;PF00948;PF01570; | 1.10.10.930;1.20.1280.260;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | 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-med... | SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membr... | null | 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... | Japanese encephalitis virus (strain Jaoars982) (JEV) |
P0DOH9 | POLS_JAEV5 | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAVLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | protein dimerization activity [GO:0046983]; structural molecule activity [GO:0005198] | PF01003;PF21659;PF02832;PF00869;PF01004;PF00948;PF01570; | 1.10.10.930;1.20.1280.260;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | 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-med... | SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membr... | null | 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... | Japanese encephalitis virus (strain SA(v)) (JEV) |
P0DOI0 | PRO_BLVJ | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPTSCPPGRFGRVPLVLATLNEVLSNEGGAPGASAPEEQPPPYDPPAILPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAAEAANTLQGFNPKTGTLTQQSAQPNAGDLRSQYQNLWLQAGKNLPTRPSAPWSTIVQGPAESSVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANRECQQILQGRGPVAAVGQKLQACAQWAPKNKQPA... | 3.4.23.- | null | proteolysis [GO:0006508]; viral budding via host ESCRT complex [GO:0039702] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: [Gag-Pro polyprotein]... | SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p15]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Bovine leukemia virus (isolate Japanese BLV-1) (BLV) |
P0DOI1 | PRO_BLVAU | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPKMGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQP... | 3.4.23.- | null | proteolysis [GO:0006508]; viral budding via host ESCRT complex [GO:0039702] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: Gag polyprotein: Myri... | SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p15]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Bovine leukemia virus (isolate Australian) (BLV) |
P0DOK0 | POLSF_SINDV | MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRC... | 3.4.21.90 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.40.10.10; | Alphavirus frameshifted structural polyprotein family | PTM: [Frameshifted structural polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, whe... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000269|PubMed:3829124}. Host cytoplasm {ECO:0000269|PubMed:23785213}. Host cell membrane {ECO:0000269|PubMed:23785213}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR LOCA... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Sindbis virus (SINV) |
P0DOK1 | POLSF_CHIKS | MEFIPTQTFYNRRYQPRPWTPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRKNRKNKKQKQKQQAPQNNTNQKKQPPKKKPAQKKKKPGRRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEWSLAIPVMCLLANTTFPCSQPPCIPCCYEKEPEETLRMLEDNVMRPGYYQLLQASLTCSP... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.40.10.10; | Alphavirus frameshifted structural polyprotein family | PTM: [Isoform Frameshifted structural polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity). The remaining polyprotein is then targeted to the host en... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Chikungunya virus (strain S27-African prototype) (CHIKV) |
P0DOK8 | POLS_JAEVM | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKHLTSFKRELGTLIDAVNKRGKKQNKRGGNESSIMWLASLAIVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAALGWMLGSNSGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | protein dimerization activity [GO:0046983]; structural molecule activity [GO:0005198] | PF01003;PF21659;PF02832;PF00869;PF01004;PF00948;PF01570; | 1.10.10.930;1.20.1280.260;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | 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-med... | SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membr... | null | 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... | Japanese encephalitis virus (strain M28) (JEV) |
P0DOQ5 | DUSP_VAR67 | MDKKSLYKYLLLRSTGDMRRAKSPTIMTRVTNNVYLGNYKNAMNAPSSEVKFKYVLNLTMDKYTLPNSNINIIHIPLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHCVAGVNRSGAMILAYLMSKNKESSPMLYFLYVYHSMRDLRGAFVENPSFKRQIIEKYVIDKN | 3.1.3.-; 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of MAPK cascade [GO:0043409]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host def... | cytosol [GO:0005829]; host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine/threonine phosphatase activity [GO:0008330] | PF00782; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P07239}. Host cytoplasm {ECO:0000250|UniProtKB:P07239}. Note=Approximately 200 molecules of OPG106 are packaged within the virion and are essential for the viability of the virus. {ECO:0000250|UniProtKB:P07239}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:16793284, ECO:0000269|PubMed:1750510... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=228 uM for para-nitrophenyl phosphate {ECO:0000269|PubMed:16793284}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:16793284}; | null | FUNCTION: Serine/tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the OPG144 protein. {ECO:0000250|UniProtKB:P07239}. | Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus) |
P0DOV1 | IFI5B_MOUSE | MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIEFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQAGTSTAQAGTSTAQKRKSMREEETGVKKSKAAKEPDQPPCCEEPTAMCQSPILHSSSSASSNILSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNIDLKEKFTKNNFITISNYFESKGILEINETSSVLEAAPKQMIEVPNCITR... | null | null | activation of innate immune response [GO:0002218]; cellular response to interferon-beta [GO:0035458] | cytosol [GO:0005829]; nuclear periphery [GO:0034399]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690] | PF02760;PF02758; | 1.10.533.10;2.40.50.140; | HIN-200 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15342947}. | null | null | null | null | null | FUNCTION: Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways (PubMed:15342947, PubMed:16458891). May work in synergy with TP53 to promote the transcription of CDKN1A/P21 (PubMed:16458891). {ECO:0000269|PubMed:15342947, ECO:0000269|PubMed:16458891}. | Mus musculus (Mouse) |
P0DOV2 | IFI4_MOUSE | MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQARTSTAQAGTSTAQKRKIMREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLEAAPDQMIEVPNSIIR... | null | null | activation of innate immune response [GO:0002218]; cellular response to interferon-alpha [GO:0035457]; cellular response to interferon-beta [GO:0035458]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:004... | cytosol [GO:0005829]; nuclear inclusion body [GO:0042405]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; transcription coregulator activity [GO:0003712] | PF02760;PF02758; | 1.10.533.10;2.40.50.140; | HIN-200 family | PTM: Acetylated upon bacterial infection, leading to translocation from nucleus to cytoplasm and subsequent recruitment of STING to activate IFN-beta production. {ECO:0000269|PubMed:28529930}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28529930}. Nucleus, nucleolus. Cytoplasm {ECO:0000269|PubMed:28529930}. Note=Nuclear in proliferating cells, translocates to cytosol during cell differentiation or bacterial infection. {ECO:0000269|PubMed:28529930}. | null | null | null | null | null | FUNCTION: Interferon-stimulated protein that plays a role in several biological processes including cell differentiation, autophagy and innate immunity (PubMed:16244109, PubMed:25710914, PubMed:30936875). Cooperates with CGAS to sense dsDNA and activates the STING-dependent type I IFN pathway (PubMed:25710914, PubMed:3... | Mus musculus (Mouse) |
P0DOX3 | IGD_HUMAN | RLQLQESGPGLVKPSETLSLTCIVSGGPIRRTGYYWGWIRQPPGKGLEWIGGVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYYCARGNPPPYYDIGTGSDDGIDVWGQGTTVHVSSAPTKAPDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKCVVQHTASKSKKEIFRWPESPKAQASSVPTAQPQAEGSLAKATTAPATTRNTGRGGEEKKKEKEKEEQEERETKTPECPSHTQPLGVYLLTPAVQDLWLRDKATFTCF... | null | null | immunoglobulin mediated immune response [GO:0016064]; monocyte activation [GO:0042117]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of tumor necrosis factor production [GO:0032760] | blood microparticle [GO:0072562]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; plasma membrane [GO:0005886] | antigen binding [GO:0003823] | PF07654;PF00047;PF20838;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of ... | Homo sapiens (Human) |
P0DOY1 | DNM3C_MOUSE | MRGGSRHLSNEEDVSGCEDCIIISGTCSDQSSDPKTVPLTQVLEAVCTVENRGCRTSSQPSKRKASSLISYVQDLTGDGDEDRDGEVGGSSGSGTPVMPQLFCETRIPSKTPAPLSWQANTSASTPWLSPASPYPIIDLTDEDVIPQSISTPSVDWSQDSHQEGMDTTQVDAESRDGGNIEYQVSADKLLLSQSCILAAFYKLVPYRESIYRTLEKARVRAGKACPSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPENKSRRRTTNDPAASESSPPKRLKTNSYGGKDRGEDEESREQMASDVTNNKGNLEDH... | 2.1.1.37 | null | cell differentiation [GO:0030154]; homologous chromosome pairing at meiosis [GO:0007129]; male meiosis I [GO:0007141]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; piRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141006]; retrotransposon sil... | nucleus [GO:0005634] | DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates [GO:0051718]; DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF17980;PF21255;PF00145; | 1.10.720.50;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.... | null | null | null | null | FUNCTION: DNA methyltransferase that specifically methylates the promoters of evolutionarily young retrotransposons in the male germline (PubMed:27856912, PubMed:28854222). De novo methylation and subsequent repression of transposable elements prevents their mobilization, which is essential for germline integrity (PubM... | Mus musculus (Mouse) |
P0DOY2 | IGLC2_HUMAN | GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS | null | null | immunoglobulin mediated immune response [GO:0016064] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; plasma membrane [GO:0005886] | antigen binding [GO:0003823] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trig... | Homo sapiens (Human) |
P0DOY3 | IGLC3_HUMAN | GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS | null | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; immunoglobulin mediated immune response [GO:0016064] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; IgD immunoglobulin complex [GO:0071738]; IgE immunoglobulin complex [GO:0071742]; IgG immunoglobulin complex [GO:0071735]; IgM immunoglobuli... | antigen binding [GO:0003823] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trig... | Homo sapiens (Human) |
P0DP23 | CALM1_HUMAN | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; G protein-coupled receptor signaling pathway [GO:0007186]; G2/M transition of mitotic cell cycle [GO:0000086]; mitochondrion-endopl... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991... | adenylate cyclase activator activity [GO:0010856]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542]; protein serine/threonine kinase activator activi... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P0DP26}. ... | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (PubMed:16760425, PubMed:23893133, PubMed:26969752, PubMed:27165696, PubMed:28890335, PubMed:31454269, PubMed:35568036). C... | Homo sapiens (Human) |
P0DP24 | CALM2_HUMAN | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | detection of calcium ion [GO:0005513]; G protein-coupled receptor signaling pathway [GO:0007186]; G2/M transition of mitotic cell cycle [GO:0000086]; negative regulation of calcium ion export across plasma membrane [GO:1905913]; negative regulation of calcium ion transmembrane transporter activity [GO:1901020]; negativ... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; sperm midpiece [GO:0097225]; spin... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542]; protein ... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Distributed throughout the cell during interphase, but during ... | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (PubMed:16760425, PubMed:26969752, PubMed:27165696). Calcium-binding is required for the activation of calmodulin (PubMed:... | Homo sapiens (Human) |
P0DP25 | CALM3_HUMAN | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | detection of calcium ion [GO:0005513]; G protein-coupled receptor signaling pathway [GO:0007186]; G2/M transition of mitotic cell cycle [GO:0000086]; negative regulation of calcium ion export across plasma membrane [GO:1905913]; negative regulation of high voltage-gated calcium channel activity [GO:1901842]; negative r... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; sperm midpiece [GO:0097225]; spindle microtubule [GO:000... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542]; protein serine/threonine kinase activator activity [GO:00... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Distributed throughout the cell during interphase, but during ... | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (PubMed:16760425, PubMed:31454269). Calcium-binding is required for the activation of calmodulin (PubMed:16760425, PubMed:... | Homo sapiens (Human) |
P0DP26 | CALM1_MOUSE | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; G2/M transition of mitotic cell cycle [GO:0000086]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; negative r... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; sarcomere [GO:0030017]; sperm midpiece [GO:0097225]; spindle microtubule [GO:0005876]; spindle pole... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235];... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29025071}... | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Mus musculus (Mouse) |
P0DP27 | CALM2_MOUSE | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; G2/M transition of mitotic cell cycle [GO:0000086]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; negative r... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; myelin sheath [GO:0043209]; sarcomere [GO:0030017]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]; vesicle [GO:0031982]; voltage-gated pot... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235];... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Mus musculus (Mouse) |
P0DP28 | CALM3_MOUSE | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; G2/M transition of mitotic cell cycle [GO:0000086]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; negative r... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; growth cone [GO:0030426]; myelin sheath [GO:0043209]; sarcomere [GO:0030017]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]; voltage-gated potassium channel complex [GO:0008076] | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235];... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Mus musculus (Mouse) |
P0DP29 | CALM1_RAT | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; establishment of protein localization to membrane [GO:0090150]; establishment of protein localization to mitochondrial membrane [GO... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; sperm ... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; nitric-oxide synthase binding [GO:0050998]; nitri... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000269|PubMed:12392717}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P0DP26... | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Rattus norvegicus (Rat) |
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