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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0DUE1 | STING_CRAGI | MEKNGAHSFLSDTPVTSLTMSVPVLRHPHVYHAFISYCADADTSHARTILDSVESRGFTCCFAERDFLPGECTSDVVVDAIHCSKNVILVISPASLQSEWSKFEMLMAVDDSHQRNNVCLVPVLLGGVKVDDLPPPLRPLTCIELMDDFRNTDDIIQAISKPEDTWESLLPVGNLAHGFAWGYYYGYLKIILPDLDKTVRQWRRVNNAEGRMSEKLFLFFPQSCRCRDSIADESSLIKHRGHLPIITKDRAGIIERQYKNTIYSVTDDNGEDYFFAGEYIGVIHTMFEMEQNATTGLQTREKYVQSMRFYLTLKRILDTD... | 3.2.2.6 | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709]; signal tr... | autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809] | PF13676;PF15009; | 1.20.5.5200;3.40.50.12100;3.40.50.10140; | Toll-like receptor family; TMEM173 family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev... | null | null | null | null | FUNCTION: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (By similarity). Binds c-di-AMP, 2'3'-cGAMP, 3'3'-cGAMP and to a lesser extent c-di-GMP. Nucleotide binding has not been seen to stimulate NAD(+) hydrolase activity (PubMed:32877915). {ECO:0000250|UniProtKB:A7SLZ2, ECO:0000269|PubMed:32... | Crassostrea gigas (Pacific oyster) (Crassostrea angulata) |
P0DUF9 | PGLX_ECOHS | MNTNNIKKYAPQARNDFRDAVIQKLTTLGIAADKKGNLQIAEAETIGETVRYGQFDYPLSTLPRRERLVKRAREQGFEVLVEHCAYTWFNRLCAIRYMELHGYLDHGFRMLSHPETPTAFEVLDHVPEVAEALLPESKAQLVEMKLSGNQDEALYRELLLGQCHALHHAMPFLFEAVDDEAELLLPDNLTRTDSILRGLVDDIPEEDWEQVEVIGWLYQFYISEKKDAVIGKVVKSEDIPAATQLFTPNWIVQYLVQNSVGRQWLQTYPDSPLKDKMEYYIEPAEQTPEVQAQLAAITPASIEPESIKVLDPACGSGHIL... | 2.1.1.72 | null | defense response to virus [GO:0051607]; macromolecule modification [GO:0043412]; methylation [GO:0032259] | null | nucleic acid binding [GO:0003676]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007] | PF20473; | 3.40.50.150; | Methyltransferase superfamily, PglX adenine methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616;... | null | null | null | null | FUNCTION: BREX systems (bacteriophage exclusion) provide immunity against bacteriophage. Part of a type 1 BREX system which protects against dsDNA phage. This system allows phage adsorption but prevents phage DNA replication, without degradation of the phage DNA. Methylation of bacterial DNA by this protein guides self... | Escherichia coli O9:H4 (strain HS) |
P0DUG4 | PA2TI_NAJHH | NVYQYRKMLQCAMPNGGPFECCQTHDNCYGEAEKLKACTSTHSSPYFK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; phospholipase A2 activity [GO:0004623]; toxin activity [GO:0090729] | null | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19622365}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=0.0012 umol/min/mg enzyme (from PMID:25522251); | null | null | null | FUNCTION: Phospholipase A2 with weak enzymatic activity, which partially inhibits thrombin enzymatic activity (Ki=73 nM), completely inhibits thrombin-induced platelet aggregation and retards fibrin clot formation (IC(50)=0.2 nM) (PubMed:19622365). May exert this anticoagulant effect through a non-enzymatic mechanism (... | Naja haje haje (Egyptian cobra) |
P0DUH5 | DDDA_BURC1 | MYEAARVTDPIDHTSALAGFLVGAVLGIALIAAVAFATFTCGFGVALLAGMMAGIGAQALLSIGESIGKMFSSQSGNIITGSPDVYVNSLSAAYATLSGVACSKHNPIPLVAQGSTNIFINGRPAARKDDKITCGATIGDGSHDTFFHGGTQTYLPVDDEVPPWLRTATDWAFTLAGLVGGLGGLLKASGGLSRAVLPCAAKFIGGYVLGEAFGRYVAGPAINKAIGGLFGNPIDVTTGRKILLAESETDYVIPSPLPVAIKRFYSSGIDYAGTLGRGWVLPWEIRLHARDGRLWYTDAQGRESGFPMLRAGQAAFSEAD... | 3.5.4.- | null | null | membrane [GO:0016020] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF14428;PF20148;PF05488;PF03527;PF05593; | 2.60.200.60;3.90.930.1;2.180.10.10; | RHS/WapA nuclease family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in double-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in double-stranded DNA + NH4(+); Xref=Rhea:RHEA:66604, Rhea:RHEA-COMP:17070, Rhea:RHEA-COMP:17071, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902; Evidence={ECO:0000269... | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Bacteria that have this module inhib... | Burkholderia cenocepacia (strain H111) |
P0DUJ5 | MORO_PTEVL | MKCIALFLVLSMVVLMAEPGEAFIHHIIGGLFHVGKSIHDLIRGKNRDMAEQQELERAFDRERAFA | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | null | PF08107; | null | Pleurocidin family | PTM: This peptide exists in N-terminally amidated and non-amidated forms. The amidated form is more active and has a greater alpha-helix content than the non-amidated form. {ECO:0000269|PubMed:29108968}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29108968}. | null | null | null | null | null | FUNCTION: The amidated peptide is bactericidal on human pathogens like S.aureus or E.coli, as well as on the fish pathogen A.salmonicida (PubMed:29108968). May also be active against a variety of fungi (By similarity). It can kill bacteria in less than 30 minutes (S.aureus) and 120 minutes (V.vulnificus) (PubMed:291089... | Pterois volitans (Red lionfish) (Gasterosteus volitans) |
P0DUJ7 | SSEK3_SALTS | MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHE... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:29449376}; | symbiont-mediated perturbation of host defense-related programmed cell death [GO:0034053] | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell Golgi apparatus [GO:0044177] | lipid binding [GO:0008289]; manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729] | null | null | Glycosyltransferase NleB family | PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000269|PubMed:32432056}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21445262}. Host Golgi apparatus {ECO:0000269|PubMed:26394407, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215}. Note=Secreted via type III secretion system 2 (SPI-2 T3SS) (PubMed:21445262). Localizes to host Golgi apparatus via lip... | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling and apoptosis (PubMed:26394407, PubMed:28069818, PubMed:28522607, PubMed:29449376, PubMed:32766249). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) ... | Salmonella typhimurium (strain SL1344) |
P0DUJ8 | SSEK2_SALTS | MARFNAAFTRIKIMFSRIRGLISCQSNTQTIAPTLSPPSSGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYLNNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNYSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETLISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLDADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLEIMHSKPYGDPYNDWLSKGLRHYFDGSHIQD... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30327479}; | null | extracellular region [GO:0005576]; host cell Golgi apparatus [GO:0044177] | manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729] | null | null | Glycosyltransferase NleB family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8ZNP4}. Host Golgi apparatus {ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32974215}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:Q8ZNP4}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:30327479). A... | Salmonella typhimurium (strain SL1344) |
P0DUM4 | AAPA1_HELPY | MATKHGKNSWKTLYLKISFLGCKVVVLLKR | null | null | regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | lipid binding [GO:0008289] | null | null | AapA toxin family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:31476357, ECO:0000305|PubMed:33229580}. | null | null | null | null | null | FUNCTION: May be involved in response to oxidative stress (Probable). Toxic component of a type I toxin-antitoxin (TA) system. When overexpression is induced in situ in the absence of its cognate antisense RNA antitoxin IsoA1 it leads to cell growth arrest and cell death without lysis. Neutralized by IsoA1 RNA which fo... | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
P0DUM6 | PDUA_CITFR | MQQEALGMVETKGLTAAIEAADAMVKSANVMLVGYEKIGSGLVTVIVRGDVGAVKAATDAGAAAARNVGEVKAVHVIPRPHTDVEKILPKGIS | null | null | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469] | null | PF00936; | 3.30.70.1710; | Bacterial microcompartments protein family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}. Note=In BMCs the hexamer concave side probably faces outward, with the N- and C-termini exposed to the cytoplasm (Probable). Modeling suggests the concave face (with both termini) is in the interior of the BMC (... | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation, probably important for metabolite diffusion into and out of the BMC (Probable). Overexpression of a C-terminally mutated form (PduA*) makes thin parallel filaments with a honeycomb-like a... | Citrobacter freundii |
P0DUN0 | PA23_BOTHY | DLMQFETLIMKSGVWYYGSYGCYCGSGGQFRPQDASDRCCFVHDCCYGKNGDIVCGGDDPCKKQICECDRVAATCFRDNKVTYDNKYWFFPAKFPPQNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29124136}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29124136}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:29124136}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.43 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA) {ECO:0000269|PubMed:29124136}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:29124136}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:29124136}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces inflammatory response, with local edema and release of cytokines IL-1 alpha, IL-6 and TNF-alpha (PubMed:29124136). Does not exhibit myotoxic, anticoagulant and antibacterial effects (PubMed:29124136). Release of pro-inflammatory cytokines may be due to mast cel... | Bothrocophias hyoprora (Amazonian hognose viper) (Porthidium hyoprora) |
P0DUN1 | PA22_BOTHY | NLLQFNKMILKETGKNAIPFYAFYGCYCGWGGRGKPKDKTDDRCCFVHDCCYGKLTGCPKWDIYPYSLKSGYITCGKGTWCEEQICECDRAAAICFRENLDTYNKYGYMFYPDSRCKGPSEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:25365526}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25365526}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:25365526}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.65 nmol/min/mg enzyme {ECO:0000269|PubMed:25365526}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:25365526}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|PubMed:25365526}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myotoxicity and local edema in mice (PubMed:25365526). In addition, it causes neuromuscular blockade in avian neuromuscular preparations with a significant direct action on skeletal muscle function (PubMed:25365526). Myotoxic action is exerted by both enzymatic... | Bothrocophias hyoprora (Amazonian hognose viper) (Porthidium hyoprora) |
P0DUN2 | PA21_BOTHY | DLWEFGKMILKETGKNPFPYYGAYGCYCGWGGRGKPKDKTDDRCCFVHDCCRYKKLTGCPKTNDRYSYSWKDLTIVCGEDDPCKELCECDKAAAVCFRENLGTYNKKYRYHLRSLCKKADKPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:21496495}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496495}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:21496495}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.96 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA) {ECO:0000269|PubMed:21496495}; Vmax=11.76 nmol/min/mg enzyme {ECO:0000269|PubMed:21496495}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:21496495}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:21496495}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces in vivo myotoxicity, moderates footpad edema, and causes in vitro neuromuscular blockade. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:21496495}. | Bothrocophias hyoprora (Amazonian hognose viper) (Porthidium hyoprora) |
P0DUN3 | PA2A1_BOTBZ | NLWQFEMLIMKIALTSGFMFYSSYGCYCGWGGHGRPKDASDRCCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXCQEESDPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28951306}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28951306}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:28951306}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-8.5. {ECO:0000269|PubMed:28951306}; | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces significant edematogenic activity. Shows mild cytotoxicity on Trypanosoma cruzi and Leishmania infantum. Also inhibits ADP- and collagen-induced platelet aggregation. Does not show myotoxic activity. {ECO:0000269|PubMed:28951306}. | Bothrops brazili (Brazil's lancehead) |
P0DUN4 | PA2A2_BOTBZ | NLWQFEMLIMKIAKTSGFMFYSSYGCYCGWGGHGRPQDASDRCCFVHDCCYGKVTGVVVCGGDDPCKXQICECDRVAATCFRDNKYWFFPAK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28951306}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28951306}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:28951306}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-8.5. {ECO:0000269|PubMed:28951306}; | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces significant edematogenic activity. Shows mild cytotoxicity on Trypanosoma cruzi and Leishmania infantum. Also inhibits ADP- and collagen-induced platelet aggregation. Does not show myotoxic activity. {ECO:0000269|PubMed:28951306}. | Bothrops brazili (Brazil's lancehead) |
P0DUN5 | PA2_BOTBS | HLLQFNKNAIPFYAFYGCYCGWGGRCCFVHDCCYGKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23509754}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23509754}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:23509754}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=24.75 nmol/min/mg enzyme {ECO:0000269|PubMed:23509754}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:23509754}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-37 degrees Celsius. {ECO:0000269|PubMed:23509754}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myonecrosis, when intramuscularly injected into mice (PubMed:23509754). Does not show systemic myotoxic effect (after intravenous injection) (PubMed:23509754). Does not show cytotoxic activities in myotubes and myoblasts (PubMed:23509754). Induces marked paw ed... | Bothrops bilineatus smaragdinus (Two-striped forest-pitviper) |
P0DUP7 | APOE_TAPIN | MKVLWAALVVTLLAGCQADVEREPEVQLGNEWAKWQAGQPWEQALGRFWNYLRWVQTLSDQVQEELLSTQATQELTVLIEETMKEVKTYKAELEQQLGPMAQETQARVSKELQAAQARLGADMEDVRNRLVQYRSELQAMMGQSTEELRGRLNSHLRKLRKRLLRDAEDLQKRLAVYQAGIREGAERSVNTLRERLGPLVEQAATVRSLVSKPLQERAEAWGQRLRGRLEKVGIQAGDRLDEVREQVQEVRAKVEEQANQMRLQAEAFHARLKSWFEPLVQDMQQRWAELVEKVQLAVGTSPTSESSEKQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Tapirus indicus (Asiatic tapir) (Malayan tapir) |
P0DUP8 | APOE_TAPTE | MKVLWAALVVTLLAGCQADVEPEPEVQLGNEWAKWQAGQPWEQALGRFWNYLRWVQTLSDQVQEELLSTQATQELTALMEETMKEVKTYKAQLEQQLGPTAQETQARVSKELQAAQARLGADMEDVRNRLVQYRSELQAMMGQSTEELRGRLNSHLRKLRKRLLRDAEDLQKRLAVYQAGIREGAERSVNTLRERLRPLVEQAATVRSLISKPLQERAEAWGQRLRGRLEKVGTQAGDRLDEVREQVQEVRAKVEEQANQMRLQAEAFHARLKSWFEPLVQDMQQKWAELVEKVQLAVGTSPTSESSEKQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Tapirus terrestris (Lowland tapir) (Brazilian tapir) |
P0DUQ3 | MAT1_BEMTA | MSISSSVAVLNVVQVSPPTAPVNNAFQDRISLTHFDLLALRAPPNQRLFFYETHLPISAFAETVIPKLRDSLSLTLQNFRPLAGTLIWSLHSDEPYIRIKDDDSVPLTIAETDADPQKLFDDPFQQETDLQQLLPPLRVSETEASLLALQITLFPSGDICLGITFHHAAQDGASLALFLKSWAHICRHGDDPPLPQNLIPIFDRDFIDDPKNIKQLFLDHLLTPLTPGGPRNRSVKPMEKPFNDRMHGSFRLTVDDIENLRRRITSLQVQNTSQEPPVRMSTVVVTCAYVLTCFVKAGLTKKHVRFILPADLRKRLQPPV... | 2.3.1.-; 2.3.1.116 | null | detoxification [GO:0098754]; response to toxic substance [GO:0009636] | null | flavonol-3-O-beta-glucoside O-malonyltransferase activity [GO:0047165]; O-malonyltransferase activity [GO:0050736] | PF02458; | 3.30.559.10; | Plant acyltransferase family, Phenolic glucoside malonyltransferase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a flavonol 3-O-beta-D-glucoside + malonyl-CoA = a flavonol 3-O-(6-O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:20085, ChEBI:CHEBI:16816, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:58034; EC=2.3.1.116; Evidence={ECO:0000269|PubMed:33770502}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: Phenolic glucoside malonyltransferase that neutralizes phenolic glycosides in host plants (PubMed:33770502). Catalyzes the transfer of a malonyl group from malonyl-CoA to the phenolic glycosides, leading to their detoxification (PubMed:33770502). Phenolic glycosides, which are among the most abundant plant se... | Bemisia tabaci (Sweetpotato whitefly) (Aleurodes tabaci) |
P0DUV7 | PDUT_CITFR | MSQAIGILELTSIAKGMEAGDAMLKSANVNLLVSKTICPGKFLLMLGGDVGAVQQAIATGTSLAGDMLVDSLVLPNIHASVLPAISGLNSVDKRQAVGIVETWSVAACICAADRAVKASNVTLVRVHMAFGIGGKCYMVVAGDVSDVNNAVTVASESAGEKGLLVYRSVIPRPHESMWRQMVEG | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:18332146, ECO:0000305|PubMed:21245529}; Note=Seems to be bound by a single Cys residue from each of 4 subunits (Probable). 3 ligands are provided by each trimer, the fourth ligand could potentially bind another protein (Probable). The... | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872] | PF00936; | 3.30.70.1710; | Bacterial microcompartments protein family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:20417607, ECO:0000305|PubMed:18332146}. | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of this protein leads to cells with either deposits or having lamina-like structures in the cytoplasm (PubMed:18332146). Not absolutely required to make artificial BMCs (PubMed:20417... | Citrobacter freundii |
P0DUV9 | HACL_ACTC0 | MADRQDAERSGAGPARQSVPVASLVAEFLQEHGVDRVFGLQGGHIQPIWDQLARRGVRIVDVRDEGSAVHMAHAHTELTGQTAVAMVTAGPGVTNTVTAVANASVSRIPLLVIGGCPPIPQSNMGPLQDIPHTAILEPITRLARTLRSADQVLREFDEAWARASGDRGEPGPVYLEIPTDVLRRDVPPALQMREHLRAKPKRRPQPHPDDVAAVADLIRAAEKPAIISGRGARTTDGTDLVRLLDASGAAYLDTQESRGLVPDSHPAAVGSARSAVMRDTDLLITVGRQLDYQLGMGSPAVFPHAKVVRIADTASELIDN... | 4.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:34952003}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:34952003, ECO:0000305|PubMed:32351493}; Note=Binds 1 thiamine diphosphate per dimer. {ECO:0000269|PubMed:34952003, ECO:0000305|PubMed:32351493}... | isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA = acetone + formyl-CoA; Xref=Rhea:RHEA:69424, ChEBI:CHEBI:15347, ChEBI:CHEBI:57376, ChEBI:CHEBI:131780; Evidence={ECO:0000269|PubMed:34952003, ECO:0000305|PubMed:32351493}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69425; Evidence={ECO:0000269|PubMed:3495... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for 2-hydroxyisobutanoyl-CoA {ECO:0000269|PubMed:34952003}; Vmax=1200 nmol/min/mg enzyme {ECO:0000269|PubMed:34952003}; Note=kcat is 1.3 sec(-1). {ECO:0000269|PubMed:34952003}; | null | null | null | FUNCTION: A lyase that reversibly degrades 2-hydroxyisobutyryl-CoA (2-HIB-CoA) to acetone and formyl-CoA (PubMed:34952003). Probably also cleaves 2-hydroxy-2-methylbutyryl-CoA to butanone and formyl-CoA. Does not act on 2-hydroxy-2-ethylbutyryl-CoA (Probable). A C-terminal lid closes the active site upon substrate bind... | Actinomycetospora chiangmaiensis (strain DSM 45062 / JCM 15998 / CCTCC AA 205017 / NBRC 104400 / YIM 0006) |
P0DUW5 | CIF_ECOLX | MKDITLPPPTSASCLTGAISVNTEAVLSPMQHTSALHVRDFASLCSQNLKANVLLNSDDHEVPIHQKNPAAIMQNIDSNIKQMATDWGMSIEEVEVIIGREKGIVEPSCGVTANAIMKLFLDKDGFSYCFENEQTLSLEQLQERLSCMPECKSFVLRVNDGALGHAYIVDIPKGENSCRPAFLYQSDLGEGVTRKLRFEDWMTHKALTPILLDDICNYFSCMSQNKTDLEQIATLFDIDGNVKMLRKENIQYQKHDNFSFQLFEYDTDNIEKNIEIIKSLCS | 3.5.1.44 | null | symbiont-mediated perturbation of host cell cycle progression [GO:0044071] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | protein-glutamine glutaminase activity [GO:0050568]; toxin activity [GO:0090729] | PF16374; | null | Cif family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15292151, ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984, ECO:0000305|PubMed:14651638}. Host nucleus {ECO:0000269|PubMed:20941356}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:14651638, ECO:0000269|PubMed:15292151, ECO:0000269|... | CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000269|PubMed:23589306, ECO:0000305|PubMed:20688984}; Physi... | null | null | null | null | FUNCTION: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death (PubMed:14651638, PubMed:16848790, PubMed:17873042, PubMed:18705694, PubMed:19225106, PubMed:19308257, PubMed:19786559, PubMed:20688984, PubMed:20941356).... | Escherichia coli |
P0DUY2 | APOE_ARVNI | MKALWAVLLATLLTGCLAEGEPEVTDQLSWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQNSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQNTEELRSRLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQALSERLRGRLEEVGNQARDRLEEMREHMEEVRSKMEEQTQQIRLQAEIFQARLKSWFEPLVEDMHRQLANLVEKIQSSVATNSVLSTSVPQENQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Arvicanthis niloticus (African grass rat) |
P0DUY3 | APOE_CAVTS | MKVLWAALVVTLLAGCRADVEPEVEVREPAVWQSGQPWELALSRFWDYLRWVQTLSDQVQEELLSNQVTQELTLLIEDTMKEVKDYKAELEKELGPVAEDTKARLAKELQAAQARLGADMEEVRNRLSQYRSEVQAMLGQSSEELRARLTSHLRKMRKRLQRDIDELQKRMAVYKAGAQEGAERGVSAIRERLGSLIEQGRLQALTSQPLQERAQAWGEQMRGRLEKVGSQARDRLEEVREQMEEVRVKVEEQAEAFQARLKSWFEPMMEDMRRQWAELIQKVQVAVGASTSAPSQEP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Cavia tschudii (Montane guinea pig) |
P0DUY4 | APOE_CTESO | MKVLCTVLVVTLLAGCQADVQPEPEALEPAVRKSDQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKAVKAYKSELEQELVPMAEDTKARLSKELQAAQARLGADMEEVRNRLAQYRSEMQAMLGQSAEELRARLASHLRKLRKKLLRDAEDLQKRLAVYKDGASEGAERSVSAVRERLESLVEQSRARAALTSQPLQERAQAWGKRLRGRLEEVGSQARDRLEEVREQMEEVRVKMEEQAEAFQARLKGWFEPMVEDMRRQWADLIEKVQAAVGASTPTPSQKP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Ctenomys sociabilis (Social tuco-tuco) |
P0DUY5 | APOE_DASPU | MKVLWAALVVTLLAGCQADVEPELEVQEPAVWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSHVTQELTLLMEDTMKEVKAYKSELEQELAPMAEDTKARLSKELQAAQSRLRADMEEVLNRLSQYRGEVQTMMGQSGEELRARLAAHLRKLRKRLLRDVEEVQKRMDVYRAGAQEGAERSVSAIRERMGSLVEEGRLQSLPSQPLRERAQAWGEQMRGRLEKVGSQARDRLEEVREQMEEVRGKVEEQAEAFQARFKSWFEPMMEDMRRQWADLIEKVQVAVGASTAAPSQKS | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Dasyprocta punctata (Central American agouti) |
P0DUY6 | APOE_DINBR | MKVLWAVLVVTLLAGCQADVEPELEAQEPAVWQNGQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKEVKAYKSELEQELAPMAEETKARLSKELKAAQARLGADMEEVRNRLSQYRGEVQSMLGHSAEELRARLATHLRKLRKRLLRDAEDLQKRLAVYKAGASEGAERSVSAIRERLGSLVEQGRLRTAALTSQPLQERAQAWGERLRGRLEEVGSKARDRLDEVREQMEEVRLKVEEQAEAFQARLKGWFEPMMEDIRRQWADLIEKMQAAVGTSTPAPTQKP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Dinomys branickii (Pacarana) |
P0DUY7 | APOE_DOLPA | MKILWAALVVTLLAGCQADVEPEVEVREPAVWQSGQPWELALGRLWDYLRWVQTLSDQVQEELLSSKVTQELTLLMEDTMKEVTAYKSELEKELGPMAEDTKARLSKELQGAQARLGADMEEVRNRLLQYRSEVQAMLGQSSEELRARLASHLRKLRKRLQRDADDVQKRLAVYRAGAQEGAERSVSAIRERLGSLMEQGRLQALTSQPLRERAQAWGEQMRGRLEKVGSQARDRLDEVREQMEEVRVKMEEQAEAFQARLKSWFEPMVEDVRRQWAELMQKVQVAMGASTPAPSQKP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Dolichotis patagonum (Patagonian mara) |
P0DUY8 | APOE_EREDO | MKVLWAVLVVTLLAGCRADAEPELEAQEPAVWQSGQPWELALGRLWDYLRWVQTLSDQVQEELLSSQVTQELTLLMEDTMKEVKAYKAELEQELAPMAEDTRARLSKELQAAQARLGADMEEVRNRLAQYRGEVQAMLGQSAEELRARLASHLRKMRKRLLRDAEDLQKRLAVYKAGAREGAERGVSAIRERLASLVEQGRLRSALTSQPLRERAQAWGERLRGRLEEVGGQARDRLDVVREQMEEVRAKVEEQAEAFQARLKGWFEPMVEDMRRQWADLIEKVQVAVGASTPAPSQKP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Erethizon dorsatum (North American porcupine) |
P0DUY9 | APOE_GRASU | MKALWAVLLATLLTGCLSEGEPEVTEQLSWQSDQPWEQALNRFWDYLRWVQTLSDQVQEELQNSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLAQYRNEVHTMLGQSTEELRSRLSSHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGVAQPLRDRAQALGDRLRGRLEEVGNQARDRLEEMREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPLVEDMQRQLANLVEKIQASTNSVLSTSVPQENQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Grammomys surdaster (African woodland thicket rat) (Thamnomys surdaster) |
P0DUZ0 | APOE_HYDHY | MKILWAALVLTLLAGCRADVEPEVEVRETAVWQSGQPWELALSRFWDYLRWVQTLSDQVQEELLSSQVTQELTLLMEDTMKELKAYKSELEKEVGPMAEDTKARLSKELQGAQARLAGDMEEVRNRLSQYRSEVQAMLGQSSEELRARLASHLRKLRKRLQRDAEELQKRLAVYKAGAQEGAERGVSAIRERLGSLMEQGRLQALTSHPLRERAQAWGEQVRGRLEKVGSQARDRLEEVREQMEEVRVKVEEQTEAFQARLKSWFEPMVEDLRRQWAELIEKVQVAVGASTSPPSQKS | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Hydrochoerus hydrochaeris (Capybara) (Carpincho) |
P0DUZ1 | APOE_HYSBR | MKVLWAVLVVTLLAGCQADVEPALEVGEPAPEVREPAMWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKEVKAYKSELEQELGPMAEDTKARLSKELQAAQARLGADMEEVRNRLTQYRSEVQTMLGQSAEELRARLASHLRKLRKRLLRDAEDLQKRLAVYKAGAQEGAERGVSAIRERLGSLVEQGRLRAAQTSQPLRERAQAWGERLRGRLEEVGGQARDRLDVVREQMEEVRAKVEEQAEAFQARLKGWFEPVVEDMRRQWAELIEKVQVAVGASTPAPSEKH | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Hystrix brachyura (Malayan porcupine) |
P0DUZ2 | APOE_HYSCR | MKVLWAVLVVTLLAGCQADVEPALEVGEPAPEVREPAMWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKEVKAYKSELEQELGPMAEDTKARLSKELQAAQARLGADMEEVRNRLTQYRSEVQTMLGQSAEELRARLASHLRKLRKRLLRDAEDLQKRLAVYKAGAQEGAERGVSAIRERLGSLVEQGRLRAAQTSQPLRERAQAWGERLRGRLEEVGGQARDRLDVVREQMEEVRAKVEEQAEAFQARLKGWFEPVVEDMRRQWAELIEKVQVAVGASTPAPSEKH | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Hystrix cristata (North African crested porcupine) |
P0DUZ3 | APOE_MASCO | MKALWAVLLVTLLTGCLAEGEPEVADELAWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSSEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKSGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQALGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPLLEDMQRQWANLVEKIQASVATNPITSTPMPEEN | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Mastomys coucha (Southern multimammate mouse) (Praomys coucha) |
P0DUZ4 | APOE_MICOH | MKALWAVLVVTLLAGCLAEGDPELEPEVTDQLGWQTNQPWEQALGRFWDYLRWVQTLSDQVQQELQTSQVTQELTVLMEDTMTELKAYKKELEEQMGPMAEETRARLAKEVQAAQSRLGADMEDLRNRLGLYRNEVQTMLGQSTEELRARLTTHLRKLRKRLMRDAEDLQKRLAVYKAGAREGAERGVGAIRERLGPLVEQGRQRTANLGAGAAQPLRERAQALGARIRGRLEEVGNQARDRLEEVREQMEEVRAKVEEQAQQMRLQAEIFQTRLKGWFEPLVEDMQRQWANLMEKIQASVATNPIPPSSVPQESQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Microtus ochrogaster (Prairie vole) |
P0DUZ5 | APOE_MUSPA | MKALWAVLLVTLLAGCLAEGEPEVTDQLEWQSSQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSALRERLGPLVEQGRQRTANLGAGAAQPLRDRAQAFGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPIVEDMHRQWANLMEKIQASVATNPIISTPMPQENQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) |
P0DUZ6 | APOE_ONYTO | MKALWAVLVVTLLAGCLAEGEPELEPEVTDRLAWQSGQPWELALGRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTELKAYKKELEEQLGPMAEETRARLAKEVQAAQSRLGADMEDLRNRLGQYRNEVQTMLGQSTEELRARLSTHLRKLRKRLMRDAEDLQKRLAVYKAGAREGAERGVGAIRERLGPLVEQGRQRTANLGAGAGKPLQDRAQALGARIRGRLEEVGNQARDRLEEVREQMEEVRAKVEEQAQQMRLQAEIFQARLKGWFEPLVEDMQRQWANLVEKIQASVAANPIPPSSVPQESQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Onychomys torridus (Southern grasshopper mouse) |
P0DUZ7 | APOE_PERLE | MKALWAVLVVTLLAGCLAEGEPELEPEVTDRLAWQSGQPWEVALGRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTELKAYKKELEEQLGPMAEETRARLAKEVQAAQSRLGADMEDLRNRLAQYRNEVHTMLGQSTEELRARLSTHLRKLRKRLMRDAEDLQKRLAVYKAGAREGAERGVGAIRERLGPLVEQGRQRTANLGAGAGKPLQDRAQALGARIRGRLEEVGNQARDRLEEMREQMEEVRAKVEEQAQQMRLQAEIFQARLKGWFEPLVEDMQRQWANLVEKIQASVAANPIPPSSVPQESP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Peromyscus leucopus (White-footed mouse) |
P0DUZ8 | APOE_RATRT | MKALWALLLVPLLTGCLAEGELEVTDQLPGQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRTANLGSGAAQPLRDRAQALSDRIRGRLEEVGNQARDRLEEVRDQMEDVRSKMEEQTQQIRLQAEVFQARLKGWFEPLVEDMQRQWANLMEKIQASVATNSIASTTVPLENQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Rattus rattus (Black rat) |
P0DUZ9 | APOE_THRSW | MKVLWALLVVTILAGCRAEVQPELEVQAPAGWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLNSQVTQELTVLMEDTMKEVKAYKSELEQELGPMAEDTKARLSKELQAAQARLGADMEEVRNRLAQYRGEMQAMLGQSAEELRARLASHLRKLRKRLLRDAEDLQKRLAVYRAGAQEGAERGVSAIRERLGSLVEQSRLRAALTSQPLHERAQAWGERLRGRLEEVGGQARDRLDEVREQMQEVRAKMEEQAEAFQARLKGWFEPLVEDMRRQWSDLVEKVQVAVRASTAAPSENH | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Thryonomys swinderianus (Greater cane rat) (African grasscutter) |
P0DV00 | APOE_TYMBA | MKVLCTVLVVTLLAGCRADVEPEPEVLEPAVWKSGQPWELALGRFWDYVRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKAVKAYKSELEQELVPMAEDTKARLSKELQAAQARLGADMEEVRNRLALYRNEMQAMLGQSAEELRARLASHLRKLRKRMLRDAEDLQKRLAVYKDGASEGAERGVSAIRERLGSLVEQSRVRAALTSQPLQERAQAWGKQLRGRLEEVRGQAQDRLEEVREQMEEVRVKIEEQAEAFQARLKGWFEPMVEDMRRQWADLIEKVQAAVGASTPAPTQNP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; 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... | Tympanoctomys barrerae (Plains viscacha rat) |
P0DV09 | COMQ_BACSC | MKEIVHEKIQNLDLKEYLINFIDEKNHFSFGILSFKHYVALSGNRSSHILTLAGGIELLILAFDIFDDLEDEDNIEIKWMKIDPSLALNAATTLYTLGLETICSISNSAEFHRLTLKYALNAMQGQHEDLRNSPETEEECIQMMKQKAGSLTAMSAVLAAMLANGEFNQTIEDYAYKIGIIKQLENDYYGLVNDQRSDIRKKRKTLIYLFLNRKFNEASEKILKLINSHTSYHSFISDSSKFDELLFEAGLNQYVSMLIKLYEEEITASMNQLNINIKL | 2.5.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22197102}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324}; | establishment of competence for transformation [GO:0030420]; isoprenoid biosynthetic process [GO:0008299] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22197102}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + L-tryptophyl-[protein] = (2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophyl-[protein] + diphosphate; Xref=Rhea:RHEA:59492, Rhea:RHEA-COMP:15365, Rhea:RHEA-COMP:15366, ChEBI:CHEBI:29954, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:141127; Evidence={E... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:22197102}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:22197102}; | FUNCTION: Part of a major quorum-sensing system that regulates the development of genetic competence (PubMed:22197102). Involved in the maturation of the competence pheromone ComX (PubMed:22197102, PubMed:25036949). Acts by catalyzing the transfer of a geranyl group on the ComX pheromone (PubMed:22197102, PubMed:250369... | Bacillus spizizenii (Bacillus subtilis subsp. spizizenii) |
P0DV10 | STING_DROEU | MIKEMAIANNADEVDNEVRAEKGRKCFYLKKMIGDYIGNTVRIVATVVLADFLQRLYRSVVEYVHCSKYYLPEDRLWTILRRSCTYSNKSRYLVMGFILIGFLRISVSGNYKDVVPTFKFLAYMPLYWIFSNLGHSTLTYSSWVRDSHGLDYAAGMASNYFHGYLKLSLPERKADGLLHRMNVYEDKYNVTFGIKRLIILIPDEMFINGVIQSRILEKATPLETQFINRAGVNRPFKHAVYRLAEKVNGKTYYFAMEGATPMLSFFEAMHSNFSATWQMKELKREIWLKFYTHLNELIKTWPETRNLVELIIYNSHDTKG... | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of peptidoglycan recognition protein signaling pathway [GO:0061059]; positive regul... | autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; 3',2'-cyclic GMP-AMP binding [GO:0140704]; cyclic-di-GMP binding [GO:0035438] | PF15009; | 3.40.50.12100; | STING family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A0B4LFY9}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:34261127). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger... | Drosophila eugracilis (Fruit fly) |
P0DV18 | GTX3B_NEOCU | AGTKEWLNKAKDFIKEKGLGMLSAAANAALN | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF07442; | null | Ponericin-G family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34302796}. Target cell membrane {ECO:0000305|PubMed:34302796}. Note=Adopts an alpha-helical conformation in membrane-mimetic environments. {ECO:0000305|PubMed:34302796}. | null | null | null | null | null | FUNCTION: Membrane-perturbating peptide with a few moderate activities (PubMed:34302796). It is insecticidal, since it induces reversible paralysis in insects (L.cuprina) after 1 hour, but fails to kill them (PubMed:34302796). It is also antiparasitic, since it moderately inhibits the larval development of the major pa... | Neoponera commutata (Large hunting ant) (Pachycondyla commutata) |
P0DV24 | PYCC1_ECOLX | MSFKDVTAKNFKGLKNVSLKKSMAMEGHTLVGTEARLGDAFELCESFSTSPSNIIEYEYQEEIRPFFQKAGLNKHSIGTHPELTGLGVGMIYNQYTVTMFVDIRKSSRLSLLLPLEQVYVVKNRILQACIDIVRALDGYPHRLMGDALMAFFGRSDVSKEDAIADAINAASTLRLILMDYIFPSLNEDIGEQIDLGVRIGLDYGAEDEVVWGNFGLGSFCEVTALGLPVDMTAKLQQLADKNTAMLGQGILDYIDFPEEYTKPKVKSGEELKYIIPNITNKEGQPINRRIRLLNMARYQELLPFKLNDKKMASAILYPNQ... | 4.6.1.6 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34644530}; Note=Cannot be replaced by Mg(2+). {ECO:0000269|PubMed:34644530}; | cyclic nucleotide biosynthetic process [GO:0009190]; defense response to virus [GO:0051607]; intracellular signal transduction [GO:0035556] | cytoplasm [GO:0005737] | adenylate cyclase activity [GO:0004016]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF18134;PF00211; | 3.30.70.1230; | Adenylyl cyclase class-4/guanylyl cyclase family, Pyrimidine cyclase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=CTP = 3',5'-cyclic CMP + diphosphate; Xref=Rhea:RHEA:14737, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58003; EC=4.6.1.6; Evidence={ECO:0000269|PubMed:34644530}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.0. {ECO:0000269|PubMed:34644530}; | null | FUNCTION: Pycsar (pyrimidine cyclase system for antiphage resistance) provides immunity against bacteriophage. The pyrimidine cyclase (PycC) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signal activates the adjacent effector, leading to bacterial cell de... | Escherichia coli |
P0DV44 | NADA3_NEIMI | MKHFPSKVLTTAILATFCSGALAATNDDDVKKAATVAIAAAYNNGQEINGFKAGETIYDIDEDGTITKKDATAADVEADDFKGLGLKKVVTNLTKTVNENKQNVDAKVKAAESEIEKLTTKLADTDAALADTDAALDATTNALNKLGENITTFAEETKTNIVKIDEKLEAVADTVDKHAEAFNDIADSLDETNTKADEAVKTANEAKQTAEETKQNVDAKVKAAETAAGKAEAAAGTANTAADKAEAVAAKVTDIKADIATNKDNIAKKANSADVYTREESDSKFVRIDGLNATTEKLDTRLASAEKSIADHDTRLNGLD... | null | null | cell adhesion [GO:0007155] | cell outer membrane [GO:0009279]; cell surface [GO:0009986] | null | PF03895; | 3.30.1300.30;1.10.287.950; | Autotransporter-2 (AT-2) (TC 1.B.40) family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:15660996}. Cell surface {ECO:0000269|PubMed:12045242, ECO:0000269|PubMed:15660996, ECO:0000269|PubMed:20971901}. | null | null | null | null | null | FUNCTION: Adheres to and induces bacterial uptake by human epithelial cells in a microfilament-dependent process. Binding is reduced by pronase treatment, suggesting there is a protein receptor on the human cells (PubMed:15660996, PubMed:30327444). Possible human protein receptors include integrin beta-1 (ITGB1) and ox... | Neisseria meningitidis serogroup B |
P0DV46 | GSDM_BRATP | MNCSRDTGDELMAALLAEGINLILPPRDNIAPGDLIIADPQGGARLGGWHEVFNLQLSPEVATDPGFKSFQFRASSILQVGVAASVMGRVLQALGLGSGSFSSAFSSSNADTIQLSIVAPANKELTNFDAVLVQMNEAKAEPAQGYTDRNFFVVTKVWRARGIRISVADKSKKQVDLSAKAVEELTAKAKMELKREDTGSYAFLAASQLIFGLTLREVTYKDGAIVDVAPTGPLKFRGKGPGDPFAFIGDDAFVDLPES | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | null | null | null | Bacterial gasdermin family | PTM: Palmitoylation helps stabilize the inactive state; may self palmitoylate. {ECO:0000269|PubMed:35025633}. | SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm {ECO:0000305|PubMed:35025633}.; SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner membrane {ECO:0000250|UniProtKB:P0DV48}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Gasdermin bGSDM]: Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0098714_109514) is toxic in E.coli on solid medium (PubMed:35025633). Cleavage of this precursor by its dedicated protease releases the ac... | Bradyrhizobium tropiciagri |
P0DV48 | GSDM_RUNZN | MECNDPFVVALKDKGYSLVAYPKTSIRPLHIYEHTIKNAFKRIWIQSEAQPTSGFIKSLFSDKIHGAIGLSDGQGIDIDLRKTNSLSSAVAAKILESYFQDSAPSFDLAFENSSSVIFHIEEIITTDADEISLRNWLNDNQNELREIYKEEIKKGNFFVATSLLRAKKMRMQFERKNKGELGVDVSKIKNLPVDAKLESKIEGSTYDRLVFETPDEGIVFGVKLVRLFFSDNGILTIDKKQDFNRVLGENMALNLFTEIQDAGFIEVT | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | null | null | null | Bacterial gasdermin family | PTM: [Gasdermin bGSDM]: Cleavage by the adjacently encoded protease (G563DRAFT_02009) between Leu-247 and Gly-248 relieves autoinhibition, releasing the N-terminus which initiates loss of cell integrity. {ECO:0000269|PubMed:35025633}.; PTM: Palmitoylation helps stabilize the inactive state; may self-palmitoylate. Palmi... | SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm {ECO:0000269|PubMed:35025633}.; SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner membrane {ECO:0000269|PubMed:35025633}; Multi-pass membrane protein {ECO:0000305}. Note=Upon proteolysis the protein forms membrane-associated puncta. {ECO:0000269|PubMed:35... | null | null | null | null | null | FUNCTION: [Gasdermin bGSDM]: Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Cleavage of this precursor by its dedicated, neighboring protease (G563DRAFT_02009) releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and trigge... | Runella zeae (strain ATCC BAA-293 / DSM 19591 / LMG 21438 / NS12) |
P0DV56 | DART_THEA5 | MPQQGLAYPVPTLIYHITHLNNLQGILQRGGLLPYSQRPPTQQNVAYGHIQAHRAQVVVPVGPRGKLHDYVPFYFCPRSPMLYAIHTQQTDYQGDQRPILHLVSSAQKVAEARIPFVFTDRHAAVQYVCFFHKLEHLKALDWQAIQASYWANVREKKQAEFLVKDFFPWELVEEIGVIDKTIQAQVESILAQFPDLHHPPVRVRRSWYYKKRLCSASCEATF | 2.4.2.- | null | null | null | DNA binding [GO:0003677]; glycosyltransferase activity [GO:0016757]; nucleotidyltransferase activity [GO:0016779] | PF14487; | null | DarT ADP-ribosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a thymidine in DNA + NAD(+) = an N-(ADP-alpha-D-ribosyl)-thymidine in DNA + H(+) + nicotinamide; Xref=Rhea:RHEA:71651, Rhea:RHEA-COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:137386, ChEBI:CHEBI:191199; Evidence={ECO:0000255|PROSITE-P... | null | null | null | null | FUNCTION: Toxic component of a hybrid type II/IV toxin-antitoxin (TA) system. Its toxic effect is neutralized by cognate antitoxin DarG. ADP-ribosylates ssDNA on the second thymidine of the consensus sequence 5'-TNTC-3'; the protein does not auto-modify. Has no activity on dsDNA in vitro. This leads to a decrease in DN... | Thermus aquaticus (strain ATCC BAA-2747 / Y51MC23) |
P0DV65 | S1544_SULMK | MVDTMNARNTQFTKAFHALKQNAGSHSPSMEDLKKMFPTLEIKIDACYLSNPYASELVLDYIDRELIQTNAYKKVLTHYPSQQRSLQKVMAESLHVKPENIFIGNGATEIIQMLLQQEEVQKVALMIPTFSSYYEFVGKGCEVVYFPLNERDDYSFDADKYCQFIENEQPDTVVLINPNNPNGAYLSLEKMHILLKRLAFVPRIIIDESFIHFAYEDEALTCLSSTVLFDMYPNVIIVKSLSKDFGIAGVRLGYALMDSRKIDALLEHGFLWNINGIGEYCLRLFVREDFLKRYEEARKQYIKEMCRFKEALLGIENVYV... | 4.1.1.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:31325159}; | biosynthetic process [GO:0009058] | null | carboxy-lyase activity [GO:0016831]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + O-phospho-L-serine = CO2 + phosphoethanolamine; Xref=Rhea:RHEA:69548, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57524, ChEBI:CHEBI:58190; Evidence={ECO:0000269|PubMed:31325159}; | null | PATHWAY: Cofactor biosynthesis. {ECO:0000305|PubMed:31325159}. | null | null | FUNCTION: Pyridoxal phosphate (PLP)-dependent decarboxylase involved in the biosynthesis of norcobamides, cofactors in the tetrachloroethene reductive dehalogenase PceA of S.multivorans. Catalyzes the decarboxylation of L-serine O-phosphate to ethanolamine O-phosphate, the precursor for the linkage between the nucleoti... | Sulfurospirillum multivorans (strain DM 12446 / JCM 15788 / NBRC 109480) |
P0DV78 | OXLA2_BOTJR | ADDRNPLEECFRETDYEEFLEIARNGLSDTDNPKEGWYANLGPMRLNEFSQENENAWYFIKDPGVLDYPVKPSEVGKHDDIFAYEKRFDEIVGGMDKEVTVTYQTSEKFEPPLPPK | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q6TGQ9}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: Glycosylated. {ECO:0000255}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28495622}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:28495622, ECO:0000269|PubMed:30534149}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for L-Phe {ECO:0000269|PubMed:30534149}; KM=0.3 mM for L-Leu {ECO:0000269|PubMed:30534149}; KM=0.6 mM for L-Met {ECO:0000269|PubMed:30534149}; KM=1.1 mM for L-Tyr {ECO:0000269|PubMed:30534149}; KM=2 mM for L-Ile {ECO:0000269|PubMed:30534149}; KM=14.1 mM for ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-9. {ECO:0000269|PubMed:30534149}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:30534149}; | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (By similarity) (PubMed:28495622). Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe a... | Bothrops jararacussu (Jararacussu) |
P0DV84 | ALK_CANLF | MGSVGLLGLLLLRLSVTASGSGAGTGSGTGSGTGTGTGQLVGSPATGPALQPREPLSYSRLQRKSLAVDFVVPSLFRVYARDLLLPPWSSSEPRAGWTEARGSLALDCAPLLRLLGPPPGVSWAEGASSPAPAQARTLTRVLKGGSVRKLRRAKQLVLELGEEAILEGCVGPSPEEVTAGLLQFNLSELFSWWIRHGEGRLRIRLMPEKKASAVGREGRLSAAIRASQPRLLFQILGTGHSSLESPTSLPSPPPDPFAWNLTWIMKDSFPFLSHRSRYGLECSFDFPCELEYSPPLHDLGNQSWSWRRVPSEEASQMDLL... | 2.7.10.1 | null | phosphorylation [GO:0016310]; regulation of cell population proliferation [GO:0042127]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF12810;PF00629;PF07714; | 2.60.120.200;4.10.400.10;1.10.510.10; | null | PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. In cells not stimulated by a ligand, receptor protein tyrosine phosphatase beta and zeta complex (PTPRB/PTPRZ1) dephosphorylates ALK at the sites in ALK that are undergoing autophosphorylation through autoactivation. {ECO:000025... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM73}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UM73}. Note=Membrane attachment is essential for promotion of neuron-like differentiation and cell proliferation arrest through specific activation of the MAP kinase pathway. {ECO:0000250|Uni... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000250|UniProtKB:Q9UM73, ECO:... | null | null | null | null | FUNCTION: Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system (By similarity). Also acts as a key thinness protein involved in the resistance... | Canis lupus familiaris (Dog) (Canis familiaris) |
P0DW16 | RBM20_PIG | MVLAAAMSQDAEPSGPEQPDRDARSVPGAPAPPAPPGPRGMQPPPPPPPPPPPPPQAGLPQIIQNAAKLLDKTPFSVSNPNPLLPSPASLQLAQLQAQLTLHRLKLAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSMISAPHGHTGVPPHATTVPSTRFPSNAITFSAGQTRGPGPSVNLPSQPPNTMVMHPFSGVMPQTPAQPAVILGIGKTGPAPAAAGFYEYGKATSGQAYGSETDSQPSFLPASASTSGSVTYEGHYSHSGQDSQAAFPKDFYGPTSQGSQVAGTFAADTAGGLKGEVGPLLQGPNSQWE... | null | null | heart formation [GO:0060914]; mRNA processing [GO:0006397]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing [GO:0008380] | cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634] | mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157]; splicing factor binding [GO:1990935]; zinc ion binding [GO:0008270] | null | 3.30.70.330; | null | PTM: Phosphorylation regulates the subcellular localization (By similarity). Phosphorylation of Ser-637 and Ser-639 in the RS (arginine/serine-rich) region promotes nuclear localization of the protein (By similarity). In contrast, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:33188278}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:33188278}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:33188278). Also localizes to cytoplasmic ribonucleo... | null | null | null | null | null | FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH (PubMed:33188278). Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predom... | Sus scrofa (Pig) |
P0DW27 | MNS60_MOUSE | MKDEVVVVTGLAAMEPLIVHRMIVERTAAGTMIIETWTTAHTHESMAVRRASMSMTTHLKSKVQRIPTRPPRAPRLSVGGGGGTGTVPLARQASPETATIGTRTIGPSKGRRRRRRMRRRRRRRPVTSSC | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; mRNA stabilization [GO:0048255]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mRNA splic... | nucleolus [GO:0005730]; nucleus [GO:0005634] | RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P0DW28}. | null | null | null | null | null | FUNCTION: Acts as a late-stage inhibitor of pre-60S ribosome assembly by preventing pre-60S ribosome export from nucleus. {ECO:0000250|UniProtKB:P0DW28}. | Mus musculus (Mouse) |
P0DW60 | THSA_ENTFC | MDKKVLIKRFSEAIEKGNAAIFAGAGLSMSQGYVSWPELLNDPATEIGLDSKKETDLVTLAQYYKNENGGSRGILNQILMDNFGEELEISENHRILASLPIETYWTTNYDHLIEKSIREAYKNPQVKKNYTQLATTNPNVDTIVYKMHGDIDDVSSTVITRDDYEKYDDDSYALFKETLKGDLLTKTFLFLGFSFTDPNLERILSDIRWVLRENQRPHYCIMRKILKENFVDSEDFFDQERYNYELTKRRLQINDLSRFSINVVEVDDYSEITDILKSIRKKYLRKTIFISGSAVDYTPFTSESKGLKFVEKLAYRLSES... | 3.2.2.5 | null | defense response to virus [GO:0051607] | null | hydrolase activity [GO:0016787]; nucleotide binding [GO:0000166] | PF13289;PF18185; | null | Soluble Thoeris ThsA family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={E... | null | null | null | null | FUNCTION: NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB (maybe AS248_15445). Activated by 3' cyclic ADP-D-ribose (3'cADPR) but not its isomers 2'cADPR, cADPR and very weakly by ADPR; binds 3'cADPR better than 2'cADPR (PubMed:36048923). Upon activation binds and... | Enterococcus faecium (Streptococcus faecium) |
P0DW82 | NCAP_SFTSV | MSEWSRIAVEFGEQQLNLTELEDFARELAYEGLDPALIIKKLKETGGDDWVKDTKFIIVFALTRGNKIVKASGKMSNSGSKRLMALQEKYGLVERAETRLSITPVRVAQSLPTWTCAAAAALKEYLPVGPAVMNLKVENYPPEMMCMAFGSLIPTAGVSEATTKTLMEAYSLWQDAFTKTINVKMRGASKTEVYNSFRDPLHAAVNSVFFPNDVRVKWLKAKGILGPDGVPSRAAEVAAAAYRNL | null | null | null | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723] | PF05733; | null | Phlebovirus nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D3K5I7}. Host cytoplasm {ECO:0000250|UniProtKB:D3K5I7}. Host nucleus {ECO:0000250|UniProtKB:D3K5I7}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi apparatus {ECO:0000250|UniProtKB:I6WJ72}. | null | null | null | null | null | FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases (PubMed:23702688). Displays high affinity for single-stranded nucleic acid (PubMed:23702688). The encapsidated genomic RNA is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:23702688). The ribonucleoprotein has a non-helical structure (By si... | SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus) |
P0DW93 | LNBX_BIFL2 | MTSRQGRQAIAATAAMGVAVALALPTAAFAQSATQGKETATTTSSGTTYYVSSAHGDDANAGTSENAPWKSLTKVNDIASDLGPGDSVLLEYGSEFNDQYLHIKDTAGNADAPITISAYGDADEGKPVIASNGVKGSQWEQDYRANVGNHKNKGTVSTTLLLKDVSYITVSNLEITNDDADVYDPIDTWKWTDTPDSDGTKLDRSASRMDRTGVAGIAENGATMSNVTLDNLYIHDVDGNIYNKHMANGGIYFMAHYPMENTSAETDVWLREHVSRFDHVTIRNSTVKDVDRWGIAVGYTAYLNYIDANYGDGSIDDALI... | 3.2.1.140 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23843461}; Note=Binds 3 Ca(2+) ions per subunit. Calcium ions are required for efficient protein folding. {ECO:0000269|PubMed:23843461}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23843461}; Note=Binds 1 Mg(2+) ... | polysaccharide catabolic process [GO:0000272] | plasma membrane [GO:0005886] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; metal ion binding [GO:0046872] | PF07554;PF18957; | 1.20.1270.90;2.160.20.10; | Glycosyl hydrolase 136 (GH136) family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:23843461}. | CATALYTIC ACTIVITY: Reaction=beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H2O = beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + lactose; Xref=Rhea:RHEA:21568, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:27707, ChEBI:CHEBI:30248; EC=3.2.1.140; Evidence={ECO:0000269|PubMed:23843461}; Physiolog... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=401 uM for lacto-N-tetraose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) {ECO:0000269|PubMed:23843461}; KM=119 uM for chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) {ECO:0000269|PubMed:23843461}; KM=186 uM for chromogenic beta-D-... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.4 with LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as chromogenic substrate. {ECO:0000269|PubMed:23843461}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius with LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as chromogenic substrate. {ECO:0000269|PubMed:23843461}; | FUNCTION: Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs) (PubMed:23843461, PubMed:28392148). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-... | Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) |
P0DW98 | TXVE_PROJR | MAAYLLAVAILFCIQGWPSATVQGQVMPFMEVYERSACQTRETLVSILKEYPDEVAHLFKPSCVPVLRCSGCCSDESLKCTATGKHSVGREVMRVDPHKGTSKIEVMQFKEHTDCECRPRSPGDVNNGRNPEEGEPRARFPFV | null | null | induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of protein phosphorylation [GO:0001934]; response to hypoxia [GO:0001666]; sp... | extracellular space [GO:0005615]; membrane [GO:0016020] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; toxin activity [GO:0090729]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184] | PF00341; | 2.10.90.10; | PDGF/VEGF growth factor family, Snake venom VEGF subfamily | PTM: The N-terminus is blocked for N-terminal sequencing, suggesting a Pyrrolidone carboxylic acid at Gln-25. {ECO:0000269|PubMed:26107411}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26107411}. | null | null | null | null | null | FUNCTION: Snake venom VEGFs that may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. This protein induces an increase in capillary permeability when intradermally injected into mice (PubMed:26107411). Also provokes a drastic hypotensive effect after intravenous inj... | Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii) |
P0DX14 | INLPC_STRC4 | MDRLHHPQLQTLVQTTSFHAQHEPTTPAVLCEGRTLTYEQLHRESNRIAHALKAAGLAPGDRVAYLGKESEHYYEILFGCAKSGTVLVPVNWRLTAPEVSHILQDSGTRLLFLEDEFGPVVEKMPAAPPETIVALGESFAAWKASHLDTDPKPHDVTPDTPVAQLYTSGTTGLPKGVVLAHRSFFAIRDALASEGLDWIDWRVGDIALIGIPGFHIGGLWWATQNFNAGTTVVAMRAFAARQAVDLIRDLGITTACVVPAMLRMMLTEPGVGAKDFTTLRKTVYGGSPISEALLEESLAVLDCEFAQIYGLTETGNTAVC... | 6.2.1.-; 6.2.1.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5SKN9}; | fatty acid metabolic process [GO:0006631] | null | ATP binding [GO:0005524]; ligase activity [GO:0016874]; metal ion binding [GO:0046872] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479, ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.4... | null | null | null | null | FUNCTION: Acyl:acyl-carrier protein ligase involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Shows a strong preference for fatty acids with a short/medium-chain length (C4-C8) in vitro, and accepts alpha,beta-unsaturated fatty acids such as crotonate, which seems to be a physiological s... | Streptomyces coeruleorubidus |
P0DX29 | PETH1_AMYMS | MSALTSQPTSSGSSEKIPRLRGWRAKAAGVVLAALALTTGVAAPAPAAANPYERGPDPTTASIEATSGSFATSTVTVSRLAVSGFGGGTIYYPTTTTAGTFGALSIAPGFTATQSSIAWLGPRLASQGFVVFTIDTLTTSDQPDSRGRQLLASLDYLTQQSSVRSRIDSTRLGVVGHSMGGGGTLEAARSRPTLQAAVPLTAWDLTKNWSTLQVPTLVVGAQSDTVAPVASHSIPFYTSLPSTLDRAYLELRGASHFAPNSPNTTIAKYTLSWLKRFIDNDTRYEQFLCPIPSTSLSISDYRGNCPHNG | 3.1.1.1; 3.1.1.3; 3.1.1.74 | null | medium-chain fatty acid catabolic process [GO:0051793]; triglyceride catabolic process [GO:0019433] | extracellular region [GO:0005576] | carboxylesterase activity [GO:0106435]; cutinase activity [GO:0050525]; triglyceride lipase activity [GO:0004806] | null | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19806375, ECO:0000269|PubMed:35195792}. | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:19806375, ECO:0000269|PubMed:21145735, ECO:0000269|PubMed:33598102, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.099 mM for p-nitrophenyl palmitate (p-NPP) (at pH 8.0 and 60 degrees Celsius) {ECO:0000269|PubMed:21145735}; Vmax=2.53 mmol/min/mg enzyme with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius) {ECO:0000269|PubMed:21145735}; Note=kcat... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with p-nitrophenyl palmitate (p-NPP) as substrate (PubMed:19806375, PubMed:21145735). At pH 7 and 9 displays around 90% of relative activity (PubMed:21145735). Stable at pH range 6-9 retaining over 95% of relative activity after 24 hours (PubMed:21145735)... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius with p-nitrophenyl palmitate (p-NPP) as substrate (PubMed:19806375, PubMed:21145735). Hydrolyzes p-NPP in the broad temperature range of 20-80 degrees Celsius (PubMed:19806375). Highly thermostable (PubMed:19806375, PubMed... | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (By similarity). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:21145735, PubMed:33598102). Has a preference for medium chain length (C-4 to C-12) fatty acid esters (P... | Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei) |
P0DX54 | WAAC_ECOK8 | MRVLIVKTSSMGDVLHTLPALTDAQQAIPGIKFDWVVEEGFAQIPSWHAAVERVIPVAIRRWRKAWFSAPIKAERKAFREALQAKNYDAVIDAQGLVKSAALVTRLAHGVKHGMDWQTAREPLASLFYNRKHHIAKQQHAVERTRELFAKSLGYSKPQTQGDYAIAQHFLTNLPTDAGEYAVFLHATTRDDKHWPEEHWRELIGLLADSGIRIKLPWGAPHEEERAKRLAEGFAYVEVLPKMSLEGVARVLAGAKFVVSVDTGLSHLTAALDRPNITVYGPTDPGLIGGYGKNQMVCRAPGNELSQLTANAVKQFIEENA... | 2.4.99.23 | null | lipopolysaccharide core region biosynthetic process [GO:0009244] | plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757] | PF01075; | 3.40.50.2000; | Glycosyltransferase 9 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P24173}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24173}; Cytoplasmic side {ECO:0000250|UniProtKB:P24173}. | CATALYTIC ACTIVITY: Reaction=ADP-L-glycero-beta-D-manno-heptose + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A = ADP + an L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-lipid A + H(+); Xref=Rhea:RHEA:74067, ChEBI:CHEBI:15378, ChEBI:CHEBI:61506, ChEBI:CHEBI:176431, ChEBI:CHEBI:193068, ChEBI:CHEBI:456216; EC=2.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for ADP-heptose {ECO:0000269|PubMed:16963083}; KM=7 uM for Kdo2-lipid A {ECO:0000269|PubMed:16963083}; | PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. {ECO:0000269|PubMed:16963083}. | null | null | FUNCTION: Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS) (PubMed:16963083). Catalyzes the addition of the first heptose unit to one 3-deoxy-D-manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module (PubMed:16963083). {ECO:0000269|PubMed:16963083}. | Escherichia coli O18:K1:H7 (strain RS218 / NMEC) |
P0DX82 | CAP2_ENTH5 | MSTVVQQVPAELQAALTLINNDPRMRTNNAWALSADKRWSLKFTAELSVPCSSFMPDNSVWHLVLWQEETLIRIEVYPDKSEGISATFQHQNYNFSDASTREWTSGNPCLENTPTVFGRNLWGLEPEALLDRISWRLSRLLLWIDAAAQEKLATTGDAVELPAFPDQSPFTVIGFSEQIDDLPFWASKTGEWGFASSTGLPGAHGTLFLREFLDNKGKLIRTTKWSPFMRKGARTTNAVWSVLPTLPVLAPWQAPRTWQELSHCFAQCGLSLPDLFSDIGRSVRALRKQRAPGLLLLGFPLENKIGDEPARIHWLALRLA... | 2.3.2.- | null | defense response to virus [GO:0051607] | null | transferase activity [GO:0016740] | PF00899; | 3.40.50.720; | HesA/MoeB/ThiF family | null | null | null | null | null | null | null | FUNCTION: CD-NTase priming component of a CBASS antiviral system (PubMed:36755092). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages (PubMed:32544385, PubMed:36755092). The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serv... | Enterobacter hormaechei subsp. hoffmannii (strain UCI 50) |
P0DX84 | DMDB_RUELI | MLGQMMTQPLLISSLIDHAARYHGQTEIVSVETDGTVTRTNWGEIAANARRMGSALTKLGLQPQDRIGTLAWNNRRHLEIYYAASGAGFVCHTINPRLFPEQLVYIINHAQDRVLFFDATFLPLVAAIRDQLTEVKHFVLMGPRNEDALQQIPGLEFYDELIETGDTDFEWPVFDENTASSLCYTSGTTGHPKGVLYSHRSTVLHSFASNTRDVIGYSAMDVVMPVVPMFHVNAWGSPYGCAMSGAQMVLPGPDLHGEALVNLIDTYGVTLAMGVPTIWQGLLAHAAKCGTKLESLERTVIGGAACPPSMIATFREKYGV... | 6.2.1.44 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30677184}; | fatty acid metabolic process [GO:0006631] | null | ATP binding [GO:0005524]; ligase activity [GO:0016874]; metal ion binding [GO:0046872] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=3-(methylsulfanyl)propanoate + ATP + CoA = 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:43052, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:49016, ChEBI:CHEBI:57287, ChEBI:CHEBI:82815, ChEBI:CHEBI:456215; EC=6.2.1.44; Evidence={ECO:0000269|PubMed:30677184}; Physi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for MMPA {ECO:0000269|PubMed:30677184}; KM=0.8 mM for ATP {ECO:0000269|PubMed:30677184}; KM=0.4 mM for CoA {ECO:0000269|PubMed:30677184}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:30677184}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:30677184}; | FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton (PubMed:30677184). Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA) (PubMed:30677184). {EC... | Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) |
P0DX85 | CAPV_PSEU5 | MTGIPTYHVLALSGGGYRGLYTATVLAELETVLGRPIASHFDLICGTSAGGMLALGLAAEIPAYELKALFEEQGSRIFGCRSLPRRLLGFWLTAKHDSAGLKEVLTERFQGTTIGDLKHRVLVPAVNYSTGRGQFFKTPHHPSFELDHRMKVVDVALATAAAPVYFPLARNDRGVFADGGLVGNAPGLFGLHEVKTFLAPKQDALVRVLAIGTMTIGATVRGGASLDRGFGKWRGGLFDLVISAQESSVDHMLRQALGNNYFQIDDKATPDQSKDVKALDRVSIGATNTLKDRGNHAAQRALGDPLFQPFRAHQADAPIF... | 3.1.1.32 | null | defense response to virus [GO:0051607]; lipid catabolic process [GO:0016042] | null | hydrolase activity [GO:0016787] | PF01734; | 3.40.1090.10; | Patatin family | null | null | 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:0000250|UniProtKB:Q9KVG8, ECO:0000305|... | null | null | null | null | FUNCTION: Effector phospholipase of a CBASS antiviral system (PubMed:36750095). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals.... | Pseudomonas aeruginosa (strain BWHPSA011 / Pa011) |
P0DX86 | CDNA_PSEU5 | MLNLSPLFFTTLDDESCMHDELDLTPGQRAWIASARTDVRDCLRTGIPRVLRANGYTEDVPQPRFFTQGSWAYKTLNAPAQHPQQADVDDGCYLPMSFVSQTKRPSTAATVFFAAAEEALKPLVEERRWKLVTDKPTCIRIVIAAYAHIDIPLYAIPDEEFVTLAKASMERYGYDSLTEAVNMAERDAWTALPADKVLLAHRECNWMSSDPRPVKEWFLGEVEAKGEQFRRVVRYLKAFRDWKWSSGGPASILLMAAAAPLFEKRDRRDDLALLDVVAALPARLRGGVNNPVEESESLTERLGQAGVEDAAKAFEEFEKV... | 2.7.7.- | null | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779] | PF21654;PF21713; | null | CD-NTase family, A01 subfamily | PTM: In bacteria expressing capV-cGAS-cap2-cap3, this protein is conjugated to about 130 cellular proteins by Cap2; more conjugated protein is found in the absence of Cap3 (PubMed:36848932). {ECO:0000269|PubMed:36848932}. | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71501; Evidence={ECO:0000269|PubMed:30787435, ECO:0000305|PubMed:36750095}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000269|P... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:30787435, PubMed:36750095). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response ... | Pseudomonas aeruginosa (strain BWHPSA011 / Pa011) |
P0DX87 | CAP2_PSEU5 | MSSAAAVADVIEAFKQRGFEFVGKTDDGWFRLHGRLTPPQADKGCPCEVQLDPTFFNLPRIRLLEIPPELPAAVPHLGADGGLCYLAKGTVVLDIYDPVGQSLACLQRAAVVFGQIMQGEMIEDLAEEFFAYWHGWHCFVDMQGEDLGRQNCIVAHANGCPLWFITDNEDRTTEKLKSLGYQVTDRTVLTYRVKTGAQPRPLTSNWPPETVGDILAWQSTLDPRCRRKIHERIKEGERKKANGVLIVIESPLMTYGFAVLYDRQSLVQKSKLIDRRDSSYGLKVMPISVVRIDDRYLAQRNMPNSKTLAGKNIAVVGCGT... | 2.3.2.- | null | defense response to virus [GO:0051607] | null | transferase activity [GO:0016740] | PF14461;PF00899; | 3.40.50.720; | HesA/MoeB/ThiF family | null | null | null | null | null | null | null | FUNCTION: CD-NTase priming component of a CBASS antiviral system (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signal... | Pseudomonas aeruginosa (strain BWHPSA011 / Pa011) |
P0DX98 | CDNE_ENTF2 | MSKFSESTLSGWTKPASVTEEDRIENTISMIKSAIKNDNNFDNLVYEVFVQGSYGNNTNVRTNSDIDVNIMLTSTFYSKYPEGKTNSDYGFTDGTITYNEYKNLILTALTNKFGTGNVTVGNKSIKITSNSYRVEADCIPSLLYRNYEYENSSSPNNYIEGIKYFASDNTSVVNYPKVHINNGIEKNNQTHKNYKRLVRVIKRLRNKMTAENHFTNENITSFLIECLIWNVPNNYINDYDTWDETIKQTLIFIKSSINDNSYKNWTEVSGMFYLFHNNRKWTSDDVSSFVNSLWSFMEY | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:37604815}; Note=Binds 2 Mg(2+) ions per subunit; only 1 is seen in the crystal structures (PubMed:37604815). {ECO:0000269|PubMed:37604815}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; nucleotidyltransferase activity [GO:0016779] | null | 3.30.460.10; | CD-NTase family, E02 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 UTP = 2',3'-c-di-UMP + 2 diphosphate; Xref=Rhea:RHEA:78003, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:228233; Evidence={ECO:0000305|PubMed:37604815}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78004; Evidence={ECO:0000305|PubMed:37604815}; CATALYTIC ACTIVITY: Reaction=CT... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:37604815). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific s... | Enterococcus faecalis (strain EnGen0062 / B16457) |
P0DXA3 | CDNB_ESCAL | MNCSDLFYADTNTENTLHQRTQLSEVILSKGIAKKNELIEFLRQELKEAFDCDVRFWLQGSYKSHTLIKPVDKFSSYDIDIGVYLFFDAENEGVDSKDVKETLRDALLSYCSINNEAKLQESKNACEGLKFSTFLTVDTPIYYKTDTKIKLATDKGWSDSDPKAIQDWITNYYKDKSDRALMKRLVRYFKAWVNVKWQNTGFKKIPSLAINVLVAQHMKQHVREDDCFIYTALSICEELESTLIVRNPLNNSNLISMPQDAECFAHQKLDELKQVCLSCIKSDDIKRGAHFSNLFQHYFPQISLDSATGSTGLPTVVNVP... | 2.7.7.-; 2.7.7.65; 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A853PXE5}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:A0A853PXE5}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779] | PF18134;PF21654; | null | CD-NTase family, B06 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71501; Evidence={ECO:0000269|PubMed:30787435, ECO:0000305|PubMed:34784509}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000305|P... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:30787435, PubMed:34784509). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response ... | Escherichia albertii |
P0DXA6 | CDNE_STASC | MLFTEEQLKLYSKPLSESEKEKCENAIRIIQESLESLGYETKKGIHRNNEDTLSYQIKMTNPSKDYELSIFVKGSYATNTNVRQNSDVDIAVVKESEFFDKYREGKTRENYKFVSSNKPPYHFKDEVEEALIERFGRSEVRRGNKAIRINGNTYRKETDCVPCFRYRDYSNDYMDDPNNFIGGITIYSDKGERIINYPEQHINNSVIKNNNTNYKYKKMVRIIKEIRYQLIDSKNENAKQTSSFGVEGLFWNIPDYKYSNDEMLGDTFNALIAFLIDNIDKLREFKEPNDILNLCDSQEKNNVYKNFILDVKNYFEYSGE... | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0DSP2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0DSP2}; | defense response to virus [GO:0051607] | null | ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; RNA binding [GO:0003723] | PF01909; | 3.30.460.10; | CD-NTase family, E03 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',2'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:68344, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:177334; Evidence={ECO:0000269|PubMed:37968393}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68345; Evidence={ECO:0000269|PubMed:37968393}; | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:37968393). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage (PubMed:37968393). The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these s... | Staphylococcus schleiferi |
P0DXD2 | CBH_BIFL2 | MCTGVRFSDDEGNTYFGRNLDWSFSYGETILVTPRGYHYDTVFGAGGKAKPNAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFVHEPVEGTENVATFEFPLWVARNFDSVDEVEEALRNVTLVSQIVPGQQESLLHWFIGDGKRSIVVEQMADGMHVHHDDVDVLTNQPTFDFHMENLRNYMCVSNEMAEPTSWGKASLTAWGAGVGMHGIPGDVSSPSRFVRVAYTNAHYPQQNDEAANVSRLFHTLGSVQMVDGMAKMGDGQFERTLFTSGYSSKTNTYYMNTYDDPAIRSYAMADYDMDSSELISVAR | 2.3.1.-; 3.5.1.-; 3.5.1.24; 3.5.1.74 | null | null | null | null | null | null | Peptidase C59 family | null | null | CATALYTIC ACTIVITY: Reaction=glycocholate + H2O = cholate + glycine; Xref=Rhea:RHEA:19353, ChEBI:CHEBI:15377, ChEBI:CHEBI:29746, ChEBI:CHEBI:29747, ChEBI:CHEBI:57305; EC=3.5.1.24; Evidence={ECO:0000250|UniProtKB:Q9KK62}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19354; Evidence={ECO:0000250|UniProtKB:Q9KK62}... | null | PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000269|PubMed:38326609}. | null | null | FUNCTION: Possesses dual functions in bile acid metabolism (PubMed:38326609). Acts as a bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids) (PubMed:38326... | Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) |
P10000 | COLI_ONCKE | MVCAPWLLAVVVVCVCNPGVGGQCWDSSHCKDLPSEDKILECTHLFRSGLQDESPEPRSAAQQSTEESLSLGILLAALTSGERALDADPEPHSDKRHSYSMEHFRWGKPIGHKRRPIKVYASSLEGGDSSEGTFPLQARRQLGSWEDEMVGALGNQGAKAQTKVVPRTLTVTGLQDKKDGSYRMGHFRWGSPTAIKRYGGFMKPYTKQSHKPLITLLKHITLKNEQ | null | null | neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852] | extracellular space [GO:0005615]; secretory granule [GO:0030141] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184] | PF00976;PF08384;PF08035; | null | POMC family | PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}. | null | null | null | null | null | FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin ... | Oncorhynchus keta (Chum salmon) (Salmo keta) |
P10026 | TRAM1_ECOLI | MAKVNLYISNDAYEKINAIIEKRRQEGAREKDVSFSATASMLLELGLRVHEAQMERKESAFNQTEFNKLLLECVVKTQSSVAKILGIESLSPHVSGNSKFEYANMVEDIREKVSSEMERFFPKNDDE | null | null | null | cytoplasm [GO:0005737] | DNA binding [GO:0003677] | PF05261; | 1.10.287.2320;1.10.10.450; | Relaxosome TraM family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1479887}. | null | null | null | null | null | FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut i... | Escherichia coli (strain K12) |
P10037 | PIT1_RAT | MSCQPFTSADTFIPLNSDASAALPLRMHHSAAEGLPASNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGTLTPCLYKFPDHTLSHGFPPLHQPLLAEDPTASEFKQELRRKSKLVEEPIDMDSPEIRELEQFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEHSKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR | null | null | adenohypophysis development [GO:0021984]; B cell differentiation [GO:0030183]; cell fate specification [GO:0001708]; cell population proliferation [GO:0008283]; determination of adult lifespan [GO:0008340]; inositol trisphosphate biosynthetic process [GO:0032959]; negative regulation of transcription by RNA polymerase ... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; lncRNA binding [GO:0106222]; RNA po... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28069}. | null | null | null | null | null | FUNCTION: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'. {ECO:0000250|UniProtKB:P28069}. | Rattus norvegicus (Rat) |
P10038 | MAB5_CAEEL | MSMYPGWTGDDSYWAGAGTTASSQSASSGTSASASSSAAAAAAANNLKTYELYNHTYMNNMKHMLAAGWMDNSSNPFAYNPLQATSANFGETRTSMPAISQPVFPWMKMGGAKGGESKRTRQTYSRSQTLELEKEFHYHKYLTRKRRQEISETLHLTERQVKIWFQNRRMKHKKEAKGEGGSNESDEESNQDEQNEQHSS | null | null | anterior/posterior pattern specification [GO:0009952]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail mating organ morphogenesis [GO:0090597]; neuroblast migration [GO:0097402]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of mesoderm... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the promoter region of the transcription factor lin-39 to repress its expression in Q neuroblasts and thereby direct left Q neuroblast (QL) daughter cell migration (PubMed:23784779, PubMed:8898225). During postembryonic development, required for posterior-specific pattern fo... | Caenorhabditis elegans |
P10039 | TENA_CHICK | MGLPSQVLACAILGLLYQHASGGLIKRIIRQKRETGLNVTLPEDNQPVVFNHVYNIKLPVGSLCSVDLDTASGDADLKAEIEPVKNYEEHTVNEGNQIVFTHRINIPRRACGCAAAPDIKDLLSRLEELEGLVSSLREQCASGAGCCPNSQTAEGRLDTAPYCSGHGNYSTEICGCVCEPGWKGPNCSEPACPRNCLNRGLCVRGKCICEEGFTGEDCSQAACPSDCNDQGKCVDGVCVCFEGYTGPDCGEELCPHGCGIHGRCVGGRCVCHEGFTGEDCNEPLCPNNCHNRGRCVDNECVCDEGYTGEDCGELICPNDC... | null | null | cell adhesion [GO:0007155]; neuron projection development [GO:0031175]; regulation of cell adhesion [GO:0030155] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; perisynaptic extracellular matrix [GO:0098966] | null | PF07974;PF18720;PF00147;PF00041; | 2.20.25.10;3.90.215.10;2.60.40.10;2.10.25.10; | Tenascin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. | Gallus gallus (Chicken) |
P10040 | CRB_DROME | MAKIANASLSQQQKQRQAETATTTTTTVAASVETATTTARSRDRTKSAAQITSHLLKRAISVYSSPQWIPLFILIYLATDVASVAVPTKEAYFNGSTYLRLTTPMPIWDHSAISFRSCRGGEILAQQYNKNSIVISVLNDFLQISLAGPAVHGPNNRLDVKLPYQLLDNRWHTLQFKYEYGNLYLHVDRAASIFANSTYNSQFLTNQDIGYKDAILILGNSFSGCLLDGPGLQFVNNSTVQNVVFGHCPLTPGPCSDHDLFTRLPDNFCLNDPCMGHGTCSSSPEGYECRCTARYSGKNCQKDNGSPCAKNPCENGGSCL... | null | null | adherens junction organization [GO:0034332]; amnioserosa maintenance [GO:0046665]; apical constriction [GO:0003383]; apical protein localization [GO:0045176]; assembly of apicomedial cortex actomyosin [GO:0106036]; cell division [GO:0051301]; cell morphogenesis involved in Malpighian tubule morphogenesis [GO:0061336]; ... | apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; photoreceptor connecting cilium [GO:0032391]; plasma membrane [GO:0005886]; rhabdomere [GO:0016028]; rhabdomere membrane [GO:0033583]; spindle [GO:0005819]; subapical complex [GO:0035003] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; protein kinase C binding [GO:0005080]; spectrin binding [GO:0030507] | PF00008;PF07645;PF12661;PF00054;PF02210; | 2.60.120.200;2.10.25.10; | Crumbs protein family | PTM: Phosphorylated in the cytoplasmic domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:30645584, ECO:0000269|PubMed:32579558}; Single-pass type I membrane protein {ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25065591}. C... | null | null | null | null | null | FUNCTION: Plays a central role in cell polarity establishment, and contributes to the organization of zonula adherens, epithelial morphogenesis, and tissue growth (PubMed:10102271, PubMed:11740560, PubMed:12900452, PubMed:2344615). Participates in the assembly, positioning and maintenance of adherens junctions via its ... | Drosophila melanogaster (Fruit fly) |
P10041 | DL_DROME | MHWIKCLLTAFICFTVIVQVHSSGSFELRLKYFSNDHGRDNEGRCCSGESDGATGKCLGSCKTRFRVCLKHYQATIDTTSQCTYGDVITPILGENSVNLTDAQRFQNKGFTNPIQFPFSFSWPGTFSLIVEAWHDTNNSGNARTNKLLIQRLLVQQVLEVSSEWKTNKSESQYTSLEYDFRVTCDLNYYGSGCAKFCRPRDDSFGHSTCSETGEIICLTGWQGDYCHIPKCAKGCEHGHCDKPNQCVCQLGWKGALCNECVLEPNCIHGTCNKPWTCICNEGWGGLYCNQDLNYCTNHRPCKNGGTCFNTGEGLYTCKCA... | null | null | actin filament organization [GO:0007015]; antennal morphogenesis [GO:0048800]; apposition of dorsal and ventral imaginal disc-derived wing surfaces [GO:0007475]; asymmetric cell division [GO:0008356]; border follicle cell migration [GO:0007298]; cell fate specification [GO:0001708]; chaeta morphogenesis [GO:0008407]; c... | apical cortex [GO:0045179]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; glycosphingolipid binding [GO:0043208]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018] | PF21700;PF01414;PF00008;PF12661;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | PTM: Ubiquitinated by Mib, leading to its endocytosis and subsequent degradation. {ECO:0000269|PubMed:15760269, ECO:0000269|PubMed:15829515}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Acts as a ligand for Notch (N) receptor. Essential for proper differentiation of ectoderm. Delta is required for the correct separation of neural and epidermal cell lineages. Fringe (fng) acts in the Golgi to determine the type of O-linked fucose on the EGF modules in N, altering the ability of N to bind with... | Drosophila melanogaster (Fruit fly) |
P10056 | PAPA3_CARPA | MAMIPSISKLLFVAICLFVHMSVSFGDFSIVGYSQDDLTSTERLIQLFNSWMLNHNKFYENVDEKLYRFEIFKDNLNYIDETNKKNNSYWLGLNEFADLSNDEFNEKYVGSLIDATIEQSYDEEFINEDTVNLPENVDWRKKGAVTPVRHQGSCGSCWAFSAVATVEGINKIRTGKLVELSEQELVDCERRSHGCKGGYPPYALEYVAKNGIHLRSKYPYKAKQGTCRAKQVGGPIVKTSGVGRVQPNNEGNLLNAIAKQPVSVVVESKGRPFQLYKGGIFEGPCGTKVDHAVTAVGYGKSGGKGYILIKNSWGTAWGEK... | 3.4.22.30 | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.; EC=3.4.22.30; Evidence={ECO:0000269|PubMed:2404797}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.2 mM for Boc-Ala-Ala-Gly-NHPhNO(2) {ECO:0000269|PubMed:2404797}; KM=0.17 mM for Boc-Ala-Ala-Gly-NHMec {ECO:0000269|PubMed:2404797}; Note=kcat is 0.5 sec(-1) with Boc-Ala-Ala-Gly-NHPhNO(2) as substrate (PubMed:2404797). kcat is 0.1 sec(-1) with Boc-Ala-Ala-Gly-NHM... | null | null | null | FUNCTION: Cysteine proteinase with a high level of diversity in substrate specificity. {ECO:0000269|PubMed:2404797}. | Carica papaya (Papaya) |
P10063 | GBRA2_BOVIN | MKTKLNSSNMQLLLFVFLAWDPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLPGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVC... | null | null | chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of postsynaptic membrane potential [GO:0060078]; signal transduction [GO:0007165]; synaptic transmission, GABAergic [GO:0051932... | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; dendrite membrane [GO:0032590]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transpor... | benzodiazepine receptor activity [GO:0008503]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; inhibitory extracellular ligand-gated monoatomic ion channel activity [GO:0005237] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRA2 sub-subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:P26048}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P26048}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P26048}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23576}. Cell projection, dendrite {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:2842688}; | null | null | null | null | FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:2842688). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and conta... | Bos taurus (Bovine) |
P10064 | GBRA3_BOVIN | MIITQMSQFYMAGLGLLFLINILPGTTGQVESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTT... | null | null | chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of postsynaptic membrane potential [GO:0060078]; signal transduction [GO:0007165]; synaptic transmission, GABAergic [GO:0051932... | chloride channel complex [GO:0034707]; dendrite membrane [GO:0032590]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | benzodiazepine receptor activity [GO:0008503]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; inhibitory extracellular ligand-gated monoatomic ion channel activity [GO:0005237] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRA3 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P14867}; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P14867}; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P14867}; | null | null | null | null | FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (By similarity). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contai... | Bos taurus (Bovine) |
P10069 | BRLA_EMENI | MRNQSSLSDRLTVEVDCSSLGSNECPSMTSSFSPLESPTPTPTSIYSQGSLESPGWHGAGSLPNNTYERTPGSASMRSAFRLAGMASTESLGLPYGSMEGQERMPMPDFLSGYDENIEQLWMPSEAPKSYDHVAQGLAYHQGMHQYPTMARNTNNNYRHQAAAYLPESTTNPCLSRSIFHQPERVPSSMSSSMSMNNMLPWMNLGDSIAPQTIAPSQVGPVTPPPSYTDFPTSLSAFKQHSPTTPIRSCSLGTGSGADTPLSRLSGGPCEYMDDFQPSPVYRDGFQRPHRVASRKMLRRQTSKQNLMLENLPQVIKQVQF... | null | null | autolysis [GO:0001896]; conidium formation [GO:0048315]; positive regulation of conidium formation [GO:0075307]; regulation of secondary metabolite biosynthetic process [GO:1900376]; regulation of sterigmatocystin biosynthetic process [GO:0010913]; regulation of transcription by RNA polymerase II [GO:0006357]; response... | nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:2196567, PubMed:2655931, PubMed:2823119, PubMed:5366214, PubMed:7704830, PubMed:8508769). They act individually and together to regulate their own expression and that of numerous other sporulation-specific g... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P10070 | GLI2_HUMAN | METSASATASEKQEAKSGILEAAGFPDPGKKASPLVVAAAAAAAVAAQGVPQHLLPPFHAPLPIDMRHQEGRYHYEPHSVHGVHGPPALSGSPVISDISLIRLSPHPAGPGESPFNAPHPYVNPHMEHYLRSVHSSPTLSMISAARGLSPADVAQEHLKERGLFGLPAPGTTPSDYYHQMTLVAGHPAPYGDLLMQSGGAASAPHLHDYLNPVDVSRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPS... | null | null | axon guidance [GO:0007411]; branching morphogenesis of an epithelial tube [GO:0048754]; cellular response to virus [GO:0098586]; cerebellar cortex morphogenesis [GO:0021696]; developmental growth [GO:0048589]; embryonic digestive tract development [GO:0048566]; epidermal cell differentiation [GO:0009913]; floor plate f... | ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytosol [GO:0005829]; GLI-SUFU complex [GO:1990788]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; se... | PF00096; | 3.30.160.60; | GLI C2H2-type zinc-finger protein family | PTM: Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2; this inhibits GLI2 transcription factor activity and promotes proteasomal degradation of GLI2. {ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:19878745}.; PTM: Acetylation at Lys-757 inhibits Hh target gene expression, probably by impeding entry into chrom... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26565916}. Cytoplasm {ECO:0000250|UniProtKB:Q0VGT2}. Cell projection, cilium {ECO:0000250|UniProtKB:Q0VGT2}. Note=STK36 promotes translocation to the nucleus. In keratinocytes, it is sequestered in the cytoplasm by SUFU. In the absence of SUFU, it translocates to the nu... | null | null | null | null | null | FUNCTION: Functions as a transcription regulator in the hedgehog (Hh) pathway (PubMed:18455992, PubMed:26565916). Functions as a transcriptional activator (PubMed:19878745, PubMed:24311597, PubMed:9557682). May also function as transcriptional repressor (By similarity). Requires STK36 for full transcriptional activator... | Homo sapiens (Human) |
P10071 | GLI3_HUMAN | MEAQSHSSTTTEKKKVENSIVKCSTRTDVSEKAVASSTTSNEDESPGQTYHRERRNAITMQPQNVQGLSKVSEEPSTSSDERASLIKKEIHGSLPHVAEPSVPYRGTVFAMDPRNGYMEPHYHPPHLFPAFHPPVPIDARHHEGRYHYDPSPIPPLHMTSALSSSPTYPDLPFIRISPHRNPTAASESPFSPPHPYINPYMDYIRSLHSSPSLSMISATRGLSPTDAPHAGVSPAEYYHQMALLTGQRSPYADIIPSAATAGTGAIHMEYLHAMDSTRFSSPRLSARPSRKRTLSISPLSDHSFDLQTMIRTSPNSLVTI... | null | null | alpha-beta T cell differentiation [GO:0046632]; anterior semicircular canal development [GO:0060873]; anterior/posterior pattern specification [GO:0009952]; artery development [GO:0060840]; axon guidance [GO:0007411]; branching involved in ureteric bud morphogenesis [GO:0001658]; camera-type eye morphogenesis [GO:00485... | axoneme [GO:0005930]; ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; GLI-SUFU complex [GO:1990788]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:00... | beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone acetyltransferase binding [GO:0035035]; histone deacetylase binding [GO:0042826]; mediator complex bindin... | PF00096; | 3.30.160.60; | GLI C2H2-type zinc-finger protein family | PTM: Phosphorylated on multiple sites by protein kinase A (PKA) and phosphorylation by PKA primes further phosphorylation by CK1 and GSK3. Phosphorylated by DYRK2 (in vitro). Phosphorylation is essential for its proteolytic processing.; PTM: Transcriptional repressor GLI3R, a C-terminally truncated form, is generated f... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, cilium. Note=GLI3FL is localized predominantly in the cytoplasm while GLI3R resides mainly in the nucleus. Ciliary accumulation requires the presence of KIF7 and SMO. Translocation to the nucleus is promoted by interaction with ZIC1. | null | null | null | null | null | FUNCTION: Has a dual function as a transcriptional activator and a repressor of the sonic hedgehog (Shh) pathway, and plays a role in limb development. The full-length GLI3 form (GLI3FL) after phosphorylation and nuclear translocation, acts as an activator (GLI3A) while GLI3R, its C-terminally truncated form, acts as a... | Homo sapiens (Human) |
P10073 | ZSC22_HUMAN | MAIPKHSLSPVPWEEDSFLQVKVEEEEEASLSQGGESSHDHIAHSEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLVEDLTQVLDKRGWDPGAEPTEASCKQSDLGESEPSNVTETLMGGVSLGPAFVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGRESGASRNSSSAWPNLTSQEKPPSEDKFDLVDAYGTEPPYTYSGKRSSKCRECRKMFQSASALEAHQKTHSRKTPYACSECGKAFSRSTHLAQHQVVHTG... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF02023;PF00096; | 3.30.160.60;1.10.4020.10; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P10074 | TZAP_HUMAN | MDGSFVQHSVRVLQELNKQREKGQYCDATLDVGGLVFKAHWSVLACCSHFFQSLYGDGSGGSVVLPAGFAEIFGLLLDFFYTGHLALTSGNRDQVLLAARELRVPEAVELCQSFKPKTSVGQAAGGQSGLGPPASQNVNSHVKEPAGLEEEEVSRTLGLVPRDQEPRGSHSPQRPQLHSPAQSEGPSSLCGKLKQALKPCPLEDKKPEDCKVPPRPLEAEGAQLQGGSNEWEVVVQVEDDGDGDYMSEPEAVLTRRKSNVIRKPCAAEPALSAGSLAAEPAENRKGTAVPVECPTCHKKFLSKYYLKVHNRKHTGEKPFE... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; telomere maintenance via telomere lengthening [GO:0010833] | chromosome, telomeric region [GO:0000781]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded telomeric DNA binding [GO:0003691]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specifi... | PF00651;PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}. Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). According to a report, preferentially binds to long telomeres that have a low concentrat... | null | null | null | null | null | FUNCTION: Telomere-binding protein that acts as a regulator of telomere length (PubMed:28082411, PubMed:28500257). Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regul... | Homo sapiens (Human) |
P10079 | FBP1_STRPU | MRTWLLAVLLLSVIAVTYGQGECDSDPCENGSTCQEGEGSYICQCPMGYDGQNCDRFTGSNCGYNVFDANGMIDSPNYPAMYNNRADCLYLVRITKARSITFTIEDFMTEVFKDVVEYGIGPEADFNQALGSFEGNLTQDDVIPAPFTVQGDQAWFIFSTDRNIVNRGFRITFSSDGDDCDPNLCQNGAACTDLVNDYACTCPPGFTGRNCEIDIDECASDPCQNGGACVDGVNGYVCNCVPGFDGDECENNINECASSPCLNGGICVDGVNMFECTCLAGFTGVRCEVNIDECASAPCQNGGICIDGINGYTCSCPLGF... | null | null | negative regulation of Notch signaling pathway [GO:0045746]; Notch signaling pathway [GO:0007219] | apical lamina of hyaline layer [GO:0032579]; cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | biotin binding [GO:0009374]; calcium ion binding [GO:0005509]; Notch binding [GO:0005112] | PF01382;PF00431;PF00008;PF12661; | 2.40.128.30;2.10.25.10;2.60.120.290; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasmic vesicle. Secreted, extracellular space, extracellular matrix, hyaline layer. Secreted, extracellular space, extracellular matrix, apical lamina. Note=In vesicles in the cytoplasm of unfertilized eggs, then to the base of the hyaline layer throughout devel... | null | null | null | null | null | FUNCTION: Forms the apical lamina, a component of the extracellular matrix. | Strongylocentrotus purpuratus (Purple sea urchin) |
P10080 | SSBP1_YEAST | MSAEIEEATNAVNNLSINDSEQQPRAPTHKTVIDPEDTIFIGNVAHECTEDDLKQLFVEEFGDEVSVEIPIKEHTDGHIPASKHALVKFPTKIDFDNIKENYDTKVVKDREIHIKRARTPGQMQRGGFRGRGGFRGRGGFRGGFRGGYRGGFRGRGNFRGRGGARGGFNGQKREKIPLDQMERSKDTLYINNVPFKATKEEVAEFFGTDADSISLPMRKMRDQHTGRIFTSDSANRGMAFVTFSGENVDIEAKAEEFKGKVFGDRELTVDVAVIRPENDEEEIEQETGSEEKQE | null | null | negative regulation of translation [GO:0017148]; negative regulation of translation in response to stress [GO:0032055] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleolus [GO:0005730]; nucleus [GO:0005634]; P-body [GO:0000932]; ribonucleoprotein complex [GO:1990904] | eukaryotic initiation factor 4G binding [GO:0031370]; mRNA binding [GO:0003729] | PF00076; | 3.30.70.330; | RRM GAR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:23222640}. Nucleus, nucleolus {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:2121740}. Cytoplasm, P-body {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23222640}. | null | null | null | null | null | FUNCTION: Functions in the transition of mRNAs from translation to an mRNP complex destined for decapping. High-copy-number suppressor of decapping defects. Overexpression suppresses decapping defects in both DCP1-2 and DCP2-7 mutations. Acts to promote translational repression of mRNA in conjunction with DHH1 and subs... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10081 | IF4A_YEAST | MSEGITDIEESQIQTNYDKVVYKFDDMELDENLLRGVFGYGFEEPSAIQQRAIMPIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQALMLAPTRELALQIQKVVMALAFHMDIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIKMFILDEADEMLSSGFKEQIYQIFTLLPPTTQVVLLSATMPNDVLEVTTKFMRNPVRILVKKDELTLEGIKQFYVNVEEEEYKYECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTIMKEFRSGSSRILISTDLL... | 3.6.4.13 | null | cytoplasmic translational initiation [GO:0002183]; positive regulation of formation of translation preinitiation complex [GO:1901195]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; eukaryotic translation initiation factor 4F complex [GO:0016281]; plasma membrane [GO:0005886]; ribosome [GO:0005840] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; translation initiation factor activity [GO:0003743] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, eIF4A subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=470 uM for ATP {ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180}; Vmax=2.6 pmol/sec/ug enzyme for ATP {ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180}; | null | FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10082 | PYY_HUMAN | MVFVRRPWPALTTVLLALLVCLGALVDAYPIKPEAPREDASPEELNRYYASLRHYLNLVTRQRYGKRDGPDTLLSKTFFPDGEDRPVRSRSEGPDLW | null | null | feeding behavior [GO:0007631]; intestinal epithelial cell differentiation [GO:0060575]; neuropeptide signaling pathway [GO:0007218] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; neuropeptide Y receptor binding [GO:0031841] | PF00159; | 6.10.250.900; | NPY family | PTM: The peptide YY form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro) to generate peptide YY(3-36). {ECO:0000269|PubMed:21314817}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. | Homo sapiens (Human) |
P10083 | AST5_DROME | MALGSENHSVFNDDEESSSAFNGPSVIRRNARERNRVKQVNNGFSQLRQHIPAAVIADLSNGRRGIGPGANKKLSKVSTLKMAVEYIRRLQKVLHENDQQKQKQLHLQQQHLHFQQQQQHQHLYAWHQELQLQSPTGSTSSCNSISSYCKPATSTIPGATPPNNFHTKLEASFEDYRNNSCSSGTEDEDILDYISLWQDDL | null | null | central nervous system development [GO:0007417]; chaeta morphogenesis [GO:0008407]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; Malpighian tubule tip cell differentiation [GO:0061382]; nervous system development [GO:0007399]; neuroblast fate determination [GO:0007400]; periph... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-s... | PF00010; | 4.10.280.10; | null | null | null | null | null | null | null | null | FUNCTION: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system. | Drosophila melanogaster (Fruit fly) |
P10084 | AST4_DROME | MKNNNNTTKSTTMSSSVLSTNETFPTTINSATKIFRYQHIMPAPSPLIPGGNQNQPAGTMPIKTRKYTPRGMALTRCSESVSSLSPGSSPAPYNVDQSQSVQRRNARERNRVKQVNNSFARLRQHIPQSIITDLTKGGGRGPHKKISKVDTLRIAVEYIRRLQDLVDDLNGGSNIGANNAVTQLQLCLDESSSHSSSSSTCSSSGHNTYYQNTISVSPLQQQQQLQRQQFNHQPLTALSLNTNLVGTSVPGGDAGCVSTSKNQQTCHSPTSSFNSSMSFDSGTYEGVPQQISTHLDRLDHLDNELHTHSQLQLKFEPYEH... | null | null | central nervous system development [GO:0007417]; chaeta development [GO:0022416]; chaeta morphogenesis [GO:0008407]; enteroendocrine cell differentiation [GO:0035883]; Malpighian tubule tip cell differentiation [GO:0061382]; negative regulation of apoptotic process [GO:0043066]; nervous system development [GO:0007399];... | RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; protein heterodimerization activity [G... | PF00010; | 4.10.280.10; | null | null | null | null | null | null | null | null | FUNCTION: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system. Also involved in sex determination and dosage compensation. {ECO:0000269|PubMed:2583094, ECO:0000269|PubMed:8370520}. | Drosophila melanogaster (Fruit fly) |
P10085 | MYOD1_MOUSE | MELLSPPLRDIDLTGPDGSLCSFETADDFYDDPCFDSPDLRFFEDLDPRLVHMGALLKPEEHAHFPTAVHPGPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAFYAPGPLPPGRGSEHYSGDSDASSPRSNCSDGMMDYSGPPSGPRRQNGYDTAYYSEAARESRPGKSAAVSSLDCLSSIVERISTDSPAAPALLLADAPPESPPGPPEGASLSDTEQGTQTPSPDAAPQCPAGSNPNAIYQVL | null | null | cardiac muscle cell differentiation [GO:0055007]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to oxygen levels [GO:0071453]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; muscl... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; myofibril [GO:0030016]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:00... | PF01586;PF00010;PF12232; | 4.10.280.10; | null | PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function. {ECO:0000269|PubMed:9029156}.; PTM: Ubiquitinated on the N-terminus; which is required for proteasomal degradation. {ECO:0000250}.; PTM: Phosphoryl... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16901893}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation (PubMed:16901893). Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblast... | Mus musculus (Mouse) |
P10088 | TFDA_CUPPJ | MSVVANPLHPLFAAGVEDIDLREALGSTEVREIERLMDEKSVLVFRGQPLSQDQQIAFARNFGPLEGGFIKVNQRPSRFKYAELADISNVSLDGKVAQRDAREVVGNFANQLWHSDSSFQQPAARYSMLSAVVVPPSGGDTEFCDMRAAYDALPRDLQSELEGLRAEHYALNSRFLLGDTDYSEAQRNAMPPVNWPLVRTHAGSGRKFLFIGAHASHVEGLPVAEGRMLLAELLEHATQREFVYRHRWNVGDLVMWDNRCVLHRGRRYDISARRELRRATTLDDAVV | 1.14.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.; | 2,4-dichlorophenoxyacetic acid catabolic process [GO:0046300]; heterocycle metabolic process [GO:0046483] | null | 2,4-dichlorophenoxyacetate alpha-ketoglutarate dioxygenase activity [GO:0018602]; L-ascorbic acid binding [GO:0031418]; metal ion binding [GO:0046872] | PF02668; | 3.60.130.10; | TfdA dioxygenase family | PTM: Hydroxylated on Trp-113; inactivates the enzyme. {ECO:0000269|PubMed:11457355}. | null | CATALYTIC ACTIVITY: Reaction=(2,4-dichlorophenoxy)acetate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + CO2 + glyoxylate + succinate; Xref=Rhea:RHEA:48984, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16738, ChEBI:CHEBI:16810, ChEBI:CHEBI:19351, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; | null | PATHWAY: Xenobiotic degradation; (2,4-dichlorophenoxy)acetate degradation. | null | null | FUNCTION: Involved in degradation of the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D). Is also able to degrade 2-methyl-4-chlorophenoxyacetic acid and 3-chlorobenzoic acid. | Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134)) |
P10090 | WHITE_DROME | MGQEDQELLIRGGSKHPSAEHLNNGDSGAASQSCINQGFGQAKNYGTLLPPSPPEDSGSGSGQLAENLTYAWHNMDIFGAVNQPGSGWRQLVNRTRGLFCNERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVA... | 7.6.2.-; 7.6.2.6 | null | aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; biogenic amine biosynthetic process [GO:0042401]; cGMP transport [GO:0070731]; compound eye pigmentation [GO:0048072]; eye pigment metabolic process [GO:0042441]; eye pigment precursor transport [GO:0006856]; gravitaxis [GO:0042332]; guanine transpo... | cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; pigment granule [GO:0048770]; pigment granule membrane [GO:0090741]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | ABC-type 3',5'-cyclic GMP transmembrane transporter activity [GO:1905948]; ABC-type guanine transporter activity [GO:0008558]; amine transmembrane transporter activity [GO:0005275]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; guanine tr... | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Eye pigment precursor importer (TC 3.A.1.204) subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11294610, ECO:0000269|PubMed:33820991}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with st/scarlet to pigment granules within pigment cells and retinula cells of the compound eye. {ECO:0000269|PubMed:11294610}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57746, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:18310115}; CATALYTIC ACTIVITY: Reaction=AT... | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters, metabolic intermediates and second messengers (PubMed:10407069, PubMed:117796, PubMed:18310115, PubMed:18931318, PubMed:33820991, PubMed:6788034, PubMed:812484). In the... | Drosophila melanogaster (Fruit fly) |
P10092 | CALCB_HUMAN | MGFRKFSPFLALSILVLYQAGSLQAAPFRSALESSPDPATLSKEDARLLLAALVQDYVQMKASELKQEQETQGSSSAAQKRACNTATCVTHRLAGLLSRSGGMVKSNFVPTNVGSKAFGRRRRDLQA | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; intracellular calcium ion homeostasis [GO:0006874]; regulation of cytosolic calcium ion concentration [GO:0051480]; signal transduction [GO:0007165] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcitonin receptor binding [GO:0031716]; neuropeptide hormone activity [GO:0005184] | PF00214; | 6.10.250.2190; | Calcitonin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. | Homo sapiens (Human) |
P10096 | G3P_BOVIN | MVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLHYMVYMFQYDSTHGKFNGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYNNTLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDEIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN... | 1.2.1.12; 2.6.99.- | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; innate immune response [GO:0045087]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of synaptic vesicle membrane [GO:0098850]; GAIT complex [GO:0097452]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634] | disordered domain specific binding [GO:0097718]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with ph... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with C... | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate... | Bos taurus (Bovine) |
P10102 | KPCA_RABIT | MADVFPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEDGNVELRQKFEKAKLGPAGNKVISP... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P05696}; | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; negative regulation of glial cell apoptotic process [GO:0034351]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell adhesion [GO:0045785]; po... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly... | Oryctolagus cuniculus (Rabbit) |
P10103 | HMGB1_BOVIN | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEEEEEDDDDE | null | null | adaptive immune response [GO:0002250]; apoptotic cell clearance [GO:0043277]; autophagy [GO:0006914]; B cell proliferation involved in immune response [GO:0002322]; chromatin remodeling [GO:0006338]; dendritic cell chemotaxis [GO:0002407]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [G... | chromatin [GO:0000785]; condensed chromosome [GO:0000793]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; chemoattractant activity [GO:0042056]; damaged DNA binding [GO:0003684]; DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; histone binding [GO:0042393]; non-sequence-specific DNA binding, bending [GO:0044378]; RAGE r... | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS. Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7409193}. Chromosome {ECO:0000269|PubMed:7409193}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; ... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Bos taurus (Bovine) |
P10105 | LAB_DROME | MMDVSSMYGNHPHHHHPHANAYDGYSTTTASAANASSYFAPQQHQPHLQLQQQQQHQHLQQPQQHLTYNGYESSSPGNYYPQQQAQLTPPPTSSHQVVQQHQQQQQAQQQQLYPHSHLFSPSAAEYGITTSTTTGNPGTPLHPSSHSPADSYYESDSVHSYYATAAVATVAPPSNSSPITAANASATSNTQQQQQQAAIISSENGMMYTNLDCMYPTAQAQAPVHGYAGQIEEKYAAVLHASYAPGMVLEDQDPMMQQATQSQMWHHQQHLAGSYALDAMDSLGMHAHMHHGLPHGHLGNLANNPHQQQPQVQQQQQQPH... | null | null | brain development [GO:0007420]; brain segmentation [GO:0035284]; cell differentiation [GO:0030154]; cell fate determination [GO:0001709]; head morphogenesis [GO:0060323]; midgut development [GO:0007494]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymeras... | nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, Labial subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for proper head development. | Drosophila melanogaster (Fruit fly) |
P10107 | ANXA1_MOUSE | MAMVSEFLKQARFLENQEQEYVQAVKSYKGGPGSAVSPYPSFNVSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQENGKPLDEVLRKALTGHLEEVVLAMLKTPAQFDADELRGAMKGLGTDEDTLIEILTTRSNEQIREINRVYREELKRDLAKDITSDTSGDFRKALLALAKGDRCQDLSVNQDLADTDARALYEAGERRKGTDVNVFTTILTSRSFPHLRRVFQNYGKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKALIRIMVSRSEIDMNEIKVFYQKKYG... | null | null | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen per... | actin filament [GO:0005884]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; extracellular... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; DNA/DNA annealing activity [GO:1990814]; double-stranded DNA helicase activity [GO:0036121]; identical protein binding [GO:... | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000269|PubMed:23727357}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000269|PubMed:18802107, ECO:0000269|PubMed:21245195}. Cell projection, cilium {ECO:0000269|PubMed:17384087}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000269|PubMed:18802107}. Cell membrane {ECO:000... | null | null | null | null | null | FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:12475898). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (PubMed:1247... | Mus musculus (Mouse) |
P10109 | ADX_HUMAN | MAAAGGARLLRAASAVLGGPAGRWLHHAGSRAGSSGLLRNRGPGGSAEASRSLSVSARARSSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFEDHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDVGKTS | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:21636783, ECO:0000269|Ref.16}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:21636783, ECO:0000269|Ref.16}; | cellular response to cAMP [GO:0071320]; cellular response to forskolin [GO:1904322]; cholesterol metabolic process [GO:0008203]; electron transport chain [GO:0022900]; hormone biosynthetic process [GO:0042446]; P450-containing electron transport chain [GO:0140647]; steroid biosynthetic process [GO:0006694] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; iron ion binding [GO:0005506] | PF00111; | 3.10.20.30; | Adrenodoxin/putidaredoxin family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:20547883}. | null | null | null | null | null | FUNCTION: Essential for the synthesis of various steroid hormones (PubMed:20547883, PubMed:21636783). Participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis (PubMed:20547883, PubMed:21636783). Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholest... | Homo sapiens (Human) |
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