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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P06732
|
KCRM_HUMAN
|
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDDLDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMTEKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLAHLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLMVEMEKKLEKGQSIDDMIPAQK
|
2.7.3.2
| null |
phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]
|
ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]
|
PF00217;PF02807;
|
1.10.135.10;3.30.590.10;
|
ATP:guanido phosphotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000250|UniProtKB:P00563, ECO:0000255|PROSITE-ProRule:PRU10029};
| null | null | null | null |
FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. {ECO:0000250|UniProtKB:P00563}.
|
Homo sapiens (Human)
|
P06733
|
ENOA_HUMAN
|
MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18560153}; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. {ECO:0000269|PubMed:18560153};
|
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of muscle contraction [GO:0045933]; positive regulation of plasminogen activation [GO:0010756]; response to virus [GO:0009615]
|
cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; M band [GO:0031430]; membrane [GO:0016020]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]
|
cadherin binding [GO:0045296]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; GTPase binding [GO:0051020]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
|
PTM: ISGylated. {ECO:0000269|PubMed:16139798, ECO:0000269|PubMed:16815975}.; PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. {ECO:0000269|PubMed:29775581}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10802057}. Cell membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.; SUBCELLULAR LOCATION: [Isoform MBP-1]: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:29775581};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:1369209}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0. {ECO:0000269|PubMed:1369209};
| null |
FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209). {ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133, ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901, ECO:0000269|PubMed:29775581}.; FUNCTION: [Isoform MBP-1]: Binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}.
|
Homo sapiens (Human)
|
P06734
|
FCER2_HUMAN
|
MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS
| null | null |
B cell antigen processing and presentation [GO:0002450]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; immune response [GO:0006955]; macrophage activation [GO:0042116]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of killing of cells of another organism [GO:0051712]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]
|
external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; IgE binding [GO:0019863]; integrin binding [GO:0005178]; low-affinity IgE receptor activity [GO:0019769]; metal ion binding [GO:0046872]
|
PF00059;
|
3.10.100.10;
| null |
PTM: N- and O-glycosylated.; PTM: The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted {ECO:0000269|PubMed:37453717}. Note=Also exists as a soluble excreted form, sCD23.
| null | null | null | null | null |
FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B cells. On B cells, initiates IgE-dependent antigen uptake and presentation to T cells (PubMed:2167225). On macrophages, upon IgE binding and antigen cross-linking induces intracellular killing of parasites through activation of L-Arginine-nitric oxide pathway (PubMed:7544003). {ECO:0000269|PubMed:2167225, ECO:0000269|PubMed:7544003}.
|
Homo sapiens (Human)
|
P06736
|
HLYC_ECOLX
|
MNINKPLEILGHVSWLWASSPLHRNWPVSLFAINVLPAIQANQYVLLTRDDYPVAYCSWANLSLENEIKYLNDVTSLVAEDWTSGDRKWFIDWIAPFGDNGALYKYMRKKFPDELFRAIRVDPKTHVGKVSEFHGGKIDKQLANKIFKQYHHELITEVKRKSDFNFSLTG
|
2.3.1.-
| null |
killing of cells of another organism [GO:0031640]; toxin metabolic process [GO:0009404]
|
cytoplasm [GO:0005737]
|
ACP-dependent peptidyl-lysine N6-myristoyltransferase activity [GO:0140769]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; peptidyl-lysine N6-myristoyltransferase activity [GO:0018030]
|
PF02794;
| null |
RTX toxin acyltransferase family
|
PTM: Proteolytically cleaved by the protease systems ClpAP, ClpXP and FtsH, leading to its degradation. {ECO:0000269|PubMed:11278516}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-tetradecanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:70611, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477, ChEBI:CHEBI:141129; Evidence={ECO:0000269|PubMed:11695909, ECO:0000269|PubMed:32461253}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70612; Evidence={ECO:0000269|PubMed:11695909, ECO:0000269|PubMed:32461253};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:11695909}; KM=3.6 uM for HlyA peptide {ECO:0000269|PubMed:11695909}; Vmax=4667 pmol/min/mg enzyme {ECO:0000269|PubMed:11695909};
| null | null | null |
FUNCTION: Protein-lysine myristoyltransferase that catalyzes myristoylation of the protoxin (HlyA) at two internal lysine residues, thereby converting it to the active toxin. {ECO:0000269|PubMed:10079090, ECO:0000269|PubMed:10413532, ECO:0000269|PubMed:11278516, ECO:0000269|PubMed:11695909, ECO:0000269|PubMed:15065878, ECO:0000269|PubMed:29908817, ECO:0000269|PubMed:32461253, ECO:0000269|PubMed:9521785}.
|
Escherichia coli
|
P06737
|
PYGL_HUMAN
|
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNESNKVNGN
|
2.4.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:12204691, ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV, ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0, ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S, ECO:0007744|PDB:1L7X};
|
5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; glucose homeostasis [GO:0042593]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; necroptotic process [GO:0070266]; response to bacterium [GO:0009617]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; secretory granule lumen [GO:0034774]
|
AMP binding [GO:0016208]; ATP binding [GO:0005524]; bile acid binding [GO:0032052]; glucose binding [GO:0005536]; glycogen phosphorylase activity [GO:0008184]; identical protein binding [GO:0042802]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; purine nucleobase binding [GO:0002060]; pyridoxal phosphate binding [GO:0030170]; SHG alpha-glucan phosphorylase activity [GO:0102499]; vitamin binding [GO:0019842]
|
PF00343;
|
3.40.50.2000;
|
Glycogen phosphorylase family
|
PTM: Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation. {ECO:0000269|PubMed:22225877}.; PTM: Phosphorylation at Ser-15 converts inactive phosphorylase b into active phosphorylase a (PubMed:10949035). Dephosphorylation of Ser-15 by phosphatase PP1 inactivates the enzyme (PubMed:22225877). {ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:22225877}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22225877}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence={ECO:0000269|PubMed:22225877}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733; Evidence={ECO:0000305|PubMed:22225877};
| null | null | null | null |
FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000269|PubMed:22225877}.
|
Homo sapiens (Human)
|
P06738
|
PHSG_YEAST
|
MPPASTSTTNDMITEEPTSPHQIPRLTRRLTGFLPQEIKSIDTMIPLKSRALWNKHQVKKFNKAEDFQDRFIDHVETTLARSLYNCDDMAAYEAASMSIRDNLVIDWNKTQQKFTTRDPKRVYYLSLEFLMGRALDNALINMKIEDPEDPAASKGKPREMIKGALDDLGFKLEDVLDQEPDAGLGNGGLGRLAACFVDSMATEGIPAWGYGLRYEYGIFAQKIIDGYQVETPDYWLNSGNPWEIERNEVQIPVTFYGYVDRPEGGKTTLSASQWIGGERVLAVAYDFPVPGFKTSNVNNLRLWQARPTTEFDFAKFNNGDYKNSVAQQQRAESITAVLYPNDNFAQGKELRLKQQYFWCAASLHDILRRFKKSKRPWTEFPDQVAIQLNDTHPTLAIVELQRVLVDLEKLDWHEAWDIVTKTFAYTNHTVMQEALEKWPVGLFGHLLPRHLEIIYDINWFFLQDVAKKFPKDVDLLSRISIIEENSPERQIRMAFLAIVGSHKVNGVAELHSELIKTTIFKDFVKFYGPSKFVNVTNGITPRRWLKQANPSLAKLISETLNDPTEEYLLDMAKLTQLGKYVEDKEFLKKWNQVKLNNKIRLVDLIKKENDGVDIINREYLDDTLFDMQVKRIHEYKRQQLNVFGIIYRYLAMKNMLKNGASIEEVAKKYPRKVSIFGGKSAPGYYMAKLIIKLINCVADIVNNDESIEHLLKVVFVADYNVSKAEIIIPASDLSEHISTAGTEASGTSNMKFVMNGGLIIGTVDGANVEITREIGEDNVFLFGNLSENVEELRYNHQYHPQDLPSSLDSVLSYIESGQFSPENPNEFKPLVDSIKYHGDYYLVSDDFESYLATHELVDQEFHNQRSEWLKKSVLSVANVGFFSSDRCIEEYSDTIWNVEPVT
|
2.4.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
glycogen catabolic process [GO:0005980]
|
cytoplasm [GO:0005737]
|
glycogen phosphorylase activity [GO:0008184]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; pyridoxal phosphate binding [GO:0030170]; SHG alpha-glucan phosphorylase activity [GO:0102499]
|
PF00343;
|
3.40.50.2000;
|
Glycogen phosphorylase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24146988}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
| null | null | null | null |
FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06744
|
G6PI_HUMAN
|
MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ
|
5.3.1.9
| null |
carbohydrate metabolic process [GO:0005975]; erythrocyte homeostasis [GO:0034101]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096]; hemostasis [GO:0007599]; humoral immune response [GO:0006959]; in utero embryonic development [GO:0001701]; learning or memory [GO:0007611]; mesoderm formation [GO:0001707]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of immunoglobulin production [GO:0002639]; response to cadmium ion [GO:0046686]; response to estradiol [GO:0032355]; response to immobilization stress [GO:0035902]; response to muscle stretch [GO:0035994]; response to progesterone [GO:0032570]; response to testosterone [GO:0033574]
|
ciliary membrane [GO:0060170]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; secretory granule lumen [GO:0034774]
|
carbohydrate derivative binding [GO:0097367]; cytokine activity [GO:0005125]; glucose-6-phosphate isomerase activity [GO:0004347]; growth factor activity [GO:0008083]; monosaccharide binding [GO:0048029]; ubiquitin protein ligase binding [GO:0031625]
|
PF00342;
|
1.10.1390.10;
|
GPI family
|
PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11437381}. Secreted {ECO:0000269|PubMed:11437381}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000269|PubMed:28803808};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269|PubMed:28803808}.
| null | null |
FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:11004567, PubMed:3352745). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:11004567, PubMed:3352745). {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381, ECO:0000269|PubMed:28803808, ECO:0000269|PubMed:3352745}.
|
Homo sapiens (Human)
|
P06745
|
G6PI_MOUSE
|
MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNFSLNLNTNHGHILVDYSKNLVNKEVMQMLVELAKSRGVEAARDNMFSGSKINYTENRAVLHVALRNRSNTPIKVDGKDVMPEVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLSPETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVAKHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLLALLGIWYINCYGCETHALLPYDQYMHRFAAYFQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKLPEEARKELQAAGKSPEDLEKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQLAKKIEPELEGSSAVTSHDSSTNGLISFIKQQRDTKLE
|
5.3.1.9
| null |
canonical glycolysis [GO:0061621]; erythrocyte homeostasis [GO:0034101]; fructose 6-phosphate metabolic process [GO:0006002]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096]; glycolytic process through glucose-6-phosphate [GO:0061620]; in utero embryonic development [GO:0001701]; learning or memory [GO:0007611]; mesoderm formation [GO:0001707]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of immunoglobulin production [GO:0002639]; response to cadmium ion [GO:0046686]; response to estradiol [GO:0032355]; response to immobilization stress [GO:0035902]; response to muscle stretch [GO:0035994]; response to progesterone [GO:0032570]; response to testosterone [GO:0033574]
|
ciliary membrane [GO:0060170]; cytosol [GO:0005829]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]
|
carbohydrate derivative binding [GO:0097367]; cytokine activity [GO:0005125]; glucose-6-phosphate isomerase activity [GO:0004347]; growth factor activity [GO:0008083]; monosaccharide binding [GO:0048029]; ubiquitin protein ligase binding [GO:0031625]
|
PF00342;
|
1.10.1390.10;
|
GPI family
|
PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}. Secreted {ECO:0000250|UniProtKB:P06744}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:8417789};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:7277315, ECO:0000269|PubMed:8417789}.
| null | null |
FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:2344351, PubMed:7277315, PubMed:8417789). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (By similarity). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:3764429). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745). {ECO:0000250|UniProtKB:P06744, ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:3352745, ECO:0000269|PubMed:3764429, ECO:0000269|PubMed:7277315, ECO:0000269|PubMed:8417789}.
|
Mus musculus (Mouse)
|
P06746
|
DPOLB_HUMAN
|
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
2.7.7.7; 4.2.99.-; 4.2.99.18
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9287163}; Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:9287163};
|
base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; double-strand break repair via nonhomologous end joining [GO:0006303]; homeostasis of number of cells [GO:0048872]; immunoglobulin heavy chain V-D-J recombination [GO:0071707]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lymph node development [GO:0048535]; neuron apoptotic process [GO:0051402]; pyrimidine dimer repair [GO:0006290]; response to ethanol [GO:0045471]; response to gamma radiation [GO:0010332]; response to hyperoxia [GO:0055093]; salivary gland morphogenesis [GO:0007435]; somatic hypermutation of immunoglobulin genes [GO:0016446]; spleen development [GO:0048536]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876]
|
5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]
|
PF14792;PF14791;PF10391;PF14716;
|
1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10;
|
DNA polymerase type-X family
|
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000269|PubMed:16600869}.; PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation. {ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; CATALYTIC ACTIVITY: Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195; Evidence={ECO:0000269|PubMed:9572863, ECO:0000269|PubMed:9614142}; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000269|PubMed:9614142};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 uM for DNA with an intact AP site {ECO:0000269|PubMed:9614142}; KM=0.5 uM for DNA with a preincised AP site {ECO:0000269|PubMed:9614142}; Note=kcat is 0.075 sec(-1) for 5'-deoxyribose-phosphate lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142). kcat is 0.004 sec(-1) for AP lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142). {ECO:0000269|PubMed:9614142};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 for 5'-deoxyribose-phosphate lyase activity. {ECO:0000269|PubMed:9614142};
| null |
FUNCTION: Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142). {ECO:0000269|PubMed:10556592, ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:17526740, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9556598, ECO:0000269|PubMed:9572863, ECO:0000269|PubMed:9614142}.
|
Homo sapiens (Human)
|
P06747
|
PHOSP_RABVP
|
MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMGRLHLDDGKSPNPGEMAKVGEGKYREDFQMDEGEDPSLLFQSYLDNVGVQIVRQIRSGERFLKIWSQTVEEIISYVAVNFPNPPGKSSEDKSTQTTGRELKKETTPTPSQRESQSSKARMAAQTASGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGILLYNFEQLKMNLDDIVKEAKNVPGVTRLARDGSKLPLRCVLGWVALANSKKFQLLVESNKLSKIMQDDLNRYTSC
| null | null |
microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral transcription [GO:0019083]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423]
|
RNA-dependent RNA polymerase activity [GO:0003968]
|
PF03012;
|
6.10.140.1560;1.20.120.820;
|
Lyssavirus protein P family
|
PTM: Phosphorylated by host PKC and by an unknown kinase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). Inhibits interferon induction pathways by interacting with host TBK1 and preventing the formation of dynamic cytoplasmic condensates that have liquid properties and that are essential for interferon production (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P16286}.
|
Rabies virus (strain Pasteur vaccins / PV) (RABV)
|
P06748
|
NPM_HUMAN
|
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
| null | null |
cellular response to UV [GO:0034644]; cellular senescence [GO:0090398]; centrosome cycle [GO:0007098]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; intracellular protein transport [GO:0006886]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of centrosome duplication [GO:0010826]; negative regulation of protein kinase activity by regulation of protein phosphorylation [GO:0044387]; nucleocytoplasmic transport [GO:0006913]; nucleosome assembly [GO:0006334]; positive regulation of cell cycle G2/M phase transition [GO:1902751]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation [GO:0045727]; protein localization [GO:0008104]; regulation of centriole replication [GO:0046599]; regulation of centrosome duplication [GO:0010824]; regulation of eIF2 alpha phosphorylation by dsRNA [GO:0060735]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of endoribonuclease activity [GO:0060699]; regulation of mRNA stability involved in cellular response to UV [GO:1902629]; ribosomal large subunit biogenesis [GO:0042273]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal small subunit export from nucleus [GO:0000056]; ribosomal subunit export from nucleus [GO:0000054]; ribosome assembly [GO:0042255]; signal transduction [GO:0007165]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; granular component [GO:0001652]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; ribonucleoprotein complex [GO:1990904]; spindle pole centrosome [GO:0031616]
|
chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; NF-kappaB binding [GO:0051059]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]; protein self-association [GO:0043621]; ribosomal large subunit binding [GO:0043023]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; Tat protein binding [GO:0030957]; transcription coactivator activity [GO:0003713]; unfolded protein binding [GO:0051082]
|
PF16276;PF03066;
|
1.10.10.2100;2.60.120.340;
|
Nucleoplasmin family
|
PTM: Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. {ECO:0000269|PubMed:16107701, ECO:0000269|Ref.17}.; PTM: ADP-ribosylated.; PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-199, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-199 phosphorylated form has higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to viral reactivation by reducing viral LANA levels. {ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:12058066, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:15190079, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:20333249, ECO:0000269|PubMed:20352051, ECO:0000269|Ref.17}.; PTM: Sumoylated by ARF. {ECO:0000269|PubMed:15897463}.; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36 (PubMed:19208757). {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:25818168}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Can shuttle between cytoplasm and nucleus. Co- localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis.
| null | null | null | null | null |
FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25956029}.
|
Homo sapiens (Human)
|
P06750
|
AGGL_RICCO
|
MYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTADATVESYTNFIRAVRSHLTTGADVRHEIPVLPNRVGLPISQRFILVELSNHAELSVTLALDVTNAYVVGCRAGNSAYFFHPDNQEDAEAITHLFTDVQNSFTFAFGGNYDRLEQLGGLRENIELGTGPLEDAISALYYYSTCGTQIPTLARSFMVCIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFNVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMDPEPIVRIVGRNGLCVDVTGEEFFDGNPIQLWPCKSNTDWNQLWTLRKDSTIRSNGKCLTISKSSPRQQVVIYNCSTATVGATRWQIWDNRTIINPRSGLVLAATSGNSGTKLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGMCLQANSGKVWLEDCTSEKAEQQWALYADGSIRPQQNRDNCLTTDANIKGTVVKILSCGPASSGQRWMFKNDGTILNLYNGLVLDVRRSDPSLKQIIVHPFHGNLNQIWLPLF
|
3.2.2.22
| null |
defense response [GO:0006952]; negative regulation of translation [GO:0017148]
|
endoplasmic reticulum [GO:0005783]
|
carbohydrate binding [GO:0030246]; nucleotide binding [GO:0000166]; rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729]
|
PF00652;PF00161;
|
2.80.10.50;3.40.420.10;4.10.470.10;
|
Ribosome-inactivating protein family, Type 2 RIP subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22;
| null | null | null | null | null |
Ricinus communis (Castor bean)
|
P06752
|
ENV_FLVSA
|
MESPTHPKPSKDKTFPWNLVFLVGILFQIDMGMANPSPHQVYNVTWVITNVQTNSRANATSMLGTLTDAYPTLYVDLCDLVGDTWEPIAPDPRSWARYSSSTHGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTYCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSNQDNSCKGKCNPLVLQFTQKGRQASWDRPKMWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQTKSKVTTQRPQITSSTPRSVASATMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSTPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYIYTHFDKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQIAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLLGPCILNRLVQFVKDRISVVQALILTQQYQQIQQYDSDRP
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00429;
|
1.10.287.210;3.90.310.10;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity). {ECO:0000250}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity). {ECO:0000250}.; PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.; PTM: The R-peptide is palmitoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is membrane-associated through its palmitate. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.
|
Feline leukemia virus (strain C/Sarma)
|
P06753
|
TPM3_HUMAN
|
MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
| null | null |
actin filament organization [GO:0007015]; muscle contraction [GO:0006936]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle thin filament tropomyosin [GO:0005862]; stress fiber [GO:0001725]
|
actin filament binding [GO:0051015]
|
PF00261;
|
1.20.5.170;1.20.5.340;
|
Tropomyosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}.
|
Homo sapiens (Human)
|
P06754
|
TPM1_DROME
|
MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNKKKTTKMTTSIPQGTLLDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELILKE
| null | null |
actin filament organization [GO:0007015]; dendrite morphogenesis [GO:0048813]; mitotic cytokinesis [GO:0000281]; muscle contraction [GO:0006936]; oogenesis [GO:0048477]; pole plasm assembly [GO:0007315]; pole plasm oskar mRNA localization [GO:0045451]; regulation of lamellipodium assembly [GO:0010591]; response to hyperoxia [GO:0055093]
|
actin filament [GO:0005884]; actomyosin contractile ring [GO:0005826]; cytosol [GO:0005829]; investment cone [GO:0070865]; sarcomere [GO:0030017]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; protein kinase binding [GO:0019901]
|
PF00261;
|
1.20.5.170;1.20.5.340;
|
Tropomyosin family
| null |
SUBCELLULAR LOCATION: [Isoform 9A]: Cytoplasm, cytoskeleton.
| null | null | null | null | null |
FUNCTION: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Drosophila melanogaster (Fruit fly)
|
P06756
|
ITAV_HUMAN
|
MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET
| null | null |
angiogenesis [GO:0001525]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; calcium ion transmembrane transport [GO:0070588]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; endodermal cell differentiation [GO:0035987]; entry into host cell by a symbiont-containing vacuole [GO:0085017]; ERK1 and ERK2 cascade [GO:0070371]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; negative chemotaxis [GO:0050919]; negative regulation of entry of bacterium into host cell [GO:2000536]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of lipid storage [GO:0010888]; negative regulation of lipid transport [GO:0032369]; negative regulation of lipoprotein metabolic process [GO:0050748]; negative regulation of low-density lipoprotein receptor activity [GO:1905598]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; regulation of phagocytosis [GO:0050764]; regulation of transforming growth factor beta activation [GO:1901388]; substrate adhesion-dependent cell spreading [GO:0034446]; symbiont entry into host cell [GO:0046718]; transforming growth factor beta production [GO:0071604]; vasculogenesis [GO:0001570]; wound healing, spreading of epidermal cells [GO:0035313]
|
alphav-beta3 integrin-HMGB1 complex [GO:0035868]; alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; alphav-beta3 integrin-PKCalpha complex [GO:0035866]; cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; integrin alphav-beta1 complex [GO:0034682]; integrin alphav-beta3 complex [GO:0034683]; integrin alphav-beta5 complex [GO:0034684]; integrin alphav-beta6 complex [GO:0034685]; integrin alphav-beta8 complex [GO:0034686]; integrin complex [GO:0008305]; lamellipodium membrane [GO:0031258]; membrane [GO:0016020]; microvillus membrane [GO:0031528]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; specific granule membrane [GO:0035579]
|
coreceptor activity [GO:0015026]; extracellular matrix binding [GO:0050840]; extracellular matrix protein binding [GO:1990430]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; opsonin binding [GO:0001846]; protease binding [GO:0002020]; protein kinase C binding [GO:0005080]; transforming growth factor beta binding [GO:0050431]; virus receptor activity [GO:0001618]; voltage-gated calcium channel activity [GO:0005245]
|
PF01839;PF08441;PF20805;PF20806;PF00357;
|
1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;
|
Integrin alpha chain family
| null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}.
| null | null | null | null | null |
FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 acts as a receptor for CD40LG (PubMed:31331973). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428). {ECO:0000269|PubMed:10640428, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464, ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for Adenovirus type C. {ECO:0000269|PubMed:20615244}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for Coxsackievirus A9 and B1. {ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:7519807, ECO:0000269|PubMed:9426447}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor for herpes simplex 1/HHV-1. {ECO:0000269|PubMed:24367260}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Human parechovirus 1. {ECO:0000269|PubMed:11160695}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus. {ECO:0000269|PubMed:23658209}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000269|PubMed:10397733}.
|
Homo sapiens (Human)
|
P06757
|
ADH1_RAT
|
MSTAGKVIKCKAAVLWEPHKPFTIEDIEVAPPKAHEVRIKMVATGVCRSDDHAVSGSLFTPLPAVLGHEGAGIVESIGEGVTCVKPGDKVIPLFSPQCGKCRICKHPESNLCCQTKNLTQPKGALLDGTSRFSCRGKPIHHFISTSTFSQYTVVDDIAVAKIDAAAPLDKVCLIGCGFSTGYGSAVQVAKVTPGSTCAVFGLGGVGLSVVIGCKTAGAAKIIAVDINKDKFAKAKELGATDCINPQDYTKPIQEVLQEMTDGGVDFSFEVIGRLDTMTSALLSCHSACGVSVIVGVPPSAQSLSVNPMSLLLGRTWKGAIFGGFKSKDAVPKLVADFMAKKFPLEPLITHVLPFEKINEAFDLLRAGKSIRTVLTF
|
1.1.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
|
acetaldehyde biosynthetic process [GO:0046186]; animal organ regeneration [GO:0031100]; behavioral response to ethanol [GO:0048149]; ethanol catabolic process [GO:0006068]; ethanol oxidation [GO:0006069]; response to progesterone [GO:0032570]; response to retinoic acid [GO:0032526]; response to steroid hormone [GO:0048545]; response to testosterone [GO:0033574]; retinoic acid metabolic process [GO:0042573]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; ethanol binding [GO:0035276]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD-retinol dehydrogenase activity [GO:0004745]; organic cyclic compound binding [GO:0097159]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family, Class-I subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
| null | null | null | null | null |
Rattus norvegicus (Rat)
|
P06759
|
APOC3_RAT
|
MQPRMLLIVALVALLASARADEGEGSLLLGSMQGYMEQASKTVQDALSSMQESDIAVVASRGWMDNRFKSLKGYWSKFTDKFTGLWESGPEDQLTTPTLEP
| null | null |
cellular response to glucose stimulus [GO:0071333]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; G protein-coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle remodeling [GO:0034375]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; negative regulation of cholesterol import [GO:0060621]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of high-density lipoprotein particle clearance [GO:0010987]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of oxidative phosphorylation [GO:0090324]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of triglyceride catabolic process [GO:0010897]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phospholipid efflux [GO:0033700]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of Cdc42 protein signal transduction [GO:0032489]; response to fatty acid [GO:0070542]; response to nutrient [GO:0007584]; response to peptide hormone [GO:0043434]; response to triglyceride [GO:0034014]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; triglyceride catabolic process [GO:0019433]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; triglyceride mobilization [GO:0006642]
|
chylomicron [GO:0042627]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
enzyme regulator activity [GO:0030234]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; lipid transporter activity [GO:0005319]; phospholipid binding [GO:0005543]
|
PF05778;
|
6.10.90.10;
|
Apolipoprotein C3 family
|
PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-96 with a core 1 or possibly core 8 glycan. {ECO:0000250|UniProtKB:P02656}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}.
| null | null | null | null | null |
FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. {ECO:0000250|UniProtKB:P02656}.
|
Rattus norvegicus (Rat)
|
P06760
|
BGLR_RAT
|
MSPRRSVCWFVLGQLLCSCAVALQGGMLFPKETPSRELKVLDGLWSFRADYSNNRLQGFEKQWYRQPLRESGPTLDMPVPSSFNDITQEAELRNFIGWVWYEREAVLPQRWTQDTDRRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADITKLVQSGPLTTFRVTIAINNTLTPYTLPPGTIVYKTDPSMYPKGYFVQDISFDFFNYAGLHRSVVLYTTPTTYIDDITVTTDVDRDVGLVNYWISVQGSDHFQLEVRLLDEDGKIVARGTGNEGQLKVPRAHLWWPYLMHEHPAYLYSLEVTMTTPESVSDFYTLPVGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGRGFDWPLLIKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNVSLRHHLEVMDELVRRDKNHPAVVMWSVANEPVSSLKPAGYYFKTLIAHTKALDPTRPVTFVSNTRYDADMGAPYVDVICVNSYLSWYHDYGHLEVIQLQLTSQFENWYKMYQKPIIQSEYGADAVSGLHEDPPRMFSEEYQTALLENYHLILDEKRKEYVIGELIWNFADFMTNQSPLRVTGNKKGIFTRQRNPKMAAFILRERYWRIANETRGYGSVPRTQCMGSRPFTF
|
3.2.1.31
| null |
carbohydrate metabolic process [GO:0005975]; chondroitin sulfate catabolic process [GO:0030207]; glucuronoside catabolic process [GO:0019391]; heparan sulfate proteoglycan catabolic process [GO:0030200]; hyaluronan catabolic process [GO:0030214]
|
extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]
|
beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; hydrolase activity [GO:0016787]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102]
|
PF00703;PF02836;PF02837;
|
2.60.120.260;3.20.20.80;2.60.40.10;
|
Glycosyl hydrolase 2 family
|
PTM: Undergoes a post-transcriptional proteolytic cleavage near its C-terminal end, which reduces its size by approximately 3 kDa. The site of this cleavage has as yet not been determined.
|
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000305|PubMed:3355537}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634; Evidence={ECO:0000305|PubMed:3355537};
| null | null | null | null |
FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates.
|
Rattus norvegicus (Rat)
|
P06761
|
BIP_RAT
|
MKFTVVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSPEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL
|
3.6.4.10
| null |
cellular response to antibiotic [GO:0071236]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to gamma radiation [GO:0071480]; cellular response to glucose starvation [GO:0042149]; cellular response to interleukin-4 [GO:0071353]; cellular response to manganese ion [GO:0071287]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to xenobiotic stimulus [GO:0071466]; cerebellar Purkinje cell layer development [GO:0021680]; cerebellum structural organization [GO:0021589]; chaperone cofactor-dependent protein refolding [GO:0051085]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; ERAD pathway [GO:0036503]; IRE1-mediated unfolded protein response [GO:0036498]; luteolysis [GO:0001554]; maintenance of protein localization in endoplasmic reticulum [GO:0035437]; negative regulation of apoptotic process [GO:0043066]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; positive regulation of cell migration [GO:0030335]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein ubiquitination [GO:0031398]; post-translational protein targeting to membrane, translocation [GO:0031204]; protein refolding [GO:0042026]; proteolysis involved in protein catabolic process [GO:0051603]; response to cocaine [GO:0042220]; response to endoplasmic reticulum stress [GO:0034976]; response to methamphetamine hydrochloride [GO:1904313]; stress response to metal ion [GO:0097501]
|
cell surface [GO:0009986]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; smooth endoplasmic reticulum [GO:0005790]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; misfolded protein binding [GO:0051787]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183]; ribosome binding [GO:0043022]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]
|
PF00012;
|
1.20.1270.10;3.30.420.40;
|
Heat shock protein 70 family
|
PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity. {ECO:0000250|UniProtKB:G3I8R9}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). {ECO:0000250|UniProtKB:P11021}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:G3I8R9};
| null | null | null | null |
FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity). {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021, ECO:0000250|UniProtKB:P20029}.
|
Rattus norvegicus (Rat)
|
P06762
|
HMOX1_RAT
|
MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSAETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM
|
1.14.14.18
| null |
angiogenesis [GO:0001525]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to cisplatin [GO:0072719]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to nutrient [GO:0031670]; epithelial cell apoptotic process [GO:1904019]; erythrocyte homeostasis [GO:0034101]; heme catabolic process [GO:0042167]; heme metabolic process [GO:0042168]; heme oxidation [GO:0006788]; intracellular iron ion homeostasis [GO:0006879]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; liver regeneration [GO:0097421]; macroautophagy [GO:0016236]; multicellular organismal-level iron ion homeostasis [GO:0060586]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of macroautophagy [GO:0016242]; negative regulation of mast cell cytokine production [GO:0032764]; negative regulation of mast cell degranulation [GO:0043305]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; phospholipid metabolic process [GO:0006644]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of epithelial cell apoptotic process [GO:1904037]; positive regulation of macroautophagy [GO:0016239]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of blood pressure [GO:0008217]; regulation of transcription by RNA polymerase II [GO:0006357]; response to 3-methylcholanthrene [GO:1904681]; response to arachidonic acid [GO:1904550]; response to estrogen [GO:0043627]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to nicotine [GO:0035094]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; small GTPase-mediated signal transduction [GO:0007264]; wound healing involved in inflammatory response [GO:0002246]
|
caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
arachidonic acid omega-hydroxylase activity [GO:0052869]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phospholipase D activity [GO:0004630]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:0005198]
|
PF01126;
|
1.20.910.10;
|
Heme oxygenase family
|
PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000305|PubMed:1935972}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:3865203}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
|
CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:1935972, ECO:0000269|PubMed:3865203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; Evidence={ECO:0000305|PubMed:1935972};
| null | null | null | null |
FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:1575508, PubMed:1935972, PubMed:3865203). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (By similarity). {ECO:0000250|UniProtKB:P09601, ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:1935972, ECO:0000269|PubMed:3865203}.; FUNCTION: [Heme oxygenase 1 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:1935972}.
|
Rattus norvegicus (Rat)
|
P06765
|
PLF4_RAT
|
MSAAAVFRGLRPSPELLLLGLLLLPAVVAVTRASPEESDGDLSCVCVKTSSSRIHLKRITSLEVIKAGPHCAVPQLIATLKNGSKICLDRQVPLYKKIIKKLLES
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; cytokine-mediated signaling pathway [GO:0019221]; defense response to protozoan [GO:0042832]; immune response [GO:0006955]; inflammatory response [GO:0006954]; leukocyte chemotaxis [GO:0030595]; negative regulation of angiogenesis [GO:0016525]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of inflammatory response [GO:0050728]; negative regulation of megakaryocyte differentiation [GO:0045653]; negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; neutrophil chemotaxis [GO:0030593]; osteoclast differentiation [GO:0030316]; platelet activation [GO:0030168]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; protein-containing complex assembly [GO:0065003]; regulation of cell population proliferation [GO:0042127]; response to aldosterone [GO:1904044]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; platelet alpha granule [GO:0031091]; protein-containing complex [GO:0032991]; vesicle [GO:0031982]
|
chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
|
PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:8033893}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Chemokine released during platelet aggregation that plays a role in different biological processes including hematopoiesis, cell proliferation, differentiation, and activation. Acts via different functional receptors including CCR1, CXCR3A or CXCR3B. Upon interaction with CXCR3A receptor, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling. Neutralizes the anticoagulant effect of heparin by binding more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Plays a role in the inhibition of hematopoiesis and in the maintenance of hematopoietic stem cell (HSC) quiescence. Chemotactic for neutrophils and monocytes via CCR1. Inhibits endothelial cell proliferation. In cooperation with toll-like receptor 8/TLR8, induces chromatin remodeling and activates inflammatory gene expression via the TBK1-IRF5 axis. In addition, induces myofibroblast differentiation and collagen synthesis in different precursor cells, including endothelial cells, by stimulating endothelial-to-mesenchymal transition. {ECO:0000250|UniProtKB:P02776}.
|
Rattus norvegicus (Rat)
|
P06766
|
DPOLB_RAT
|
MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
|
2.7.7.7; 4.2.99.-; 4.2.99.18
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06746}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:P06746};
|
apoptotic process [GO:0006915]; base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; DNA damage response [GO:0006974]; DNA replication [GO:0006260]; double-strand break repair via nonhomologous end joining [GO:0006303]; homeostasis of number of cells [GO:0048872]; immunoglobulin heavy chain V-D-J recombination [GO:0071707]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lymph node development [GO:0048535]; neuron apoptotic process [GO:0051402]; pyrimidine dimer repair [GO:0006290]; response to ethanol [GO:0045471]; response to gamma radiation [GO:0010332]; response to hyperoxia [GO:0055093]; salivary gland morphogenesis [GO:0007435]; somatic diversification of immunoglobulins [GO:0016445]; somatic hypermutation of immunoglobulin genes [GO:0016446]; spleen development [GO:0048536]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876]
|
5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]
|
PF14792;PF14791;PF10391;PF14716;
|
1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10;
|
DNA polymerase type-X family
|
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000250}.; PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P06746}; CATALYTIC ACTIVITY: Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195; Evidence={ECO:0000250|UniProtKB:P06746}; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000250|UniProtKB:P06746};
| null | null | null | null |
FUNCTION: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase. {ECO:0000250|UniProtKB:P06746}.
|
Rattus norvegicus (Rat)
|
P06767
|
TKN1_RAT
|
MKILVAVAVFFLVSTQLFAEEIGANDDLNYWSDWSDSDQIKEAMPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQISHKRHKTDSFVGLMGKRALNSVAYERSAMQNYERRRK
| null | null |
associative learning [GO:0008306]; cellular response to nerve growth factor stimulus [GO:1990090]; chemical synaptic transmission [GO:0007268]; inflammatory response [GO:0006954]; long-term memory [GO:0007616]; negative regulation of heart rate [GO:0010459]; neuropeptide signaling pathway [GO:0007218]; positive regulation of action potential [GO:0045760]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of corticosterone secretion [GO:2000854]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of lymphocyte proliferation [GO:0050671]; positive regulation of ossification [GO:0045778]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of synaptic transmission, cholinergic [GO:0032224]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; regulation of blood pressure [GO:0008217]; response to hormone [GO:0009725]; response to lipopolysaccharide [GO:0032496]; response to pain [GO:0048265]; sensory perception of pain [GO:0019233]; tachykinin receptor signaling pathway [GO:0007217]
|
axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; synapse [GO:0045202]
|
substance K receptor binding [GO:0031837]; substance P receptor binding [GO:0031835]
|
PF02202;
| null |
Tachykinin family
|
PTM: [Substance P]: The substance P form is cleaved at Pro-59 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Substance P is also cleaved and degraded by Angiotensin-converting enzyme (ACE) and neprilysin (MME). {ECO:0000250|UniProtKB:P20366}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
|
Rattus norvegicus (Rat)
|
P06774
|
HAP2_YEAST
|
MSADETDAKFHPLETDLQSDTAAATSTAAASRSPSLQEKPIEMPLDMGKAPSPRGEDQRVTNEEDLFLFNRLRASQNRVMDSLEPQQQSQYTSSSVSTMEPSADFTSFSAVTTLPPPPHQQQQQQQQQQQQQQLVVQAQYTQNQPNLQSDVLGTAIAEQPFYVNAKQYYRILKRRYARAKLEEKLRISRERKPYLHESRHKHAMRRPRGEGGRFLTAAEIKAMKSKKSGASDDPDDSHEDKKITTKIIQEQPHATSTAAAADKKT
| null | null |
carbon catabolite activation of transcription from RNA polymerase II promoter [GO:0000436]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of cellular respiration [GO:0043457]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
CCAAT-binding factor complex [GO:0016602]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]
|
PF02045;
|
6.10.250.2430;
|
NFYA/HAP2 subunit family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP complexes I and II. {ECO:0000269|PubMed:15075264}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06777
|
RAD1_YEAST
|
MSQLFYQGDSDDELQEELTRQTTQASQSSKIKNEDEPDDSNHLNEVENEDSKVLDDDAVLYPLIPNEPDDIETSKPNINDIRPVDIQLTLPLPFQQKVVENSLITEDALIIMGKGLGLLDIVANLLHVLATPTSINGQLKRALVLVLNAKPIDNVRIKEALEELSWFSNTGKDDDDTAVESDDELFERPFNVVTADSLSIEKRRKLYISGGILSITSRILIVDLLSGIVHPNRVTGMLVLNADSLRHNSNESFILEIYRSKNTWGFIKAFSEAPETFVMEFSPLRTKMKELRLKNVLLWPRFRVEVSSCLNATNKTSHNKVIEVKVSLTNSMSQIQFGLMECLKKCIAELSRKNPELALDWWNMENVLDINFIRSIDSVMVPNWHRISYESKQLVKDIRFLRHLLKMLVTSDAVDFFGEIQLSLDANKPSVSRKYSESPWLLVDEAQLVISYAKKRIFYKNEYTLEENPKWEQLIHILHDISHERMTNHLQGPTLVACSDNLTCLELAKVLNASNKKRGVRQVLLNKLKWYRKQREETKKLVKEVQSQDTFPENATLNVSSTFSKEQVTTKRRRTRGASQVAAVEKLRNAGTNVDMEVVFEDHKLSEEIKKGSGDDLDDGQEENAANDSKIFEIQEQENEILIDDGDAEFDNGELEYVGDLPQHITTHFNKDLWAEHCNEYEYVDRQDEILISTFKSLNDNCSLQEMMPSYIIMFEPDISFIRQIEVYKAIVKDLQPKVYFMYYGESIEEQSHLTAIKREKDAFTKLIRENANLSHHFETNEDLSHYKNLAERKLKLSKLRKSNTRNAGGQQGFHNLTQDVVIVDTREFNASLPGLLYRYGIRVIPCMLTVGDYVITPDICLERKSISDLIGSLQNNRLANQCKKMLKYYAYPTLLIEFDEGQSFSLEPFSERRNYKNKDISTVHPISSKLSQDEIQLKLAKLVLRFPTLKIIWSSSPLQTVNIILELKLGREQPDPSNAVILGTNKVRSDFNSTAKGLKDGDNESKFKRLLNVPGVSKIDYFNLRKKIKSFNKLQKLSWNEINELINDEDLTDRIYYFLRTEKEEQEQESTDENLESPGKTTDDNALHDHHNDVPEAPV
| null | null |
DNA amplification [GO:0006277]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing, removal of nonhomologous ends [GO:0000736]; meiotic mismatch repair [GO:0000710]; mitotic recombination [GO:0006312]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair involved in interstrand cross-link repair [GO:1901255]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; removal of nonhomologous ends [GO:0000735]; resolution of meiotic recombination intermediates [GO:0000712]
|
endonuclease complex [GO:1905348]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634]
|
damaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]
|
PF02732;
|
3.40.50.10130;1.10.150.20;
|
XPF family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD10 forms an endonuclease that specifically degrades single-stranded DNA. {ECO:0000269|PubMed:8479526}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06778
|
RAD52_YEAST
|
MNEIMDMDEKKPVFGNHSEDIQTKLDKKLGPEYISKRVGFGTSRIAYIEGWRVINLANQIFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINMGNTNSNVLTTEKDPVVAKQSPTASSNPEAEQITFVTAKAATSVQNERYIGEESIFDPKYQAQSIRHTVDQTTSKHIPASVLKDKTMTTARDSVYEKFAPKGKQLSMKNNDKELGPHMLEGAGNQVPRETTPIKTNATAFPPAAAPRFAPPSKVVHPNGNGAVPAVPQQRSTRREVGRPKINPLHARKPT
| null | null |
DNA amplification [GO:0006277]; DNA recombinase assembly [GO:0000730]; double-strand break repair via break-induced replication [GO:0000727]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing [GO:0045002]; meiotic joint molecule formation [GO:0000709]; mitochondrial DNA repair [GO:0043504]; mitotic recombination [GO:0006312]; postreplication repair [GO:0006301]; telomere maintenance via recombination [GO:0000722]
|
mitochondrion [GO:0005739]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]
|
DNA strand exchange activity [GO:0000150]; DNA/DNA annealing activity [GO:1990814]
|
PF04098;
|
3.30.390.80;
|
RAD52 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06779
|
RAD7_YEAST
|
MYRSRNRPKRGGENEVKGPNSALTQFLREEGISAENIKQKWYQRQSKKQEDATDEKKGKAEDDSFTAEISRVVEDEEIDEIGTGSGTETERAQVSYDARMKLVPADSDEEEYETSHISDTPVSLSSANDRESLTKKRQNTAKIIQNRRRKRKRAADLLDRRVNKVSSLQSLCITKISENISKWQKEADESSKLVFNKLRDVLGGVSTANLNNLAKALSKNRALNDHTLQLFLKTDLKRLTFSDCSKISFDGYKTLAIFSPHLTELSLQMCGQLNHESLLYIAEKLPNLKSLNLDGPFLINEDTWEKFFVIMKGRLEEFHISNTHRFTDKSLSNLLINCGSTLVSLGLSRLDSISNYALLPQYLVNDEFHSLCIEYPFNEEDVNDEIIINLLGQIGRTLRKLVLNGCIDLTDSMIINGLTAFIPEKCPLEVLSLEESDQITTDSLSYFFSKVELNNLIECSFRRCLQLGDMAIIELLLNGARDSLRSLNLNSLKELTKEAFVALACPNLTYLDLGFVRCVDDSVIQMLGEQNPNLTVIDVFGDNLVTEKATMRPGLTLIGRQSDSI
| null | null |
global genome nucleotide-excision repair [GO:0070911]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; protein localization [GO:0008104]; response to UV [GO:0009411]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; nucleotide-excision repair factor 4 complex [GO:0000113]; SCF ubiquitin ligase complex [GO:0019005]
| null | null |
3.80.10.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. {ECO:0000269|PubMed:10601031, ECO:0000269|PubMed:15177043}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06780
|
RHO1_YEAST
|
MSQQVGNSIRRKLVIVGDGACGKTCLLIVFSKGQFPEVYVPTVFENYVADVEVDGRRVELALWDTAGQEDYDRLRPLSYPDSNVVLICFSIDLPDSLENVQEKWIAEVLHFCQGVPIILVGCKVDLRNDPQTIEQLRQEGQQPVTSQEGQSVADQIGATGYYECSAKTGYGVREVFEAATRASLMGKSKTNGKAKKNTTEKKKKKCVLL
|
3.6.5.2
| null |
(1->3)-beta-D-glucan biosynthetic process [GO:0006075]; actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; ascospore wall assembly [GO:0030476]; budding cell bud growth [GO:0007117]; cellular bud neck septin ring organization [GO:0032186]; fungal-type cell wall biogenesis [GO:0009272]; positive regulation of endocytosis [GO:0045807]; positive regulation of mitotic actomyosin contractile ring assembly [GO:1903501]; positive regulation of protein kinase C signaling [GO:0090037]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell size [GO:0008361]; regulation of cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0090334]; regulation of exocyst localization [GO:0060178]; regulation of fungal-type cell wall organization [GO:0060237]; regulation of protein localization [GO:0032880]; regulation of secondary cell septum biogenesis [GO:1903395]; regulation of vacuole fusion, non-autophagic [GO:0032889]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264]
|
1,3-beta-D-glucan synthase complex [GO:0000148]; cell periphery [GO:0071944]; cellular bud [GO:0005933]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; fungal-type cell wall [GO:0009277]; fungal-type vacuole membrane [GO:0000329]; Golgi apparatus [GO:0005794]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; spore wall [GO:0031160]
|
G-protein beta-subunit binding [GO:0031681]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null |
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Peroxisome membrane; Lipid-anchor. Note=Plasma membrane-associated at sites of polarized growth such as incipient bud sites, bud tips, the bud neck during cytokinesis, and the neck and tip of mating projections. Also found on internal membranes of endosomes and peroxisomes.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P61586};
| null | null | null | null |
FUNCTION: Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7. {ECO:0000269|PubMed:11283608, ECO:0000269|PubMed:11447600, ECO:0000269|PubMed:12207708, ECO:0000269|PubMed:12419188, ECO:0000269|PubMed:12810699, ECO:0000269|PubMed:12928491, ECO:0000269|PubMed:15514049, ECO:0000269|PubMed:15596542, ECO:0000269|PubMed:7579704, ECO:0000269|PubMed:8195291, ECO:0000269|PubMed:8602514, ECO:0000269|PubMed:8602515, ECO:0000269|PubMed:8621575, ECO:0000269|PubMed:8846785, ECO:0000269|PubMed:8947028}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06781
|
RHO2_YEAST
|
MSEKAVRRKLVIIGDGACGKTSLLYVFTLGKFPEQYHPTVFENYVTDCRVDGIKVSLTLWDTAGQEEYERLRPFSYSKADIILIGFAVDNFESLINARTKWADEALRYCPDAPIVLVGLKKDLRQEAHFKENATDEMVPIEDAKQVARAIGAKKYMECSALTGEGVDDVFEVATRTSLLMKKEPGANCCIIL
|
3.6.5.2
| null |
actin filament organization [GO:0007015]; establishment of cell polarity [GO:0030010]; fungal-type cell wall organization [GO:0031505]; microtubule-based process [GO:0007017]; regulation of actin cytoskeleton organization [GO:0032956]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264]
|
cell periphery [GO:0071944]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P61586};
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06782
|
SNF1_YEAST
|
MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLKPHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANKSVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRANMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNEKIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN
|
2.7.11.1
| null |
establishment of mitotic spindle orientation [GO:0000132]; filamentous growth [GO:0030447]; fungal-type cell wall assembly [GO:0071940]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of translation [GO:0017148]; phosphorylation [GO:0016310]; positive regulation of filamentous growth of a population of unicellular organisms in response to starvation [GO:1900436]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of macroautophagy [GO:0016239]; positive regulation of pseudohyphal growth [GO:2000222]; regulation of cellular response to glucose starvation [GO:1904547]; regulation of invasive growth in response to glucose limitation [GO:2000217]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]; single-species surface biofilm formation [GO:0090606]
|
cellular bud neck septin ring [GO:0000144]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear envelope lumen [GO:0005641]; nuclear membrane [GO:0031965]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]; vacuolar membrane [GO:0005774]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; molecular function activator activity [GO:0140677]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF16579;PF00069;PF08587;
|
1.10.8.10;3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086). {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086}.; PTM: Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by interaction of SUMO attached to Lys-549 with a SUMO-interacting sequence motif located near the active site of SNF1, and by targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) ubiquitin ligase (PubMed:24108357). {ECO:0000269|PubMed:24108357}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269|PubMed:25869125}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554};
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase essential for release from glucose repression (PubMed:1944227, PubMed:25869125, PubMed:3049551, PubMed:3526554, PubMed:6366512, PubMed:8289797, PubMed:8628258). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:26667037, PubMed:8289797). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831). {ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989, ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125, ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512, ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06784
|
STE7_YEAST
|
MFQRKTLQRRNLKGLNLNLHPDVGNNGQLQEKTETHQGQSRIEGHVMSNINAIQNNSNLFLRRGIKKKLTLDAFGDDQAISKPNTVVIQQPQNEPVLVLSSLSQSPCVSSSSSLSTPCIIDAYSNNFGLSPSSTNSTPSTIQGLSNIATPVENEHSISLPPLEESLSPAAADLKDTLSGTSNGNYIQLQDLVQLGKIGAGNSGTVVKALHVPDSKIVAKKTIPVEQNNSTIINQLVRELSIVKNVKPHENIITFYGAYYNQHINNEIIILMEYSDCGSLDKILSVYKRFVQRGTVSSKKTWFNELTISKIAYGVLNGLDHLYRQYKIIHRDIKPSNVLINSKGQIKLCDFGVSKKLINSIADTFVGTSTYMSPERIQGNVYSIKGDVWSLGLMIIELVTGEFPLGGHNDTPDGILDLLQRIVNEPSPRLPKDRIYSKEMTDFVNRCCIKNERERSSIHELLHHDLIMKYVSPSKDDKFRHWCRKIKSKIKEDKRIKREALDRAKLEKKQSERSTH
|
2.7.12.2
| null |
cell wall integrity MAPK cascade [GO:0000196]; invasive growth in response to glucose limitation [GO:0001403]; MAPK cascade [GO:0000165]; pheromone response MAPK cascade [GO:0071507]; phosphorylation [GO:0016310]; pseudohyphal growth [GO:0007124]; signal transduction involved in filamentous growth [GO:0001402]
|
cytoplasm [GO:0005737]; mating projection tip [GO:0043332]
|
ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
| null | null |
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=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; 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=2.7.12.2;
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06785
|
TYSY_YEAST
|
MTMDGKNKEEEQYLDLCKRIIDEGEFRPDRTGTGTLSLFAPPQLRFSLRDDTFPLLTTKKVFTRGIILELLWFLAGDTDANLLSEQGVKIWDGNGSREYLDKMGFKDRKVGDLGPVYGFQWRHFGAKYKTCDDDYTGQGIDQLKQVIHKLKTNPYDRRIIMSAWNPADFDKMALPPCHIFSQFYVSFPKEGEGSGKPRLSCLLYQRSCDMGLGVPFNIASYALLTRMIAKVVDMEPGEFIHTLGDAHVYKDHIDALKEQITRNPRPFPKLKIKRDVKDIDDFKLTDFEIEDYNPHPRIQMKMSV
|
2.1.1.45
| null |
dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; methylation [GO:0032259]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear periphery [GO:0034399]
|
dihydrofolate reductase activity [GO:0004146]; thymidylate synthase activity [GO:0004799]
|
PF00303;
|
3.30.572.10;
|
Thymidylate synthase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8132557}. Note=Localizes to the nuclear periphery.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000269|PubMed:7028756};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for dUMP {ECO:0000269|PubMed:7028756}; KM=70 uM for 5,10-methylene-tetrahydropteroylglutamate {ECO:0000269|PubMed:7028756};
|
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7.2. {ECO:0000269|PubMed:7028756};
| null |
FUNCTION: Thymidylate synthase required for de novo biosynthesis of pyrimidine deoxyribonucleotides. Required for both nuclear and mitochondrial DNA synthesis. {ECO:0000269|PubMed:17248617, ECO:0000269|PubMed:334734, ECO:0000269|PubMed:4580573, ECO:0000269|PubMed:6287238, ECO:0000269|PubMed:7028756}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06786
|
TOP2_YEAST
|
MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED
|
5.6.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342};
|
chromatin organization [GO:0006325]; chromatin remodeling at centromere [GO:0031055]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA topological change [GO:0006265]; reciprocal meiotic recombination [GO:0007131]; regulation of mitotic recombination [GO:0000019]; replication fork progression beyond termination site [GO:0097046]; resolution of meiotic recombination intermediates [GO:0000712]; rRNA transcription [GO:0009303]; sister chromatid segregation [GO:0000819]
|
DNA replication termination region [GO:0097047]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF00204;PF00521;PF02518;PF01751;PF16898;
|
3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10;
|
Type II topoisomerase family
|
PTM: Phosphorylation enhances the activity. Stimulates decatenation activity. {ECO:0000269|PubMed:1316274}.
|
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374};
| null | null | null | null |
FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. {ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06787
|
CALM_YEAST
|
MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAEVDDMLREVSDGSGEINIQQFAALLSK
| null | null |
cell budding [GO:0007114]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; microautophagy [GO:0016237]; phosphatidylinositol biosynthetic process [GO:0006661]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; protein import into nucleus [GO:0006606]; receptor-mediated endocytosis [GO:0006898]; regulation of membrane tubulation [GO:1903525]; regulation of microtubule nucleation [GO:0010968]; spindle pole body organization [GO:0051300]; vacuole fusion, non-autophagic [GO:0042144]; vesicle transport along actin filament [GO:0030050]
|
actin cortical patch [GO:0030479]; cellular bud [GO:0005933]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; central plaque of spindle pole body [GO:0005823]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; myosin I complex [GO:0045160]; myosin II complex [GO:0016460]; myosin V complex [GO:0031475]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; enzyme regulator activity [GO:0030234]; mitogen-activated protein kinase binding [GO:0051019]
|
PF13499;
|
1.10.238.10;
|
Calmodulin family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8247006}.
| null | null | null | null | null |
FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. {ECO:0000269|PubMed:10339566}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06789
|
VE1_HPV18
|
MADPEGTDGEGTGCNGWFYVQAIVDKKTGDVISDDEDENATDTGSDMVDFIDTQGTFCEQAELETAQALFHAQEVHNDAQVLHVLKRKFAGGSTENSPLGERLEVDTELSPRLQEISLNSGQKKAKRRLFTISDSGYGCSEVEATQIQVTTNGEHGGNVCSGGSTEAIDNGGTEGNNSSVDGTSDNSNIENVNPQCTIAQLKDLLKVNNKQGAMLAVFKDTYGLSFTDLVRNFKSDKTTCTDWVTAIFGVNPTIAEGFKTLIQPFILYAHIQCLDCKWGVLILALLRYKCGKSRLTVAKGLSTLLHVPETCMLIQPPKLRSSVAALYWYRTGISNISEVMGDTPEWIQRLTIIQHGIDDSNFDLSEMVQWAFDNELTDESDMAFEYALLADSNSNAAAFLKSNCQAKYLKDCATMCKHYRRAQKRQMNMSQWIRFRCSKIDEGGDWRPIVQFLRYQQIEFITFLGALKSFLKGTPKKNCLVFCGPANTGKSYFGMSFIHFIQGAVISFVNSTSHFWLEPLTDTKVAMLDDATTTCWTYFDTYMRNALDGNPISIDRKHKPLIQLKCPPILLTTNIHPAKDNRWPYLESRITVFEFPNAFPFDKNGNPVYEINDKNWKCFFERTWSRLDLHEEEEDADTEGNPFGTFKLRAGQNHRPL
|
3.6.4.12
| null |
DNA replication [GO:0006260]; viral genome replication [GO:0019079]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]
|
PF00519;PF20450;PF00524;
|
3.40.1310.10;3.40.50.300;1.10.10.510;
|
Papillomaviridae E1 protein family
|
PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.; PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04000};
| null | null | null | null |
FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. {ECO:0000255|HAMAP-Rule:MF_04000}.
|
Human papillomavirus type 18
|
P06795
|
MDR1B_MOUSE
|
MEFEENLKGRADKNFSKMGKKSKKEKKEKKPAVGVFGMFRYADWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAGAKRS
|
7.6.2.1; 7.6.2.2
| null |
ceramide translocation [GO:0099040]; establishment of endothelial blood-brain barrier [GO:0014045]; phospholipid translocation [GO:0045332]; response to xenobiotic stimulus [GO:0009410]; Sertoli cell barrier remodeling [GO:0061843]
|
apical plasma membrane [GO:0016324]; external side of apical plasma membrane [GO:0098591]; Golgi membrane [GO:0000139]; intercellular canaliculus [GO:0046581]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; floppase activity [GO:0140328]; phosphatidylcholine floppase activity [GO:0090554]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily
|
PTM: Several phosphorylated serine residues are present in the linker domain.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08183}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000250|UniProtKB:P08183}. Cytoplasm {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane versus cytoplasm). {ECO:0000250|UniProtKB:P08183}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:36439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38943, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P08183};
| null | null | null | null |
FUNCTION: Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. {ECO:0000250|UniProtKB:P08183}.
|
Mus musculus (Mouse)
|
P06797
|
CATL1_MOUSE
|
MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQLHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKNSWGSEWGMEGYIKIAKDRDNHCGLATAASYPVVN
|
3.4.22.15
| null |
antigen processing and presentation of peptide antigen [GO:0048002]; autophagic cell death [GO:0048102]; CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; cell communication [GO:0007154]; cellular response to starvation [GO:0009267]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; elastin catabolic process [GO:0060309]; enkephalin processing [GO:0034230]; hair follicle morphogenesis [GO:0031069]; immune response [GO:0006955]; keratinocyte proliferation [GO:0043616]; male gonad development [GO:0008584]; negative regulation of keratinocyte proliferation [GO:0010839]; nerve development [GO:0021675]; positive regulation of apoptotic signaling pathway [GO:2001235]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to gonadotropin [GO:0034698]; response to organic cyclic compound [GO:0014070]; Sertoli cell differentiation [GO:0060008]; spermatogenesis [GO:0007283]; thyroid hormone generation [GO:0006590]; zymogen activation [GO:0031638]
|
apical plasma membrane [GO:0016324]; chromaffin granule [GO:0042583]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; microvillus [GO:0005902]; neuron projection [GO:0043005]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perikaryon [GO:0043204]; vacuole [GO:0005773]
|
aminopeptidase activity [GO:0004177]; cysteine-type carboxypeptidase activity [GO:0016807]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activity [GO:0004175]; histone binding [GO:0042393]; kininogen binding [GO:0030984]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
|
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (PubMed:11483509). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (By similarity). {ECO:0000250|UniProtKB:P07711, ECO:0000269|PubMed:11483509}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11483509, ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:12782676}. Secreted, extracellular space {ECO:0000269|PubMed:12417635}. Secreted {ECO:0000269|PubMed:10716919}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages (PubMed:12417635). {ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:12782676}.
|
CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000269|PubMed:8554545};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:10716919};
| null |
FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (PubMed:12869695). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells (PubMed:12021314). Also mediates invariant chain processing in cortical thymic epithelial cells (PubMed:9545226). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (PubMed:12417635). Secreted form generates endostatin from COL18A1 (PubMed:10716919). Critical for cardiac morphology and function (PubMed:11972068). Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (PubMed:12163394). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity). {ECO:0000250|UniProtKB:P07154, ECO:0000269|PubMed:10716919, ECO:0000269|PubMed:11972068, ECO:0000269|PubMed:12021314, ECO:0000269|PubMed:12163394, ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:12782676, ECO:0000269|PubMed:12869695, ECO:0000269|PubMed:9545226, ECO:0000305}.
|
Mus musculus (Mouse)
|
P06800
|
PTPRC_MOUSE
|
MTMGLWLKLLAFGFALLDTEVFVTGQTPTPSDELSTTENALLLPQSDPLPARTTESTPPSISERGNGSSETTYHPGVLSTLLPHLSPQPDSQTPSAGGADTQTFSSQADNPTLTPAPGGGTDPPGVPGERTVPGTIPADTAFPVDTPSLARNSSAASPTHTSNVSTTDISSGASLTTLTPSTLGLASTDPPSTTIATTTKQTCAAMFGNITVNYTYESSNQTFKADLKDVQNAKCGNEDCENVLNNLEECSQIKNISVSNDSCAPATTIDLYVPPGTDKFSLHDCTPKEKANTSICLEWKTKNLDFRKCNSDNISYVLHCEPENNTKCIRRNTFIPERCQLDNLRAQTNYTCVAEILYRGVKLVKNVINVQTDLGIPETPKPSCGDPAARKTLVSWPEPVSKPESASKPHGYVLCYKNNSEKCKSLPNNVTSFEVESLKPYKYYEVSLLAYVNGKIQRNGTAEKCNFHTKADRPDKVNGMKTSRPTDNSINVTCGPPYETNGPKTFYILVVRSGGSFVTKYNKTNCQFYVDNLYYSTDYEFLVSFHNGVYEGDSVIRNESTNFNAKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSNLDEQQELVERDDEKQLMDVEPIHSDILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHSCLHNMKKRDPPSDPSPLEAEYQRLPSYRSWRTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEMSKESEPESDESSDDDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIYPAQNGQVKKTNSQDKIEFHNEVDGGKQDANCVRPDGPLNKAQEDSRGVGTPEPTNSAEEPEHAANGSASPAPTQSS
|
3.1.3.48
| null |
alpha-beta T cell proliferation [GO:0046633]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; bone marrow development [GO:0048539]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle phase transition [GO:0044770]; cellular response to extracellular stimulus [GO:0031668]; defense response to virus [GO:0051607]; dephosphorylation [GO:0016311]; extrinsic apoptotic signaling pathway [GO:0097191]; gamma-delta T cell differentiation [GO:0042492]; hematopoietic progenitor cell differentiation [GO:0002244]; heterotypic cell-cell adhesion [GO:0034113]; leukocyte cell-cell adhesion [GO:0007159]; MAPK cascade [GO:0000165]; natural killer cell differentiation [GO:0001779]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein tyrosine kinase activity [GO:0061099]; negative regulation of T cell mediated cytotoxicity [GO:0001915]; negative thymic T cell selection [GO:0045060]; plasma membrane raft distribution [GO:0044855]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of antigen receptor-mediated signaling pathway [GO:0050857]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060369]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of hematopoietic stem cell migration [GO:2000473]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein tyrosine phosphatase activity [GO:1903615]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of T cell mediated immunity [GO:0002711]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of tumor necrosis factor production [GO:0032760]; positive thymic T cell selection [GO:0045059]; protein dephosphorylation [GO:0006470]; regulation of cell cycle [GO:0051726]; regulation of extrinsic apoptotic signaling pathway [GO:2001236]; regulation of gene expression [GO:0010468]; regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002923]; regulation of interleukin-8 production [GO:0032677]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; release of sequestered calcium ion into cytosol [GO:0051209]; response to gamma radiation [GO:0010332]; stem cell development [GO:0048864]; synaptic membrane adhesion [GO:0099560]; T cell differentiation [GO:0030217]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]
|
bleb [GO:0032059]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; membrane microdomain [GO:0098857]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
ankyrin binding [GO:0030506]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; signaling receptor binding [GO:0005102]; spectrin binding [GO:0030507]
|
PF12567;PF12453;PF00102;
|
2.60.40.10;3.90.190.10;
|
Protein-tyrosine phosphatase family, Receptor class 1/6 subfamily
|
PTM: Heavily N- and O-glycosylated.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:P08575}. Synapse {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:P08575}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
| null | null | null | null |
FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity. {ECO:0000250, ECO:0000269|PubMed:10415030}.
|
Mus musculus (Mouse)
|
P06801
|
MAOX_MOUSE
|
MEPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLNIHGLLPPCIISQELQVLRIIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSDVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANRNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLVVMAMEKEGLSKENARKKIWLVDSKGLIVKGRASLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSNPTSKAECSAEQCYKVTKGRAIFASGSPFDPVTLPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTAEVISQQVSDKHLQEGRLYPPLNTIRGVSLKIAVKIVQDAYKEKMATVYPEPQNKEEFVSSQMYSTNYDQILPDCYPWPAEVQKIQTKVNQ
|
1.1.1.40
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P48163}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P48163}; Note=Divalent metal cations. Prefers magnesium or manganese. {ECO:0000250|UniProtKB:P48163};
|
malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; protein homotetramerization [GO:0051289]; pyruvate metabolic process [GO:0006090]; regulation of NADP metabolic process [GO:1902031]; response to hormone [GO:0009725]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; malic enzyme activity [GO:0004470]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxaloacetate decarboxylase activity [GO:0008948]
|
PF00390;PF03949;
|
3.40.50.10380;3.40.50.720;
|
Malic enzymes family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48163}.
|
CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; Evidence={ECO:0000250|UniProtKB:P48163}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254; Evidence={ECO:0000250|UniProtKB:P48163}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18255; Evidence={ECO:0000250|UniProtKB:P48163}; CATALYTIC ACTIVITY: Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=1.1.1.40; Evidence={ECO:0000250|UniProtKB:P48163}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642; Evidence={ECO:0000250|UniProtKB:P48163};
| null | null | null | null |
FUNCTION: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate. {ECO:0000250|UniProtKB:P48163}.
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Mus musculus (Mouse)
|
P06802
|
ENPP1_MOUSE
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MERDGDQAGHGPRHGSAGNGRELESPAAASLLAPMDLGEEPLEKAERARPAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFSNCRCDAACVSLGNCCLDFQETCVEPTHIWTCNKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKKSWVEETCESIDTPECPAEFESPPTLLFSLDGFRAEYLHTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPDIYKVYNGSVPFEERILAVLEWLQLPSHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYLGDVNNVKVVYGPAARLRPTDVPETYYSFNYEALAKNLSCREPNQHFRPYLKPFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLGLIPAPNNGSHGSLNHLLKKPIYNPSHPKEEGFLSQCPIKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDVDDIYHMTVPYGRPRILLKQHHVCLLQQQQFLTGYSLDLLMPLWASYTFLRNDQFSRDDFSNCLYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPRLNRVSNHIYSEALLTSNIVPMYQSFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQNSRVIRSQEILIPTHFFIVLTSCKQLSETPLECSALESSAYILPHRPDNIESCTHGKRESSWVEELLTLHRARVTDVELITGLSFYQDRQESVSELLRLKTHLPIFSQED
|
3.1.4.1; 3.6.1.9
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:30356045}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:30356045};
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adipose tissue development [GO:0060612]; adult locomotory behavior [GO:0008344]; adult walking behavior [GO:0007628]; aorta development [GO:0035904]; apoptotic process involved in development [GO:1902742]; artery development [GO:0060840]; articular cartilage development [GO:0061975]; ATP metabolic process [GO:0046034]; axon regeneration [GO:0031103]; B-1 B cell homeostasis [GO:0001922]; biomineral tissue development [GO:0031214]; bone development [GO:0060348]; bone growth [GO:0098868]; bone mineralization [GO:0030282]; bone mineralization involved in bone maturation [GO:0035630]; bone remodeling [GO:0046849]; bone resorption [GO:0045453]; bone trabecula formation [GO:0060346]; calcium ion homeostasis [GO:0055074]; cartilage development [GO:0051216]; cell morphogenesis [GO:0000902]; cell population proliferation [GO:0008283]; cellular homeostasis [GO:0019725]; cellular response to sodium phosphate [GO:1904384]; cementum mineralization [GO:0071529]; central nervous system myelination [GO:0022010]; coenzyme A catabolic process [GO:0015938]; collagen-activated signaling pathway [GO:0038065]; defense response to protozoan [GO:0042832]; determination of adult lifespan [GO:0008340]; diphosphate metabolic process [GO:0071344]; endochondral bone morphogenesis [GO:0060350]; endochondral ossification [GO:0001958]; establishment of localization in cell [GO:0051649]; fat cell differentiation [GO:0045444]; fat pad development [GO:0060613]; fatty acid metabolic process [GO:0006631]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; glucose import [GO:0046323]; glycolytic process [GO:0006096]; heart development [GO:0007507]; hematopoietic stem cell migration to bone marrow [GO:0097241]; hormone metabolic process [GO:0042445]; inflammatory response to antigenic stimulus [GO:0002437]; inhibition of non-skeletal tissue mineralization [GO:0140928]; inorganic diphosphate transport [GO:0030505]; kidney development [GO:0001822]; leukocyte activation involved in inflammatory response [GO:0002269]; ligamentous ossification [GO:0036076]; long-term synaptic potentiation [GO:0060291]; macrophage differentiation [GO:0030225]; magnesium ion homeostasis [GO:0010960]; microglia differentiation [GO:0014004]; microglial cell migration [GO:1904124]; middle ear morphogenesis [GO:0042474]; mitochondrion organization [GO:0007005]; morphogenesis of an epithelium [GO:0002009]; mRNA transcription by RNA polymerase II [GO:0042789]; mucus secretion [GO:0070254]; multicellular organism growth [GO:0035264]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of bone mineralization [GO:0030502]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of hh target transcription factor activity [GO:1990787]; negative regulation of ossification [GO:0030279]; neuron apoptotic process [GO:0051402]; nucleoside triphosphate catabolic process [GO:0009143]; odontogenesis [GO:0042476]; oligodendrocyte apoptotic process [GO:0097252]; organic phosphonate metabolic process [GO:0019634]; ossification [GO:0001503]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; phosphate ion homeostasis [GO:0055062]; plasma cell differentiation [GO:0002317]; post-embryonic forelimb morphogenesis [GO:0035128]; regulation of bone mineralization [GO:0030500]; response to ATP [GO:0033198]; response to dietary excess [GO:0002021]; response to Gram-positive bacterium [GO:0140459]; response to inorganic substance [GO:0010035]; response to insulin [GO:0032868]; response to magnesium ion [GO:0032026]; response to platelet-derived growth factor [GO:0036119]; response to sodium phosphate [GO:1904383]; response to vitamin B6 [GO:0034516]; response to wounding [GO:0009611]; sensory perception of mechanical stimulus [GO:0050954]; sensory perception of sound [GO:0007605]; sensory perception of temperature stimulus [GO:0050951]; skin development [GO:0043588]; smoothened signaling pathway [GO:0007224]; spinal cord development [GO:0021510]; T cell differentiation [GO:0030217]; tooth mineralization [GO:0034505]; vascular associated smooth muscle cell migration [GO:1904738]; vascular associated smooth muscle cell proliferation [GO:1990874]; vasculogenesis [GO:0001570]; vitamin D3 metabolic process [GO:0070640]; Wnt signaling pathway [GO:0016055]
|
apical dendrite [GO:0097440]; basal dendrite [GO:0097441]; basolateral plasma membrane [GO:0016323]; cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
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3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; ATP diphosphatase activity [GO:0047693]; calcium ion binding [GO:0005509]; coenzyme A diphosphatase activity [GO:0010945]; cyclic-GMP-AMP hydrolase activity [GO:0106177]; dinucleotide phosphatase activity [GO:0004551]; GTP diphosphatase activity [GO:0036219]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; phosphatase activity [GO:0016791]; phosphodiesterase I activity [GO:0004528]; phosphoric diester hydrolase activity [GO:0008081]; polysaccharide binding [GO:0030247]; protein homodimerization activity [GO:0042803]; pyrophosphatase activity [GO:0016462]; scavenger receptor activity [GO:0005044]; UTP diphosphatase activity [GO:0036221]; zinc ion binding [GO:0008270]
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PF01223;PF01663;PF01033;
|
4.10.410.20;3.40.720.10;3.40.570.10;
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Nucleotide pyrophosphatase/phosphodiesterase family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:8223581}.; PTM: The secreted form is produced through cleavage at Lys-85 by intracellular processing. {ECO:0000269|PubMed:23041369}.
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SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1]: Cell membrane {ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:3104326, ECO:0000269|PubMed:3917281}; Single-pass type II membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:11598187, ECO:0000269|PubMed:15075217}; Single-pass type II membrane protein. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. {ECO:0000269|PubMed:11598187, ECO:0000269|PubMed:15075217}.; SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form]: Secreted {ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:8223581}. Note=Secreted following proteolytic cleavage. {ECO:0000269|PubMed:23041369}.
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CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000269|PubMed:11027689, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:8223581}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:11027689, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:30356045, ECO:0000269|PubMed:8223581}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; Evidence={ECO:0000269|PubMed:30356045}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:23027977}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:23027977}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = diphosphate + GMP + H(+); Xref=Rhea:RHEA:29391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:23027977}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CMP + diphosphate + H(+); Xref=Rhea:RHEA:27762, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:60377; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:23027977}; CATALYTIC ACTIVITY: Reaction=2',3'-cGAMP + 2 H2O = AMP + GMP + 2 H(+); Xref=Rhea:RHEA:58808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115, ChEBI:CHEBI:143093, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:30356045}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58809; Evidence={ECO:0000269|PubMed:30356045}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP + 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P22413}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P22413};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for ATP {ECO:0000269|PubMed:23027977}; KM=4.3 mM for UTP {ECO:0000269|PubMed:23027977}; KM=4.2 mM for GTP {ECO:0000269|PubMed:23027977}; KM=1.2 mM for CTP {ECO:0000269|PubMed:23027977}; Note=kcat is 16 sec(-1) with ATP as substrate. kcat is 200 sec(-1) with UTP as substrate. kcat is 820 sec(-1) with GTP as substrate. kcat is 8.7 sec(-1) with CTP as substrate. {ECO:0000269|PubMed:23027977};
| null | null | null |
FUNCTION: Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930, PubMed:9662402). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:19419305, PubMed:22510396, PubMed:25260930, PubMed:25479107, PubMed:26910915, PubMed:30111653, PubMed:35147247, PubMed:9662402). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:11027689, PubMed:1647027, PubMed:23027977, PubMed:8223581). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:1647027). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (PubMed:30111653). Appears to modulate insulin sensitivity (By similarity). Also involved in melanogenesis (By similarity). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (By similarity). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3',3'-cGAMP (By similarity). {ECO:0000250|UniProtKB:P22413, ECO:0000269|PubMed:10352096, ECO:0000269|PubMed:11004006, ECO:0000269|PubMed:11027689, ECO:0000269|PubMed:12082181, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:19419305, ECO:0000269|PubMed:22510396, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:25260930, ECO:0000269|PubMed:25344812, ECO:0000269|PubMed:25479107, ECO:0000269|PubMed:26910915, ECO:0000269|PubMed:30111653, ECO:0000269|PubMed:35147247, ECO:0000269|PubMed:8223581, ECO:0000269|PubMed:9662402}.
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Mus musculus (Mouse)
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P06803
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PIM1_MOUSE
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MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11309};
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apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular detoxification [GO:1990748]; cellular response to type II interferon [GO:0071346]; negative regulation of apoptotic process [GO:0043066]; negative regulation of innate immune response [GO:0045824]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cardioblast proliferation [GO:1905062]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of TORC1 signaling [GO:1904263]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of hematopoietic stem cell proliferation [GO:1902033]; regulation of transmembrane transporter activity [GO:0022898]; vitamin D receptor signaling pathway [GO:0070561]
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cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
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ATP binding [GO:0005524]; manganese ion binding [GO:0030145]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ribosomal small subunit binding [GO:0043024]
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PF00069;
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1.10.510.10;
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Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PIM subfamily
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PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P11309}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P11309}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1825810}. Nucleus {ECO:0000269|PubMed:1825810}. Cell membrane {ECO:0000269|PubMed:1825810}. Note=Mainly located in the cytoplasm.
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CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed:15199164, PubMed:1825810). Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (By similarity). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (PubMed:18438430). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (PubMed:18438430). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (PubMed:15280015). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (By similarity). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (By similarity). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (By similarity). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (By similarity). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (By similarity). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (By similarity). Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (PubMed:19687226). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex (PubMed:31548394). Acts as a negative regulator of innate immunity by mediating phosphorylation and inactivation of GBP1 in absence of infection: phosphorylation of GBP1 induces interaction with 14-3-3 protein sigma (SFN) and retention in the cytosol (By similarity). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (By similarity). Promotes brown adipocyte differentiation (PubMed:27923061). {ECO:0000250|UniProtKB:P11309, ECO:0000269|PubMed:15199164, ECO:0000269|PubMed:15280015, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:19687226, ECO:0000269|PubMed:27923061, ECO:0000269|PubMed:31548394}.
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Mus musculus (Mouse)
|
P06804
|
TNFA_MOUSE
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MSTESMIRDVELAEEALPQKMGGFQNSRRCLCLSLFSFLLVAGATTLFCLLNFGVIGPQRDEKFPNGLPLISSMAQTLTLRSSSQNSSDKPVAHVVANHQVEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLVYSQVLFKGQGCPDYVLLTHTVSRFAISYQEKVNLLSAVKSPCPKDTPEGAELKPWYEPIYLGGVFQLEKGDQLSAEVNLPKYLDFAESGQVYFGVIAL
| null | null |
animal organ morphogenesis [GO:0009887]; antiviral innate immune response [GO:0140374]; apoptotic signaling pathway [GO:0097190]; calcium-mediated signaling [GO:0019722]; cellular extravasation [GO:0045123]; cellular response to amino acid stimulus [GO:0071230]; cellular response to amyloid-beta [GO:1904646]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nicotine [GO:0071316]; cellular response to retinoic acid [GO:0071300]; cellular response to toxic substance [GO:0097237]; cellular response to type II interferon [GO:0071346]; chronic inflammatory response to antigenic stimulus [GO:0002439]; circadian rhythm [GO:0007623]; cortical actin cytoskeleton organization [GO:0030866]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; defense response to Gram-positive bacterium [GO:0050830]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; embryonic digestive tract development [GO:0048566]; endothelial cell apoptotic process [GO:0072577]; epithelial cell proliferation involved in salivary gland morphogenesis [GO:0060664]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glucose metabolic process [GO:0006006]; humoral immune response [GO:0006959]; inflammatory response [GO:0006954]; inflammatory response to wounding [GO:0090594]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; JNK cascade [GO:0007254]; leukocyte migration [GO:0050900]; leukocyte migration involved in inflammatory response [GO:0002523]; leukocyte tethering or rolling [GO:0050901]; liver regeneration [GO:0097421]; macrophage activation involved in immune response [GO:0002281]; microglial cell activation [GO:0001774]; necroptotic signaling pathway [GO:0097527]; negative regulation of alkaline phosphatase activity [GO:0010693]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of apoptotic process [GO:0043066]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of bile acid secretion [GO:0120190]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of branching involved in lung morphogenesis [GO:0061048]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of glucose import [GO:0046325]; negative regulation of heart rate [GO:0010459]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of L-glutamate import across plasma membrane [GO:0002037]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of myelination [GO:0031642]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of oxidative phosphorylation [GO:0090324]; negative regulation of protein-containing complex disassembly [GO:0043242]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular wound healing [GO:0061044]; negative regulation of viral genome replication [GO:0045071]; osteoclast differentiation [GO:0030316]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of action potential [GO:0045760]; positive regulation of amide metabolic process [GO:0034250]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood microparticle formation [GO:2000334]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chronic inflammatory response to antigenic stimulus [GO:0002876]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of fever generation [GO:0031622]; positive regulation of fractalkine production [GO:0032724]; positive regulation of gene expression [GO:0010628]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of hair follicle development [GO:0051798]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-18 production [GO:0032741]; positive regulation of interleukin-33 production [GO:0150129]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of leukocyte adhesion to arterial endothelial cell [GO:1904999]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of neutrophil activation [GO:1902565]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitrogen compound metabolic process [GO:0051173]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein transport [GO:0051222]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of synoviocyte proliferation [GO:1901647]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translational initiation by iron [GO:0045994]; positive regulation of type II interferon production [GO:0032729]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; positive regulation of vitamin D biosynthetic process [GO:0060557]; protein localization to plasma membrane [GO:0072659]; regulation of branching involved in salivary gland morphogenesis [GO:0060693]; regulation of cell population proliferation [GO:0042127]; regulation of endothelial cell apoptotic process [GO:2000351]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of immunoglobulin production [GO:0002637]; regulation of inflammatory response [GO:0050727]; regulation of insulin secretion [GO:0050796]; regulation of membrane lipid metabolic process [GO:1905038]; regulation of osteoclast differentiation [GO:0045670]; regulation of protein phosphorylation [GO:0001932]; regulation of protein secretion [GO:0050708]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of synapse organization [GO:0050807]; response to 3,3',5-triiodo-L-thyronine [GO:1905242]; response to activity [GO:0014823]; response to ethanol [GO:0045471]; response to fructose [GO:0009750]; response to glucocorticoid [GO:0051384]; response to gold nanoparticle [GO:1990268]; response to Gram-negative bacterium [GO:0140460]; response to hypoxia [GO:0001666]; response to isolation stress [GO:0035900]; response to L-glutamate [GO:1902065]; response to lipopolysaccharide [GO:0032496]; response to macrophage colony-stimulating factor [GO:0036005]; response to nutrient levels [GO:0031667]; response to organic substance [GO:0010033]; response to xenobiotic stimulus [GO:0009410]; sequestering of triglyceride [GO:0030730]; skeletal muscle contraction [GO:0003009]; toll-like receptor 3 signaling pathway [GO:0034138]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor production [GO:0010573]; vasodilation [GO:0042311]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule [GO:0030141]
|
cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; receptor ligand activity [GO:0048018]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By similarity). {ECO:0000250}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated by SIRT6, promoting its secretion. {ECO:0000250|UniProtKB:P01375}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (PubMed:25586176). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (PubMed:32741026). {ECO:0000250|UniProtKB:P01375, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:32741026}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
|
Mus musculus (Mouse)
|
P06811
|
LAC1_NEUCR
|
MKFLGIAALVAGLLAPSLVLGAPAPGTEGVNLLTPVDKRQDSQAERYGGGGGGGCNSPTNRQCWSPGFNINTDYELGTPNTGKTRRYKLTLTETDNWIGPDGVIKDKVMMVNDKIIGPTIQADWGDYIEITVINKLKSNGTSIHWHGMHQRNSNIQDGVNGVTECPIPPRGGSKVYRWRATQYGTSWYHSHFSAQYGNGIVGPIVINGPASANYDVDLGPFPLTDYYYDTADRLVLLTQHAGPPPSNNVLFNGFAKHPTTGAGQYATVSLTKGKKHRLRLINTSVENHFQLSLVNHSMTIISADLVPVQPYKVDSLFLGVGQRYDVIIDANQAVGNYWFNVTFGGSKLCGDSDNHYPAAIFRYQGAPKALPTNQGVAPVDHQCLDLNDLKPVLQRSLNTNSIALNTGNTIPITLDGFVWRVNGTAININWNKPVLEYVLTGNTNYSQSDNIVQVEGVNQWKYWLIENDPDGAFSLPHPIHLHGHDFLILGRSPDVTAISQTRYVFDPAVDMARLNGNNPTRRDTAMLPAKGWLLIAFRTDNPGSWLMHCHIAWHVSGGLSNQFLERAQDLRNSISPADKKAFNDNCDAWRAYFPDNAPFPKDDSGLRSGVKAREVKMKW
|
1.10.3.2
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q70KY3}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
|
lignin catabolic process [GO:0046274]
|
extracellular region [GO:0005576]
|
copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491]
|
PF00394;PF07731;PF07732;
|
2.60.40.420;
|
Multicopper oxidase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
|
CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000250|UniProtKB:Q70KY3};
| null | null | null | null |
FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000250|UniProtKB:Q70KY3}.
|
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
|
P06814
|
CAN2_RABIT
|
QKLIRIRNPWGEVEWTGRWNDNCPNWNTVDPEVRERLAERHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYVIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELRGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKNGDFCVRVFSEKKADYQAVDDEIEADLEEADVSEDDIDDGFRRLFAQLAGEDAEISAFELQNILRRVLAKRQDIKTDGLSIETCKIMVDMLDSDGTGKLGLKEFYVLWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHEVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPDNTGMIQLDLISWLCFSVL
|
3.4.22.53
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250};
|
cellular response to amino acid stimulus [GO:0071230]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]
|
PF01067;PF13833;PF00648;
|
2.60.120.380;3.90.70.10;1.10.238.10;
|
Peptidase C2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
|
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
| null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:P17655}.
|
Oryctolagus cuniculus (Rabbit)
|
P06815
|
CAN1_RABIT
|
RESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPRELVGQPALHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKRAGTQELDDQIQANLPDEQVLSAEEIDENFKALFRQLAGEDLEISVRELQTILNRITSKHKDLRTKGFSMESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLAIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
|
3.4.22.52
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:3038855}; Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:3038855};
|
proteolysis [GO:0006508]; regulation of catalytic activity [GO:0050790]; self proteolysis [GO:0097264]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; peptidase activity [GO:0008233]
|
PF01067;PF13833;
|
2.60.120.380;1.10.238.10;
|
Peptidase C2 family
|
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:3667575}.; PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity). {ECO:0000250|UniProtKB:P07384}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}.
|
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000250|UniProtKB:P07384};
| null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1. Cleaves and activates caspase-7 (CASP7). {ECO:0000250|UniProtKB:P07384}.
|
Oryctolagus cuniculus (Rabbit)
|
P06820
|
NRAM_I67A0
|
MNPNQKIITIGSVSLTIATVCFLMQIAILVTTVTLHFKQHECDSPASNQVMPCEPIIIERNITEIVYLNNTTIEKEICPKVVEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRNPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWSTPNSKSQINRQVIVDSDNRSGYSGIFSVEGKSCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
|
3.2.1.18
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809};
|
carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872]
|
PF00064;
|
2.120.10.10;
|
Glycosyl hydrolase 34 family
|
PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP-Rule:MF_04071}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
| null | null | null | null |
FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. {ECO:0000255|HAMAP-Rule:MF_04071}.
|
Influenza A virus (strain A/Tokyo/3/1967 H2N2)
|
P06821
|
M2_I34A1
|
MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE
| null | null |
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]; uncoating of virus [GO:0019061]
|
extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; virion membrane [GO:0055036]
|
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
|
PF00599;
|
6.10.250.1640;
|
Influenza viruses matrix protein M2 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
| null | null | null | null | null |
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
|
P06829
|
L_SENDE
|
MDGQESSQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYRLKDDSIINITKHKIRNGGLSPRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTRELSSGFQDLWLNIFKQLGNIEGREGYDPLQDISTIPEITDKYSRNRWYRPFLTWFSIKYDMRWMQKTRPGGPIDTSNSHNLLECKSYTLVTYGDLVMILNKLTLTGYILTPELVLMYCDVVEGRWNMSAAGHLDKRSIGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLNDPVIPLRGAFMRHVLTELQTVLTSRDVYTDAEADTIVESLLAIFHGTSIDEKAEIFSFFRTFGHPSLEAVTAADKVRAHMYAQKAIKLKTLYECHAVFCTIIINGYRERHGGQWPPCDFPDHVCLELRNAQGSNTAISYECAVDNYTSFIGFKFRKFIEPQLDEDLTIYMKDKALSPRKEAWDSVYPDSNLYYKAPESEETRRLIEVFINDENFNPEEIINYVESGDWLKDEKFNISYSLKEKEIKQEGRLFAKMTYKMRAVQVLAETLLAKGIGELFSENGMVKGEIDLLKRLTTLSVSGVPRTDSVYNNSKSSEKRNEGMKKKNSGGYWDEKKRSRHEFKATDSSTDGYETLSCFLTTDLKKYCLNWRFESTALFGQRCNEIFGFKTFFNWMHPILERCTIYVGDPYCPVADRMHRQLQDHADSGIFIHNPRGGIEGYCQKLWTLISISAIHLAAVRVGVRVSAMVQGDNQAIAVTSRVPVAQTYKQKKNHVYEETTKYFGALRHVMFDVGHELKLNETIISSKMFVYSKRIYYDGKILPQCLKALTRCVFWSETLVDENRSACSNISTSIAKAIENGYSPILGYCIALYKTCQQVCISLGMTINPTISPTVRDQYFKGKNWLRCAVLIPANVGGFNYMSTSRCFVRNIGDPAVAALADLKRFIRADLLDKQVLYRVMNQEPGDSSFLDWAPDPYSCNLPHSQSITTIIKNITARSVLQESPNPLLSGLFTETSGEEDLNLASFLMDRKVILPRVAHEILGNSLTGVREAIAGMLDTTKSLVRASVRKGGLSYGILRRLVNYDLLQYETLTRTLRKPVKDNIEYEYMCSVELAVGLRQKMWIHLTYGRPIHGLETPDPLELLRGTFIEGSEVCKLCRSEGADPIYTWFYLPDNIDLDTLTNGSPAIRIPYFGSATDERSEAQLGYVRNLSKPAKAAIRIAMVYTWAYGTDEISWMEAALIAQTRANLSLENLKLLTPVSTPTNLSHRLKDTATQMKFSSATLVRASRFITISNDNMALKEAGESKDTNLVYQQIMLTGLSLFEFNMRYKKGSLGKPLILHLHLNNGCCIMESPQEANIPPRSTLDLEITQENNKLIYDPDPLKDVDLELFSKVRDVVHTVDMTYWSDDEVIRATSICTAMTIADTMSQLDRDNLKEMIALVNDDDVNSLITEFMVIDVPLFCSTFGGILVNQFAYSLYGLNIRGREEIWGHVVRILKDTSHAVLKVLSNALSHPKIFKRFWNAGVVEPVYGPNLSNQDKILLALSVCEYSVDLFMHDWQGGVPLEIFICDNDPDVADMRRSSFLARHLAYLCSLAEISRDGPRLESMNSLERLESLKSYLELTFLDDPVLRYSQLTGLVIKVFPSTLTYIRKSSIKVLRTRGIGVPEVLEDWDPEADNALLDGIAAEIQQNIPLGHQTRAPFWGLRVSKSQVLRLRGYKEITRGEIGRSGVGLTLPFDGRYLSHQLRLFGINSTSCLKALELTYLLSPLVDKDKDRLYLGEGAGAMLSCYDATLGPCINYYNSGVYSCDVNGQRELNIYPAEVALVGKKLNNVTSLGQRVKVLFNGNPGSTWIGNDECEALIWNELQNSSIGLVHCDMEGGDHKDDQVVLHEHYSVIRIAYLVGDRDVVLISKIAPRLGTDWTRQLSLYLRYWDEVNLIVLKTSNPASTEMYLLSRHPKSDIIEDSKTVLASLLPLSKEDSIKIEKWILIEKAKAHEWVTRELREGSSSSGMLRPYHQALQTFGFEPNLYKLSRDFLSTMNIADTHNCMIAFNRVLKDTIFEWARITESDKRLKLTGKYDLYPVRDSGKLKTISRRLVLSWISLSMSTRLVTGSFPDQKFEARLQLGIVSLSSREIRNLRVITKTLLDRFEDIIHSITYRFLTKEIKILMKILGAVKMFGARQNEYTTVIDDGSLGDIEPYDSS
|
2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.-
| null | null |
host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
|
ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF14318;PF00946;
| null |
Paramyxovirus L protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156484; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate; Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88; Evidence={ECO:0000250|UniProtKB:P28887}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P28887};
| null | null | null | null |
FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. {ECO:0000250|UniProtKB:P03523}.; FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated. {ECO:0000250|UniProtKB:P03523}.
|
Sendai virus (strain Enders) (SeV)
|
P06836
|
NEUM_BOVIN
|
MLCCMRRTKQVEKNDEDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEANEKDEAAVAEGTEKKEGEGSTPAEAAPGAGPKPEEKTGKAGETPSEEKKGEGAPDAATEQAAPQAPAPSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATAPAAEDAAAMATAQPPTETAESSQAEEKIEAVDETKPKDSARQDEGKGEEREADQEHA
| null | null |
axon choice point recognition [GO:0016198]; axon regeneration [GO:0031103]; localization [GO:0051179]; regulation of growth [GO:0040008]; tissue regeneration [GO:0042246]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786]
|
PF00612;PF06614;PF10580;
|
1.20.5.190;
|
Neuromodulin family
|
PTM: Phosphorylated (PubMed:1828073, PubMed:2140056, PubMed:8454596). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (PubMed:2140056). {ECO:0000269|PubMed:1828073, ECO:0000269|PubMed:2140056, ECO:0000269|PubMed:8454596}.; PTM: Palmitoylated by ZDHHC3 (By similarity). Palmitoylation is regulated by ARF6 and is essential for plasma membrane association and axonal and dendritic filopodia induction. Deacylated by LYPLA2 (By similarity). {ECO:0000250|UniProtKB:P06837, ECO:0000250|UniProtKB:P17677}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Synapse {ECO:0000250|UniProtKB:P17677}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}. Perikaryon {ECO:0000250|UniProtKB:P07936}. Cell projection, dendrite {ECO:0000250|UniProtKB:P07936}. Cell projection, axon {ECO:0000250|UniProtKB:P07936}. Cytoplasm {ECO:0000250|UniProtKB:P07936}. Note=Cytoplasmic surface of growth cone and synaptic plasma membranes. {ECO:0000250|UniProtKB:P17677}.
| null | null | null | null | null |
FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction (By similarity). {ECO:0000250|UniProtKB:P17677}.
|
Bos taurus (Bovine)
|
P06837
|
NEUM_MOUSE
|
MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAATKAAQPPTETAESSQAEEEKDAVDEAKPKESARQDEGKEDPEADQEHA
| null | null |
astrocyte differentiation [GO:0048708]; axon choice point recognition [GO:0016198]; axon guidance [GO:0007411]; axon regeneration [GO:0031103]; cell fate commitment [GO:0045165]; radial glial cell differentiation [GO:0060019]; regulation of filopodium assembly [GO:0051489]; regulation of growth [GO:0040008]; regulation of postsynaptic specialization assembly [GO:0099150]; response to auditory stimulus [GO:0010996]; tissue regeneration [GO:0042246]
|
axon [GO:0030424]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; GABA-ergic synapse [GO:0098982]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]
|
calmodulin binding [GO:0005516]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786]
|
PF00612;PF06614;PF10580;
|
1.20.5.190;
|
Neuromodulin family
|
PTM: Phosphorylated (PubMed:18493953). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P07936, ECO:0000269|PubMed:18493953}.; PTM: Palmitoylated by ZDHHC3 (PubMed:27875292). Palmitoylation is regulated by ARF6 and is essential for plasma membrane association and axonal and dendritic filopodia induction. Deacylated by LYPLA2 (By similarity). {ECO:0000250|UniProtKB:P17677, ECO:0000269|PubMed:27875292}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Synapse {ECO:0000250|UniProtKB:P17677}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}. Perikaryon {ECO:0000250|UniProtKB:P07936}. Cell projection, dendrite {ECO:0000250|UniProtKB:P07936}. Cell projection, axon {ECO:0000250|UniProtKB:P07936}. Cytoplasm {ECO:0000250|UniProtKB:P07936}. Note=Cytoplasmic surface of growth cone and synaptic plasma membranes. {ECO:0000250|UniProtKB:P17677}.
| null | null | null | null | null |
FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction. {ECO:0000250|UniProtKB:P17677}.
|
Mus musculus (Mouse)
|
P06838
|
RAD10_YEAST
|
MNNTDPTSFESILAGVAKLRKEKSGADTTGSQSLEIDASKLQQQEPQTSRRINSNQVINAFNQQKPEEWTDSKATDDYNRKRPFRSTRPGKTVLVNTTQKENPLLNHLKSTNWRYVSSTGINMIYYDYLVRGRSVLFLTLTYHKLYVDYISRRMQPLSRNENNILIFIVDDNNSEDTLNDITKLCMFNGFTLLLAFNFEQAAKYIEYLNL
| null | null |
DNA amplification [GO:0006277]; double-strand break repair via single-strand annealing, removal of nonhomologous ends [GO:0000736]; meiotic mismatch repair [GO:0000710]; mitotic recombination [GO:0006312]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; removal of nonhomologous ends [GO:0000735]; UV-damage excision repair [GO:0070914]
|
endonuclease complex [GO:1905348]; ERCC4-ERCC1 complex [GO:0070522]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634]
|
damaged DNA binding [GO:0003684]; endonuclease activity [GO:0004519]; single-stranded DNA binding [GO:0003697]
|
PF03834;
|
3.40.50.10130;
|
ERCC1/RAD10/SWI10 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD1 forms an endonuclease that specifically degrades single-stranded DNA. {ECO:0000269|PubMed:8479526}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06839
|
RAD3_YEAST
|
MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEAIPGNIRRAEHFVSFLKRLIEYLKTRMKVLHVISETPKSFLQHLKQLTFIERKPLRFCSERLSLLVRTLEVTEVEDFTALKDIATFATLISTYEEGFLLIIEPYEIENAAVPNPIMRFTCLDASIAIKPVFERFSSVIITSGTISPLDMYPRMLNFKTVLQKSYAMTLAKKSFLPMIITKGSDQVAISSRFEIRNDPSIVRNYGSMLVEFAKITPDGMVVFFPSYLYMESIVSMWQTMGILDEVWKHKLILVETPDAQETSLALETYRKACSNGRGAILLSVARGKVSEGIDFDHQYGRTVLMIGIPFQYTESRILKARLEFMRENYRIRENDFLSFDAMRHAAQCLGRVLRGKDDYGVMVLADRRFSRKRSQLPKWIAQGLSDADLNLSTDMAISNTKQFLRTMAQPTDPKDQEGVSVWSYEDLIKHQNSRKDQGGFIENENKEGEQDEDEDEDIEMQ
|
3.6.4.12
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305|PubMed:16973432}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305|PubMed:16973432};
|
nucleotide-excision repair [GO:0006289]; positive regulation of mitotic recombination [GO:0045951]; regulation of mitotic recombination [GO:0000019]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
cytosol [GO:0005829]; nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [GO:0005675]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872]
|
PF06733;PF06777;PF13307;
|
1.10.275.40;1.10.30.20;3.40.50.300;
|
Helicase family, RAD3/XPD subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
| null | null | null | null |
FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/RAD3 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. XPD/RAD3 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication. {ECO:0000269|PubMed:7813015, ECO:0000269|PubMed:7961739, ECO:0000269|PubMed:8269516, ECO:0000269|PubMed:8631896}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06843
|
SPT2_YEAST
|
MSFLSKLSQIRKSTTASKAQVQDPLPKKNDEEYSLLPKNYIRDEDPAVKRLKELRRQELLKNGALAKKSGVKRKRGTSSGSEKKKIERNDDDEGGLGIRFKRSIGASHAPLKPVVRKKPEPIKKMSFEELMKQAENNEKQPPKVKSSEPVTKERPHFNKPGFKSSKRPQKKASPGATLRGVSSGGNSIKSSDSPKPVKLNLPTNGFAQPNRRLKEKLESRKQKSRYQDDYDEEDNDMDDFIEDDEDEGYHSKSKHSNGPGYDRDEIWAMFNRGKKRSEYDYDELEDDDMEANEMEILEEEEMARKMARLEDKREEAWLKKHEEEKRRRKKGIR
| null | null |
chromatin organization [GO:0006325]; heterochromatin formation [GO:0031507]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; regulation of DNA-templated transcription [GO:0006355]; transcription by RNA polymerase I [GO:0006360]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA secondary structure binding [GO:0000217]; histone binding [GO:0042393]; histone chaperone activity [GO:0140713]
|
PF08243;
| null |
SPT2 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2072912, ECO:0000269|PubMed:26109053}.
| null | null | null | null | null |
FUNCTION: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Global regulatory protein that plays positive as well as negative regulatory roles in transcription (PubMed:2072912). {ECO:0000269|PubMed:2072912, ECO:0000269|PubMed:26109053}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06844
|
SPT3_YEAST
|
MMDKHKYRVEIQQMMFVSGEINDPPVETTSLIEDIVRGQVIEILLQSNKTAHLRGSRSILPEDVIFLIRHDKAKVNRLRTYLSWKDLRKNAKDQDASAGVASGTGNPGAGGEDDLKKAGGGEKDEKDGGNMMKVKKSQIKLPWELQFMFNEHPLENNDDNDDMDEDEREANIVTLKRLKMADDRTRNMTKEEYVHWSDCRQASFTFRKNKRFKDWSGISQLTEGKPHDDVIDILGFLTFEIVCSLTETALKIKQREQVLQTQKDKSQQSSQDNTNFEFASSTLHRKKRLFDGPENVINPLKPRHIEEAWRVLQTIDMRHRALTNFKGGRLSSKPIIM
| null | null |
chromatin organization [GO:0006325]; invasive growth in response to glucose limitation [GO:0001403]; pseudohyphal growth [GO:0007124]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; SLIK (SAGA-like) complex [GO:0046695]
|
protein heterodimerization activity [GO:0046982]; transcription coregulator activity [GO:0003712]
|
PF02269;
|
1.10.20.10;
|
SPT3 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SPT3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. SPT3 regulates Ty1 as well as the mating factor genes. {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10580001, ECO:0000269|PubMed:10611242, ECO:0000269|PubMed:11485989, ECO:0000269|PubMed:12370284}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06845
|
TYRO_STRGA
|
MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVTTHNAFIIGDTDAGERTGHRSPSFLPWHRRYLLEFERALQSVDASVALPYWDWSADRTARASLWAPDFLGGTGRSLDGRVMDGPFAASAGNWPINVRVDGRAYLRRSLGTAVRELPTRAEVESVLGMATYDTAPWNSASDGFRNHLEGWRGVNLHNRVHVWVGGQMATGMSPNDPVFWLHHAYVDKLWAEWQRRHPGSGYLPAAGTPDVVDLNDRMKPWNDTSPADLLDHTAHYTFDTD
|
1.14.18.1
|
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:1901488, ECO:0000269|PubMed:2846043}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:1901488, ECO:0000269|PubMed:2846043};
|
melanin biosynthetic process [GO:0042438]; pigmentation [GO:0043473]
| null |
metal ion binding [GO:0046872]; tyrosinase activity [GO:0004503]
|
PF00264;
|
1.10.1280.10;
|
Tyrosinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1;
| null | null | null | null |
FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
|
Streptomyces glaucescens
|
P06850
|
CRF_HUMAN
|
MRLPLLVSAGVLLVALLPCPPCRALLSRGPVPGARQAPQHPQPLDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSLLAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGGHQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK
| null | null |
adrenal gland development [GO:0030325]; associative learning [GO:0008306]; cellular response to cocaine [GO:0071314]; cellular response to dexamethasone stimulus [GO:0071549]; chemical synaptic transmission [GO:0007268]; diterpenoid metabolic process [GO:0016101]; female pregnancy [GO:0007565]; glucocorticoid biosynthetic process [GO:0006704]; hormone-mediated apoptotic signaling pathway [GO:0008628]; hypothalamus development [GO:0021854]; inflammatory response [GO:0006954]; learning or memory [GO:0007611]; locomotory exploration behavior [GO:0035641]; long-term synaptic potentiation [GO:0060291]; lung development [GO:0030324]; monoatomic ion homeostasis [GO:0050801]; negative regulation of circadian sleep/wake cycle, REM sleep [GO:0042322]; negative regulation of epinephrine secretion [GO:0032811]; negative regulation of gene expression [GO:0010629]; negative regulation of glucagon secretion [GO:0070093]; negative regulation of luteinizing hormone secretion [GO:0033685]; negative regulation of norepinephrine secretion [GO:0010700]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuron apoptotic process [GO:0051402]; parturition [GO:0007567]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of circadian sleep/wake cycle, wakefulness [GO:0010841]; positive regulation of corticosterone secretion [GO:2000854]; positive regulation of corticotropin secretion [GO:0051461]; positive regulation of cortisol secretion [GO:0051464]; positive regulation of digestive system process [GO:0060456]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of protein phosphorylation [GO:0001934]; regulation of NMDA receptor activity [GO:2000310]; regulation of serotonin secretion [GO:0014062]; response to aldosterone [GO:1904044]; response to corticosterone [GO:0051412]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to ether [GO:0045472]; response to immobilization stress [GO:0035902]; response to pain [GO:0048265]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]; synaptic transmission, dopaminergic [GO:0001963]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; synapse [GO:0045202]; varicosity [GO:0043196]
|
corticotropin-releasing hormone activity [GO:0017045]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; corticotropin-releasing hormone receptor 2 binding [GO:0051431]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]
|
PF00473;
|
6.10.250.1920;
|
Sauvagine/corticotropin-releasing factor/urotensin I family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06296}.
| null | null | null | null | null |
FUNCTION: Hormone regulating the release of corticotropin from pituitary gland (By similarity). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). {ECO:0000250|UniProtKB:P06296, ECO:0000250|UniProtKB:Q8CIT0}.
|
Homo sapiens (Human)
|
P06856
|
DPOL_VACCW
|
MDVRCINWFESHGENRFLYLKSRCRNGETVFIRFPHYFYYVVTDEIYQSLSPPPFNARPLGKMRTIDIDETISYNLDIKDRKCSVADMWLIEEPKKRSIQNATMDEFLNISWFYISNGISPDGCYSLDEQYLTKINNGCYHCDDPRNCFAKKIPRFDIPRSYLFLDIECHFDKKFPSVFINPISHTSYCYIDLSGKRLLFTLINEEMLTEQEIQEAVDRGCLRIQSLMEMDYERELVLCSEIVLLRIAKQLLELTFDYVVTFNGHNFDLRYITNRLELLTGEKIIFRSPDKKEAVYLCIYERNQSSHKGVGGMANTTFHVNNNNGTIFFDLYSFIQKSEKLDSYKLDSISKNAFSCMGKVLNRGVREMTFIGDDTTDAKGKAAAFAKVLTTGNYVTVDEDIICKVIRKDIWENGFKVVLLCPTLPNDTYKLSFGKDDVDLAQMYKDYNLNIALDMARYCIHDACLCQYLWEYYGVETKTDAGASTYVLPQSMVFEYRASTVIKGPLLKLLLETKTILVRSETKQKFPYEGGKVFAPKQKMFSNNVLIFDYNSLYPNVCIFGNLSPETLVGVVVSTNRLEEEINNQLLLQKYPPPRYITVHCEPRLPNLISEIAIFDRSIEGTIPRLLRTFLAERARYKKMLKQATSSTEKAIYDSMQYTYKIVANSVYGLMGFRNSALYSYASAKSCTSIGRRMILYLESVLNGAELSNGMLRFANPLSNPFYMDDRDINPIVKTSLPIDYRFRFRSVYGDTDSVFTEIDSQDVDKSIEIAKELERLINNRVLFNNFKIEFEAVYKNLIMQSKKKYTTMKYSASSNSKSVPERINKGTSETRRDVSKFHKNMIKTYKTRLSEMLSEGRMNSNQVCIDILRSLETDLRSEFDSRSSPLELFMLSRMHHSNYKSADNPNMYLVTEYNKNNPETIELGERYYFAYICPANVPWTKKLVNIKTYETIIDRSFKLGSDQRIFYEVYFKRLTSEIVNLLDNKVLCISFFERMFGSKPTFYEA
|
2.7.7.7; 3.1.11.-
| null |
base-excision repair, gap-filling [GO:0006287]; DNA recombination [GO:0006310]; DNA replication proofreading [GO:0045004]; nucleotide-excision repair, DNA gap filling [GO:0006297]; SOS response [GO:0009432]; viral DNA genome replication [GO:0039693]
| null |
3'-5' exonuclease activity [GO:0008408]; 3'-5'-DNA exonuclease activity [GO:0008296]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; nucleotide binding [GO:0000166]
|
PF00136;PF08408;PF03104;PF08452;
|
1.10.287.690;3.90.1600.10;3.30.420.10;
|
DNA polymerase type-B family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral OPG148/A20 and OPG116/D4 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perform OPG116/D4synthesis across an abasic site. {ECO:0000269|PubMed:15843688}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P06857
|
LIPR1_CANLF
|
MVSIWTIALFLLGAAKAKEVCYEQIGCFSDAEPWAGTAIRPLKVLPWSPERIGTRFLLYTNKNPNNFQTLLPSDPSTIEASNFQTDKKTRFIIHGFIDKGEENWLLDMCKNMFKVEEVNCICVDWKKGSQTSYTQAANNVRVVGAQVAQMLSMLSANYSYSPSQVQLIGHSLGAHVAGEAGSRTPGLGRITGLDPVEASFQGTPEEVRLDPTDADFVDVIHTDAAPLIPFLGFGTSQQMGHLDFFPNGGEEMPGCKKNALSQIVDLDGIWEGTRDFVACNHLRSYKYYSESILNPDGFASYPCASYRAFESNKCFPCPDQGCPQMGHYADKFAVKTSDETQKYFLNTGDSSNFARWRYGVSITLSGKRATGQAKVALFGSKGNTHQFNIFKGILKPGSTHSNEFDAKLDVGTIEKVKFLWNNNVVNPTFPKVGAAKITVQKGEEKTVHSFCSESTVREDVLLTLTPC
| null | null |
lipid catabolic process [GO:0016042]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; carboxylic ester hydrolase activity [GO:0052689]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9726421}.
| null | null | null | null | null |
FUNCTION: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro).
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P06858
|
LIPL_HUMAN
|
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
|
3.1.1.32; 3.1.1.34
| null |
cellular response to fatty acid [GO:0071398]; cellular response to nutrient [GO:0031670]; cholesterol homeostasis [GO:0042632]; chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle mediated signaling [GO:0055096]; phospholipid metabolic process [GO:0006644]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chemokine production [GO:0032722]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of lipid storage [GO:0010884]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of sequestering of triglyceride [GO:0010890]; positive regulation of tumor necrosis factor production [GO:0032760]; response to bacterium [GO:0009617]; response to glucose [GO:0009749]; triglyceride catabolic process [GO:0019433]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
catalytic complex [GO:1902494]; cell surface [GO:0009986]; chylomicron [GO:0042627]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]
|
1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; phospholipase activity [GO:0004620]; protein homodimerization activity [GO:0042803]; protein-membrane adaptor activity [GO:0043495]; signaling receptor binding [GO:0005102]; triglyceride lipase activity [GO:0004806]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
|
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:24291057, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:27811232}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; Evidence={ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:30559189, ECO:0000269|PubMed:7592706}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:7592706}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:12032167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:12032167}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:7592706}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000305|PubMed:7592706}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:7592706}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000305|PubMed:7592706}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:12032167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000305|PubMed:12032167};
| null | null | null | null |
FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232). {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8675619}.
|
Homo sapiens (Human)
|
P06859
|
PA2A1_PROFL
|
MRTLWIMAVLLVGVDGGLWQFENMIIKVVKKSGILSYSAYGCYCGWGGRGKPKDATDRCCFVHDCCYGKVTGCNPKLGKYTYSWNNGDIVCEGDGPCKEVCECDRAAAICFRDNLDTYDRNKYWRYPASNCQEDSEPC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that is highly lipolytic and myolytic. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:1288500}.
|
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
|
P06865
|
HEXA_HUMAN
|
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
|
3.2.1.52
| null |
adult walking behavior [GO:0007628]; carbohydrate metabolic process [GO:0005975]; cell morphogenesis involved in neuron differentiation [GO:0048667]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; lipid storage [GO:0019915]; lysosome organization [GO:0007040]; maintenance of location in cell [GO:0051651]; myelination [GO:0042552]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; sensory perception of sound [GO:0007605]; sexual reproduction [GO:0019953]; skeletal system development [GO:0001501]
|
azurophil granule [GO:0042582]; beta-N-acetylhexosaminidase complex [GO:1905379]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:0016020]
|
acetylglucosaminyltransferase activity [GO:0008375]; beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]; protein heterodimerization activity [GO:0046982]
|
PF00728;PF14845;
|
3.30.379.10;3.20.20.80;
|
Glycosyl hydrolase 20 family
|
PTM: N-linked glycan at Asn-115 consists of Man(3)-GlcNAc(2) (Probable) (PubMed:1533633, PubMed:16698036, PubMed:19159218). N-linked glycan at Asn-157 consists of either GlcNAc or GlcNAc(2)-Man(7-9). N-linked glycan at Asn-295 consists of either GlcNAc, GlcNAc-Fuc, or GlcNAc(2)-Man(4) (Probable). {ECO:0000269|PubMed:1533633, ECO:0000269|PubMed:16698036, ECO:0000269|PubMed:19159218, ECO:0000305|PubMed:11707436}.
|
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164; Evidence={ECO:0000269|PubMed:11707436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277; Evidence={ECO:0000305|PubMed:11707436}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065, ChEBI:CHEBI:71502; Evidence={ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941; Evidence={ECO:0000305|PubMed:9694901}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218; Evidence={ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969; Evidence={ECO:0000305|PubMed:9694901}; CATALYTIC ACTIVITY: Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372, ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565, ChEBI:CHEBI:152566; Evidence={ECO:0000269|PubMed:11707436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373; Evidence={ECO:0000305|PubMed:11707436}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377, ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064; Evidence={ECO:0000269|PubMed:11707436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385; Evidence={ECO:0000305|PubMed:11707436};
| null | null | null | null |
FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2 (PubMed:11707436). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:8123671, PubMed:8672428, PubMed:9694901). {ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}.
|
Homo sapiens (Human)
|
P06866
|
HPT_RAT
|
MRALGAVVTLLLWGQLFAVELGNDATDIEDDSCPKPPEIANGYVEHLVRYRCRQFYKLQTEGDGIYTLNSEKQWVNPAAGDKLPKCEAVCGKPKHPVDQVQRIIGGSMDAKGSFPWQAKMISRHGLTTGATLISDQWLLTTAQNLFLNHSENATAKDIAPTLTLYVGKNQLVEIEKVVLHPERSVVDIGLIKLKQKVLVTEKVMPICLPSKDYVAPGRMGYVSGWGRNVNFRFTERLKYVMLPVADQEKCELHYEKSTVPEKKGAVSPVGVQPILNKHTFCAGLTKYEEDTCYGDAGSAFAVHDTEEDTWYAAGILSFDKSCAVAEYGVYVRATDLKDWVQETMAKN
| null | null |
acute-phase response [GO:0006953]; animal organ regeneration [GO:0031100]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; liver development [GO:0001889]; negative regulation of hydrogen peroxide catabolic process [GO:2000296]; Notch signaling pathway [GO:0007219]; response to bacterium [GO:0009617]; response to cobalamin [GO:0033590]; response to electrical stimulus [GO:0051602]; response to glucocorticoid [GO:0051384]; response to growth hormone [GO:0060416]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to lipopolysaccharide [GO:0032496]; response to magnesium ion [GO:0032026]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to starvation [GO:0042594]; response to X-ray [GO:0010165]; response to xenobiotic stimulus [GO:0009410]; spermatogenesis [GO:0007283]
|
blood microparticle [GO:0072562]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838]
|
antioxidant activity [GO:0016209]; hemoglobin binding [GO:0030492]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.10.70.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P06867
|
PLMN_PIG
|
MDHKEVVLLLLLFLKSGLGDSLDDYVNTQGAFLFSLSRKQVAARSVEECAAKCEAETNFICRAFQYHSKDQQCVVMAENSKTSPIARMRDVVLFEKRIYLSECKTGNGKNYRGTTSKTKSGVICQKWSVSSPHIPKYSPEKFPLAGLEENYCRNPDNDEKGPWCYTTDPETRFDYCDIPECEDECMHCSGEHYEGKISKTMSGIECQSWGSQSPHAHGYLPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPNKRWEFCDIPRCTTPPPTSGPTYQCLKGRGENYRGTVSVTASGHTCQRWSAQSPHKHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSEVRWDYCKIPSCGSSTTSTEYLDAPVPPEQTPVAQDCYRGNGESYRGTSSTTITGRKCQSWVSMTPHRHEKTPGNFPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEYCNLKKCSETEQQVTNFPAIAQVPSVEDLSEDCMFGNGKRYRGKRATTVAGVPCQEWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDDNGPWCYTTNPQKLFDYCDVPQCVTSSFDCGKPKVEPKKCPARVVGGCVSIPHSWPWQISLRHRYGGHFCGGTLISPEWVLTAKHCLEKSSSPSSYKVILGAHEEYHLGEGVQEIDVSKLFKEPSEADIALLKLSSPAIITDKVIPACLPTPNYVVADRTACYITGWGETKGTYGAGLLKEARLPVIENKVCNRYEYLGGKVSPNELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCALPNKPGVYVRVSRFVTWIEEIMRRN
|
3.4.21.7
| null |
blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; tissue remodeling [GO:0048771]
|
extracellular space [GO:0005615]
|
endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]
|
PF00051;PF00024;PF00089;
|
3.50.4.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family, Plasminogen subfamily
|
PTM: N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:3356193}.; PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-579, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7;
| null | null | null | null |
FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells (By similarity). {ECO:0000250}.
|
Sus scrofa (Pig)
|
P06868
|
PLMN_BOVIN
|
MLPASPKMEHKAVVFLLLLFLKSGLGDLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGRIVGGCVSKPHSWPWQVSLRRSSRHFCGGTLISPKWVLTAAHCLDNILALSFYKVILGAHNEKVREQSVQEIPVSRLFREPSQADIALLKLSRPAIITKEVIPACLPPPNYMVAARTECYITGWGETQGTFGEGLLKEAHLPVIENKVCNRNEYLDGRVKPTELCAGHLIGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSPYVPWIEETMRRN
|
3.4.21.7
| null |
blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; response to heat [GO:0009408]; tissue remodeling [GO:0048771]
|
extracellular space [GO:0005615]
|
endopeptidase activity [GO:0004175]; protein domain specific binding [GO:0019904]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]
|
PF00051;PF00024;PF00089;
|
3.50.4.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family, Plasminogen subfamily
|
PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:3846532}.; PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-583, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7;
| null | null | null | null |
FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P06869
|
UROK_MOUSE
|
MKVWLASLFLCALVVKNSEGGSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAVLQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSLSKKPSSSVDQQGFQCGQKALRPRFKIVGGEFTEVENQPWFAAIYQKNKGGSPPSFKCGGSLISPCWVASAAHCFIQLPKKENYVVYLGQSKESSYNPGEMKFEVEQLILHEYYREDSLAYHNDIALLKIRTSTGQCAQPSRSIQTICLPPRFTDAPFGSDCEITGFGKESESDYLYPKNLKMSVVKLVSHEQCMQPHYYGSEINYKMLCAADPEWKTDSCKGDSGGPLICNIEGRPTLSGIVSWGRGCAEKNKPGVYTRVSHFLDWIQSHIGEEKGLAF
|
3.4.21.73
| null |
angiogenesis [GO:0001525]; fibrinolysis [GO:0042730]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; plasminogen activation [GO:0031639]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of smooth muscle cell migration [GO:0014911]; regulation of cell adhesion [GO:0030155]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cell population proliferation [GO:0042127]; regulation of fibrinolysis [GO:0051917]; regulation of hepatocyte proliferation [GO:2000345]; regulation of plasminogen activation [GO:0010755]; regulation of smooth muscle cell-matrix adhesion [GO:2000097]; response to hypoxia [GO:0001666]; skeletal muscle tissue regeneration [GO:0043403]; smooth muscle cell migration [GO:0014909]; urokinase plasminogen activator signaling pathway [GO:0038195]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; protein complex involved in cell-matrix adhesion [GO:0098637]; serine protease inhibitor complex [GO:0097180]; serine-type endopeptidase complex [GO:1905370]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF00051;PF00089;
|
2.10.25.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4. {ECO:0000250|UniProtKB:P00749}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00749}.
|
CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.73;
| null | null | null | null |
FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. {ECO:0000250|UniProtKB:P00749}.
|
Mus musculus (Mouse)
|
P06870
|
KLK1_HUMAN
|
MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVELPTEEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKILPNDECKKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLMCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS
|
3.4.21.35
| null |
regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
extracellular exosome [GO:0070062]; nucleus [GO:0005634]; secretory granule [GO:0030141]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
|
PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located. {ECO:0000269|PubMed:15651049, ECO:0000269|PubMed:3163150}.
| null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.; FUNCTION: (Microbial infection) Cleaves Neisseria meningitidis NHBA in saliva; Neisseria is an obligate commensal of the nasopharyngeal mucosa. {ECO:0000269|PubMed:31369555}.
|
Homo sapiens (Human)
|
P06873
|
PRTK_PARAQ
|
MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLDENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA
|
3.4.21.64
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
|
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF05922;PF00082;
|
3.30.70.80;3.40.50.200;
|
Peptidase S8 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.; EC=3.4.21.64;
| null | null | null | null |
FUNCTION: Hydrolyzes keratin at aromatic and hydrophobic residues.
|
Parengyodontium album (Tritirachium album)
|
P06875
|
PAC_ECOLX
|
MKNRNRMIVNCVTASLMYYWSLPALAEQSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRAQIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLTALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNYPLKFNQQNSQTAALLPRYDLPAPMLDRPAKGADGALLALTAGKNRETIAAQFAQGGANGLAGYPTTSNMWVIGKSKAQDAKAIMVNGPQFGWYAPAYTYGIGLHGAGYDVTGNTPFAYPGLVFGHNGVISWGSTAGFGDDVDIFAERLSAEKPGYYLHNGKWVKMLSREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVASLLAWTHQMKAKNWQEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQSGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANWNNSPQKDYPASDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFLPTLQAATSGLTQSDPRRQLVETLTRWDGINLLNDDGKTWQQPGSAILNVWLTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAVQGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAMALTFRANNFFGVPQAAAEETRHQAEYQNRGTENDMIVFSPTTSDRPVLAWDVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQEVLHVQR
|
3.5.1.11
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per dimer.;
|
antibiotic biosynthetic process [GO:0017000]; response to antibiotic [GO:0046677]
|
periplasmic space [GO:0042597]
|
metal ion binding [GO:0046872]; penicillin amidase activity [GO:0008953]
|
PF01804;
|
1.10.1400.10;1.10.287.150;2.30.120.10;3.60.20.10;1.10.439.10;
|
Peptidase S45 family
| null |
SUBCELLULAR LOCATION: Periplasm.
|
CATALYTIC ACTIVITY: Reaction=a penicillin + H2O = 6-aminopenicillanate + a carboxylate; Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11;
| null | null | null | null | null |
Escherichia coli
|
P06876
|
MYB_MOUSE
|
MARRPRHSIYSSDEDDEDIEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQEPSKASQTPVATSFQKNNHLMGFGHASPPSQLSPSGQSSVNSEYPYYHIAEAQNISSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQALPTQNHTCSYPGWHSTSIVDQTRPHGDSAPVSCLGEHHATPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHESSGLDAPTLPSTPLIGHKLTPCRDQTVKTQKENSIFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHAVEDLQDVIKQESDESGIVAEFQESGPPLLKKIKQEVESPTEKSGNFFCSNHWAENSLSTQLFSQASPVADAPNILTSSVLMTPVSEDEDNVLKAFTVPKNRPLVGPLQPCSGAWEPASCGKTEDQMTASGPARKYVNAFSARTLVM
| null | null |
B cell differentiation [GO:0030183]; calcium ion transport [GO:0006816]; cellular response to interleukin-6 [GO:0071354]; cellular response to leukemia inhibitory factor [GO:1990830]; embryonic digestive tract development [GO:0048566]; G1/S transition of mitotic cell cycle [GO:0000082]; homeostasis of number of cells [GO:0048872]; in utero embryonic development [GO:0001701]; mitotic cell cycle [GO:0000278]; myeloid cell development [GO:0061515]; myeloid cell differentiation [GO:0030099]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of hepatic stellate cell activation [GO:2000491]; positive regulation of hepatic stellate cell proliferation [GO:1904899]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of testosterone secretion [GO:2000845]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta production [GO:0071636]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; spleen development [GO:0048536]; stem cell division [GO:0017145]; thymus development [GO:0048538]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; WD40-repeat domain binding [GO:0071987]
|
PF09316;PF07988;PF00249;
|
1.10.10.60;
| null |
PTM: SUMOylated by TRAF7; leading to MYB transcriptional activity inhibition. {ECO:0000269|PubMed:16162816}.; PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.; PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16162816}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. {ECO:0000269|PubMed:16162816}.
|
Mus musculus (Mouse)
|
P06879
|
PRL_MOUSE
|
MNSQGSAQKAGTLLLLLISNLLFCQNVQPLPICSAGDCQTSLRELFDRVVILSHYIHTLYTDMFIEFDKQYVQDREFMVKVINDCPTSSLATPEDKEQALKVPPEVLLNLILSLVQSSSDPLFQLITGVGGIQEAPEYILSRAKEIEEQNKQLLEGVEKIISQAYPEAKGNGIYFVWSQLPSLQGVDEESKILSLRNTIRCLRRDSHKVDNFLKVLRCQIAHQNNC
| null | null |
cell population proliferation [GO:0008283]; epithelial cell proliferation [GO:0050673]; female pregnancy [GO:0007565]; lactation [GO:0007595]; mammary gland development [GO:0030879]; maternal behavior [GO:0042711]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of lactation [GO:1903489]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; regulation of ossification [GO:0030278]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; response to nutrient levels [GO:0031667]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation.
|
Mus musculus (Mouse)
|
P06880
|
SOMA_MOUSE
|
MATDSRTSWLLTVSLLCLLWPQEASAFPAMPLSSLFSNAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKEEAQQRTDMELLRFSLLLIQSWLGPVQFLSRIFTNSLMFGTSDRVYEKLKDLEEGIQALMQELEDGSPRVGQILKQTYDKFDANMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF
| null | null |
animal organ development [GO:0048513]; cellular response to alkaline pH [GO:0071469]; cellular response to insulin stimulus [GO:0032869]; cellular response to thyroid hormone stimulus [GO:0097067]; female pregnancy [GO:0007565]; growth hormone receptor signaling pathway [GO:0060396]; lung alveolus development [GO:0048286]; neuroblast proliferation [GO:0007405]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of growth [GO:0045927]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of neurogenesis [GO:0050769]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of intracellular steroid hormone receptor signaling pathway [GO:0033143]; regulation of response to nutrient levels [GO:0032107]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to food [GO:0032094]; response to light stimulus [GO:0009416]; response to nutrient levels [GO:0031667]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; trans-Golgi network [GO:0005802]
|
growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
Mus musculus (Mouse)
|
P06881
|
CALCA_HUMAN
|
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFGRRRRDLQA
| null | null |
activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; cell-cell signaling [GO:0007267]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor internalization [GO:0002031]; leukocyte cell-cell adhesion [GO:0007159]; negative regulation of blood pressure [GO:0045776]; negative regulation of bone resorption [GO:0045779]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of osteoclast differentiation [GO:0045671]; nervous system process involved in regulation of systemic arterial blood pressure [GO:0001976]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of interleukin-1 alpha production [GO:0032730]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of macrophage differentiation [GO:0045651]; protein phosphorylation [GO:0006468]; receptor internalization [GO:0031623]; regulation of blood pressure [GO:0008217]; regulation of cytosolic calcium ion concentration [GO:0051480]; vasculature development [GO:0001944]; vasodilation [GO:0042311]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcitonin receptor binding [GO:0031716]; hormone activity [GO:0005179]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
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. It also elevates platelet cAMP. {ECO:0000269|PubMed:1318039}.
|
Homo sapiens (Human)
|
P06882
|
THYG_RAT
|
MMTLVLWVSTLLSSVCLVAANIFEYQVDAQPLRPCELQREKAFLKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLSFCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRSRRLLHGVGDKSPPQCDADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFTATSFGHPYIPSCHRDGHYQTVQCQMERMCWCVDAQGIEIPGTRQQGQPLFCAKDQSCASERQQALSRLYFETPGYFSPQDLLSSEDRLVPVSGARLDISCPPRIKELFVDSGLLRSIAVERYQQLSESRSLLREAIRAIFPSRELAGLALQFTTNPKRLQQNLFGGTFLVNAAQLNLSGALGTRSTFNFSQFFQQFGLPGFLVRDRATDLAKLLPVSLDSSPTPVPLRVPEKRVAMNKSVVGTFGFKVNLQENQDALKFLVSLMELPEFLVFLQRAVSVPEDRARDLGDVMEMVFSAQACKQTSGRFFVPSCTAEGSYEDIQCYAGECWCVNSQGKEVEGSRVSGGHPRCPTKCEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNSECYCVDAEGQVIPGTQSTIGEPKLCPSVCQLQAEQAFLGVVGVLLSNSSMVPPISSVYIPQCSTSGQWMPVQCDGPHEQVFEWYERWNTQNSDGQELTTATLLMKLMSYREVASTNFSLFLQSLYDAGQQSIFPVLAQYPSLQDVPQVVLEGATIQPGENIFLDPYIFWQILNGQLSQYPGPYSDFSMPLEHFNLRSCWCVDEAGQELDGTRTRAGEIPACPGPCEEVKFRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELGLPPLYPSREAFSEKFLRGSEYAIRLAAQSTLTFYQKLRASLGESNGTASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSQMPQCPTSCELSRANGLISAWKQAGHQRNPGPGDLFTPVCLQTGEYVRQQTSGTGAWCVDPSSGEGVPTNTNSSAQCPGLCDALKSRVLSRKVGLGYTPVCEALDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACESPQCPLPFSGSDVTDGVVFCETASSSGVTTVQQCQLFCRQGLRNVFSPGPLICNLESQRWVTLPLPRACQRPQLWQTMQTQAHFQLLLPPGKMCSIDYSGLLQAFQVFILDELITRGFCQIQVKTFGTLVSRTVCDNSSIQVGCLTAERLGVNATWKLQLEDISVGSLPNLHSIERALMGQDLLGRFANLIQSGKFQLHLDSKTFSADTILYFLNGDRFVTSPMTQLGCLEGFYRVSTTSQDPLGCVKCPEGSFSQDGKCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHCVTDCQRDEAGLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWLQTEAGLSESQCLMMRKFEKAPESKVIFDASSPVIVKSRVPSANSPLVQCLADCADDEACSFVTVSSMSSEVSCDLYSWTRDNFACVTSDQEEDAVDSLKETSFGSLRCQVKVRNSGKDSLAVYVKKGHEFTASGQKSFEPTGFQNVLSGLYSSVVFSALGTNLTDTHLFCLLACDQDSCCDGFIVTQVKEGPTICGLLSAPDILVCHINDWRDASDTQANGTCAGVTYDQGSRQMTMSLGGQEFLQGLTLLEGTQDSFISFQQVYLWKDSDIGSRPESMGCGRGMVPKSEAPEGADMATELFSPVDITQVIVNTSHSLPSQQYWLSTHLFSAEQANLWCLSRCAQEPVFCQLADIMESSSLYFTCSLYPEAQVCDNDVESNAKNCSQILPRQPTALFQRKVVLNDRVKNFYTRLPFQKLSGISIRDRIPMSEKLISNGFFECERLCDRDPCCTGFGFLNVSQMQGGEMTCLTLNSMGIQTCSEENGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDAPSFCPSAALQSLTEEKVALDSWQTLALSSVIIDPSIKHFDVAHISISATRNFSLAQDFCLQECSRHQDCLVTTLQIQQGVVRCVFYPDIQSCEHSLRSKTCWLLLHEEAAYIYRKSGAPLHQSDGISTPSVHIDSFGQLQGGSQVVKVGTAWKQVYQFLGVPYAAPPLAENRFQAPEVLNWTGSWDATKLRSSCWQPGTRTPTPPQISEDCLYLNVFVPENLVSNASVLVFFHNTVEMEGSGGQLNIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLITRPTRLQLFRKALLMGGSALSPAAIISPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNSKTAFYQALQNSLGGEDSDARILAAAIWYYSLEHSTDDYASFSRALENATRDYFIICPIVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQKAAEFATPWPDFVPGAGGESYKELSAQLPNRQGLKKADCSFWSKYIQTLKDADGAKDAQLTKSGEEDLEVGPGSEEDFSGSLEPVPKSYSK
| null | null |
hormone biosynthetic process [GO:0042446]; iodide transport [GO:0015705]; regulation of myelination [GO:0031641]; response to lipopolysaccharide [GO:0032496]; response to pH [GO:0009268]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]; thyroid hormone metabolic process [GO:0042403]; transcytosis [GO:0045056]
|
extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
anion binding [GO:0043168]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]
|
PF00135;PF07699;PF00086;
|
3.40.50.1820;4.10.800.10;2.10.50.10;
|
Type-B carboxylesterase/lipase family
|
PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2574 is coupled to donor Tyr-2541, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-109 in monomer 2 (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250|UniProtKB:P01266}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of thyroxine (T4). Following endocytosis, further processing occurs leading to the release of triiodothyronine (T3) and more T4 hormones. {ECO:0000250|UniProtKB:O08710}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08710}. Note=Secreted into the thyroid follicle lumen. Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers. {ECO:0000250|UniProtKB:O08710}.
| null | null | null | null | null |
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (By similarity). One dimer produces 7 thyroid hormone molecules (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266}.
|
Rattus norvegicus (Rat)
|
P06883
|
GLUC_RAT
|
MKTVYIVAGLFVMLVQGSWQHAPQDTEENARSFPASQTEPLEDPDQINEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIAEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDKK
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cellular response to glucagon stimulus [GO:0071377]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; negative regulation of apoptotic process [GO:0043066]; negative regulation of appetite [GO:0032099]; negative regulation of execution phase of apoptosis [GO:1900118]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; positive regulation of calcium ion import [GO:0090280]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; protein kinase A signaling [GO:0010737]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of insulin secretion [GO:0050796]; regulation of lipid metabolic process [GO:0019216]; response to activity [GO:0014823]; response to L-arginine [GO:1903576]; response to starvation [GO:0042594]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
|
PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas. {ECO:0000269|PubMed:8721980}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01275}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000250|UniProtKB:P01275}.
| null | null | null | null | null |
FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12626323}.; FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-dependent insulin release (Probable). Also stimulates insulin release in response to IL6 (By similarity). Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis (Probable). {ECO:0000250|UniProtKB:P01275, ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.; FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. {ECO:0000305|PubMed:10322410, ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.; FUNCTION: [Glicentin]: May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744}.; FUNCTION: Oxyntomodulin significantly reduces food intake. {ECO:0000269|PubMed:11564680}.
|
Rattus norvegicus (Rat)
|
P06899
|
H2B1J_HUMAN
|
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
| null | null |
antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; chromatin organization [GO:0006325]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO:0002227]; killing of cells of another organism [GO:0031640]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; nucleosome assembly [GO:0006334]; protein localization to CENP-A containing chromatin [GO:0061644]
|
CENP-A containing nucleosome [GO:0043505]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; lipopolysaccharide binding [GO:0001530]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons. {ECO:0000269|PubMed:11709551, ECO:0000269|PubMed:16627869}.; PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation (PubMed:12757711). Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. {ECO:0000250|UniProtKB:Q64475, ECO:0000269|PubMed:12757711}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: ADP-ribosylated by PARP1 or PARP2 on Ser-7 (H2BS6ADPr) in response to DNA damage (PubMed:34874266). H2BS6ADPr promotes recruitment of CHD1L (PubMed:34874266). Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in response to single-strand breaks (PubMed:27530147). Poly ADP-ribosylation on Glu-36 (H2BE35ADPr) by PARP1 regulates adipogenesis: it inhibits phosphorylation at Ser-37 (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). {ECO:0000250|UniProtKB:Q6ZWY9, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:34874266}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000269|PubMed:31645732}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
|
Homo sapiens (Human)
|
P06907
|
MYP0_RAT
|
MAPGAPSSSPSPILAALLFSSLVLSPTLAIVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGILGVVLLLLLLFYLIRYCWLRRQAALQRRLSAMEKGKFHKSSKDSSKRGRQTPVLYAMLDHSRSTKAASEKKSKGLGESRKDKK
| null | null |
cell aggregation [GO:0098743]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cell-cell junction maintenance [GO:0045217]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]
|
basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]
| null |
PF10570;PF07686;
|
2.60.40.10;
|
Myelin P0 protein family
|
PTM: N-glycosylated; contains sulfate-substituted glycan. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25189}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}.
| null | null | null | null | null |
FUNCTION: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction. {ECO:0000250|UniProtKB:P25189}.
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Rattus norvegicus (Rat)
|
P06909
|
CFAH_MOUSE
|
MRLSARIIWLILWTVCAAEDCKGPPPRENSEILSGSWSEQLYPEGTQATYKCRPGYRTLGTIVKVCKNGKWVASNPSRICRKKPCGHPGDTPFGSFRLAVGSQFEFGAKVVYTCDDGYQLLGEIDYRECGADGWINDIPLCEVVKCLPVTELENGRIVSGAAETDQEYYFGQVVRFECNSGFKIEGHKEIHCSENGLWSNEKPRCVEILCTPPRVENGDGINVKPVYKENERYHYKCKHGYVPKERGDAVCTGSGWSSQPFCEEKRCSPPYILNGIYTPHRIIHRSDDEIRYECNYGFYPVTGSTVSKCTPTGWIPVPRCTLKPCEFPQFKYGRLYYEESLRPNFPVSIGNKYSYKCDNGFSPPSGYSWDYLRCTAQGWEPEVPCVRKCVFHYVENGDSAYWEKVYVQGQSLKVQCYNGYSLQNGQDTMTCTENGWSPPPKCIRIKTCSASDIHIDNGFLSESSSIYALNRETSYRCKQGYVTNTGEISGSITCLQNGWSPQPSCIKSCDMPVFENSITKNTRTWFKLNDKLDYECLVGFENEYKHTKGSITCTYYGWSDTPSCYERECSVPTLDRKLVVSPRKEKYRVGDLLEFSCHSGHRVGPDSVQCYHFGWSPGFPTCKGQVASCAPPLEILNGEINGAKKVEYSHGEVVKYDCKPRFLLKGPNKIQCVDGNWTTLPVCIEEERTCGDIPELEHGSAKCSVPPYHHGDSVEFICEENFTMIGHGSVSCISGKWTQLPKCVATDQLEKCRVLKSTGIEAIKPKLTEFTHNSTMDYKCRDKQEYERSICINGKWDPEPNCTSKTSCPPPPQIPNTQVIETTVKYLDGEKLSVLCQDNYLTQDSEEMVCKDGRWQSLPRCIEKIPCSQPPTIEHGSINLPRSSEERRDSIESSSHEHGTTFSYVCDDGFRIPEENRITCYMGKWSTPPRCVGLPCGPPPSIPLGTVSLELESYQHGEEVTYHCSTGFGIDGPAFIICEGGKWSDPPKCIKTDCDVLPTVKNAIIRGKSKKSYRTGEQVTFRCQSPYQMNGSDTVTCVNSRWIGQPVCKDNSCVDPPHVPNATIVTRTKNKYLHGDRVRYECNKPLELFGQVEVMCENGIWTEKPKCRDSTGKCGPPPPIDNGDITSLSLPVYEPLSSVEYQCQKYYLLKGKKTITCRNGKWSEPPTCLHACVIPENIMESHNIILKWRHTEKIYSHSGEDIEFGCKYGYYKARDSPPFRTKCINGTINYPTCV
| null | null |
activation of membrane attack complex [GO:0001905]; angiogenesis [GO:0001525]; ATP metabolic process [GO:0046034]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; determination of adult lifespan [GO:0008340]; gene expression [GO:0010467]; glomerulus development [GO:0032835]; immune response [GO:0006955]; inflammatory response [GO:0006954]; kidney development [GO:0001822]; mitochondrial DNA metabolic process [GO:0032042]; mitochondrial gene expression [GO:0140053]; mitochondrion organization [GO:0007005]; monocyte aggregation [GO:0070487]; neuromuscular process [GO:0050905]; organelle localization [GO:0051640]; photoreceptor cell differentiation [GO:0046530]; platelet aggregation [GO:0070527]; regulation of complement activation [GO:0030449]; regulation of complement-dependent cytotoxicity [GO:1903659]; response to cytokine [GO:0034097]; response to dietary excess [GO:0002021]; retina development in camera-type eye [GO:0060041]; retinal pigment epithelium development [GO:0003406]; retinal rod cell development [GO:0046548]; vascular associated smooth muscle cell differentiation [GO:0035886]; visual perception [GO:0007601]
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axon [GO:0030424]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]
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complement component C3b binding [GO:0001851]; heparin binding [GO:0008201]
|
PF00084;
|
2.10.70.10;
| null |
PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P08603}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08603}.
| null | null | null | null | null |
FUNCTION: Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed. {ECO:0000250|UniProtKB:P08603}.
|
Mus musculus (Mouse)
|
P06915
|
CSP_PLABE
|
MKKCTILVVASLLLVNSLLPGYGQNKIIQAQRNLNELCYNEGNDNKLYHVLNSKNGKIYNRNTVNRLLPMLRRKKNEKKNEKIERNNKLKQPPPPPNPNDPPPPNPNDPPPPNPNDPPPPNPNDPPPPNANDPPPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPPPPNPNDPAPPQGNNNPQPQPRPQPQPQPQPQPQPQPQPQPRPQPQPQPGGNNNNKNNNNDDSYIPSAEKILEFVKQIRDSITEEWSQCNVTCGSGIRVRKRKGSNKKAEDLTLEDIDTEICKMDKCSSIFNIVSNSLGFVILLVLVFFN
| null | null |
positive regulation of developmental process [GO:0051094]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
| null |
PF00090;
|
2.20.100.10;
|
Plasmodium circumsporozoite protein family
|
PTM: During host cell invasion, proteolytically cleaved at the cell membrane in the region I by a papain-like cysteine protease of parasite origin. Cleavage is triggered by the sporozoite contact with highly sulfated heparan sulfate proteoglycans (HSPGs) present on the host hepatocyte cell surface. Cleavage exposes the TSP type-1 (TSR) domain and is required for productive invasion of host hepatocytes but not for adhesion to the host cell membrane. Cleavage is dispensable for sporozoite development in the oocyst, motility and for traversal of host and vector cells. {ECO:0000250|UniProtKB:P23093}.; PTM: O-glycosylated; maybe by POFUT2. {ECO:0000250|UniProtKB:P19597}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23093}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and the budding sporozoites. {ECO:0000250|UniProtKB:P23093}.
| null | null | null | null | null |
FUNCTION: Essential sporozoite protein (PubMed:9002517). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (PubMed:9002517). In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes (By similarity). Binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By similarity). {ECO:0000250|UniProtKB:P23093, ECO:0000269|PubMed:9002517}.; FUNCTION: [Circumsporozoite protein C-terminus]: In the vertebrate host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes and is required for sporozoite invasion of the host hepatocytes. {ECO:0000250|UniProtKB:P23093}.
|
Plasmodium berghei
|
P06922
|
VE4_HPV16
|
MADPAAATKYPLLKLLGSTWPTTPPRPIPKPSPWAPKKHRRLSSDQDQSQTPETPATPLSCCTETQWTVLQSSLHLTAHTKDGLTVIVTLHP
| null | null |
symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
| null |
PF02711;
| null |
Papillomaviridae E4 protein family
|
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability. {ECO:0000269|PubMed:19211765}.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:17360743}. Host nucleus {ECO:0000269|PubMed:17360743}.
| null | null | null | null | null |
FUNCTION: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions. {ECO:0000269|PubMed:12208959, ECO:0000269|PubMed:14694114, ECO:0000269|PubMed:15767402, ECO:0000269|PubMed:17360743, ECO:0000269|PubMed:25142587}.
|
Human papillomavirus type 16
|
P06935
|
POLG_WNV
|
MSKKPGGPGKNRAVNMLKRGMPRGLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSTKQKKRGGTAGFTILLGLIACAGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAILLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLADVRSYCYLASVSDLSTRAACPTMGEAHNEKRADPAFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACTTKATGWIIQKENIKYEVAIFVHGPTTVESHGKIGATQAGRFSITPSAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMSVGEKSFLVHREWFMDLNLPWSSAGSTTWRNRETLMEFEEPHATKQSVVALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFARTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANSKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLRGAQRLAALGDTAWDFGSVGGVFTSVGKAIHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIAMTFLAVGGVLLFLSVNVHADTGCAIDIGRQELRCGSGVFIHNDVEAWMDRYKFYPETPQGLAKIIQKAHAEGVCGLRSVSRLEHQMWEAIKDELNTLLKENGVDLSVVVEKQNGMYKAAPKRLAATTEKLEMGWKAWGKSIIFAPELANNTFVIDGPETEECPTANRAWNSMEVEDFGFGLTSTRMFLRIRETNTTECDSKIIGTAVKNNMAVHSDLSYWIESGLNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTISDSCEHRGPAARTTTESGKLITDWCCRSCTLPPLRFQTENGCWYGMEIRPTRHDEKTLVQSRVNAYNADMIDPFQLGLMVVFLATQEVLRKRWTAKISIPAIMLALLVLVFGGITYTDVLRYVILVGAAFAEANSGGDVVHLALMATFKIQPVFLVASFLKARWTNQESILLMLAAAFFQMAYYDAKNVLSWEVPDVLNSLSVAWMILRAISFTNTSNVVVPLLALLTPGLKCLNLDVYRILLLMVGVGSLIKEKRSSAAKKKGACLICLALASTGVFNPMILAAGLMACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADITWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVIGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGHDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDYPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMEEPAPAGFEPEMLRKKQITVLDLHPGAGKTRKILPQIIKEAINKRLRTAVLAPTRVVAAEMSEALRGLPIRYQTSAVHREHSGNEIVDVMCHATLTHRLMSPHRVPNYNLFIMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTSDPFPESNAPISDMQTEIPDRAWNTGYEWITEYVGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIIEEGDGRVILGEPSAITAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLVAQLYQPEREKVYTMDGEYRLRGEERKNFLEFLRTADLPVWLAYKVAAAGISYHDRKWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWADARVYSDHQALKSFKDFASGKRSQIGLVEVLGRMPEHFMVKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIVLIALLSVMSLGVFFLLMQRKGIGKIGLGGVILGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKNDIGSLLGHRPEARETTLGVESFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAVGCWGQVTLTVTVTAAALLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNVVVDGIVATDVPELERTTPVMQKKVGQIILILVSMAAVVVNPSVRTVREAGILTTAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSIMWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNHMTKEEFTRYRKEAITEVDRSAAKHARREGNITGGHPVSRGTAKLRWLVERRFLEPVGKVVDLGCGRGGWCYYMATQKRVQEVKGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSEASDTLLCDIGESSSSAEVEEHRTVRVLEMVEDWLHRGPKEFCIKVLCPYMPKVIEKMETLQRRYGGGLIRNPLSRNSTHEMYWVSHASGNIVHSVNMTSQVLLGRMEKKTWKGPQFEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLKKEYSSTWHQDANHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLARDKKPRMCSREEFIGKVNSNAALGAMFEEQNQWKNAREAVEDPKFWEMVDEEREAHLRGECNTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILKEVGTKPGGKVYADDTAGWDTRITKADLENEAKVLELLDGEHRRLARSIIELTYRHKVVKVMRPAADGKTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLGKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELIGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPANWVPTGRTTWSIHAKGEWMTTEDMLAVWNRVWIEENEWMEDKTPVERWSDVPYSGKREDIWCGSLIGTRTRATWAENIHVAINQVRSVIGEEKYVDYMSSLRRYEDTIVVEDTVL
|
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
| null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; positive regulation of viral genome replication [GO:0045070]; proteolysis [GO:0006508]; RNA 5'-cap (guanine-N7)-methylation [GO:0106005]; RNA stabilization [GO:0043489]; symbiont-mediated suppression of host apoptosis [GO:0033668]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity [GO:0039576]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; protein-DNA complex [GO:0032993]; ribonucleoprotein complex [GO:1990904]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA/DNA annealing activity [GO:1990814]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; peptidase activity [GO:0008233]; protein dimerization activity [GO:0046983]; RNA binding [GO:0003723]; RNA folding chaperone [GO:0140691]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
|
PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
|
1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10;
|
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:17067286}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: Not N-glycosylated. {ECO:0000269|PubMed:2441520}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Serine protease/Helicase NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.
|
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease/Helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000269|PubMed:16699025}. Host cytoplasm {ECO:0000250|UniProtKB:P14335}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity). Shuttles between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:P17763}.
|
CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; 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:0000250|UniProtKB:Q9Q6P4}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
| null | null | null | null |
FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:23522008}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes (PubMed:15367621). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM (By similarity). They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured (By similarity). These uncleaved prM would play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease/Helicase NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (By similarity). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:17267492). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:17267492). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:17267492}.
|
West Nile virus (WNV)
|
P06939
|
VPX_HV2RO
|
MTDPRETVPPGNSGEETIGEAFAWLNRTVEAINREAVNHLPRELIFQVWQRSWRYWHDEQGMSESYTKYRYLCIIQKAVYMHVRKGCTCLGRGHGPGGWRPGPPPPPPPGLV
| null | null |
viral life cycle [GO:0019058]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]; virion component [GO:0044423]
| null |
PF00522;
|
1.20.5.4730;
|
Lentivirus VPX protein family
| null |
SUBCELLULAR LOCATION: Virion. Host nucleus. Note=Nuclear just after virion uncoating, or if expressed in the absence of unprocessed GAG.
| null | null | null | null | null |
FUNCTION: Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:16457868}.
|
Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2)
|
P06959
|
ODP2_ECOLI
|
MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM
|
2.3.1.12
|
COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 3 lipoyl cofactors covalently.;
|
acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glycolytic process [GO:0006096]; pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090]
|
cytoplasm [GO:0005737]; pyruvate dehydrogenase complex [GO:0045254]
|
acetyltransferase activity [GO:0016407]; dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; lipoic acid binding [GO:0031405]
|
PF00198;PF00364;PF02817;
|
2.40.50.100;3.30.559.10;4.10.320.10;
|
2-oxoacid dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
| null | null | null | null |
FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
|
Escherichia coli (strain K12)
|
P06960
|
OTC2_ECOLI
|
MSDLYKKHFLKLLDFTPAQFTSLLTLAAQLKADKKNGKEVQKLTGKNIALIFEKDSTRTRCSFEVAAFDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAQYAGVPVWNGLTNEFHPTQLLADLMTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLLAPKACWPEESLVAECSALAEKHGGKITLTEDVAAGVKGADFIYTDVWVSMGEAKEKWAERIALLRGYQVNAQMMALTDNPNVKFLHCLPAFHDDQTTLGKQMAKEFDLHGGMEVTDEVFESAASIVFDQAENRMHTIKAVMMATLGE
|
2.1.3.3
| null |
arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240]; DNA damage response [GO:0006974]
|
cytoplasm [GO:0005737]
|
amino acid binding [GO:0016597]; metal ion binding [GO:0046872]; ornithine carbamoyltransferase activity [GO:0004585]
|
PF00185;PF02729;
|
3.40.50.1370;
|
Aspartate/ornithine carbamoyltransferase superfamily, OTCase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01109};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.02 mM for carbamoyl phosphate {ECO:0000269|PubMed:789338}; KM=5 mM for L-ornithine {ECO:0000269|PubMed:789338};
|
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
| null | null |
FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. {ECO:0000269|PubMed:789338}.
|
Escherichia coli (strain K12)
|
P06961
|
CCA_ECOLI
|
MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAPDVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALMREMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPAKWHPEIDTGIHTLMTLSMAAMLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIVKLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRIAAVASWKEQRCPKPE
|
2.7.7.72; 3.1.3.-; 3.1.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O28126}; Note=Magnesium is required for nucleotidyltransferase activity. {ECO:0000250|UniProtKB:O28126}; COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Nickel for phosphatase activity. {ECO:0000269|PubMed:15210699};
|
RNA repair [GO:0042245]; tRNA 3'-terminal CCA addition [GO:0001680]; tRNA surveillance [GO:0106354]
| null |
ATP binding [GO:0005524]; CCA tRNA nucleotidyltransferase activity [GO:0004810]; CCACCA tRNA nucleotidyltransferase activity [GO:0160016]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; magnesium ion binding [GO:0000287]; phosphatase activity [GO:0016791]; tRNA binding [GO:0000049]
|
PF01966;PF01743;PF12627;
|
3.30.460.10;1.10.3090.10;
|
TRNA nucleotidyltransferase/poly(A) polymerase family, Bacterial CCA-adding enzyme type 1 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72; Evidence={ECO:0000269|PubMed:3516995}; CATALYTIC ACTIVITY: Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3' CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071, ChEBI:CHEBI:195187; Evidence={ECO:0000269|PubMed:22076379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76236; Evidence={ECO:0000269|PubMed:22076379};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for ATP (in the tRNA-NT activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.03 mM for CTP (in the tRNA-NT activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.015 mM for tRNA-CC {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.02 mM for tRNA-C {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=6.2 mM for pNPP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.1 mM for PPi {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.15 mM for NADP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.19 mM for ADP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.18 mM for ATP (in the phosphatase activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.53 mM for CDP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.13 mM for CTP (in the phosphatase activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.76 mM for 2'-AMP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.49 mM for 2',3'-cAMP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=1.6 mM for 2',3'-cGMP {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=12.4 umol/min/mg enzyme with pNPP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=3.01 umol/min/mg enzyme with PPi as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=17.9 umol/min/mg enzyme with NADP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=1.49 umol/min/mg enzyme with ADP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=4.53 umol/min/mg enzyme with ATP as substrate (in the phosphatase activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=5.8 umol/min/mg enzyme with CDP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=4.03 umol/min/mg enzyme with CTP as substrate (in the phosphatase activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=3.71 umol/min/mg enzyme with 2'-AMP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=3.21 umol/min/mg enzyme with 2',3'-cAMP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; Vmax=2.36 umol/min/mg enzyme with 2',3'-cGMP as substrate {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4 for AMP incorporation, 10.0 for CMP incorporation, and 7.0 for the phosphatase and phosphodiesterase activities. {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
| null |
FUNCTION: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template (PubMed:3516995). Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate (PubMed:3516995). tRNA 3'-terminal CCA addition is required both for tRNA processing and repair (PubMed:22076379). Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs (PubMed:22076379). While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded (PubMed:22076379). The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA (By similarity). This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (By similarity). Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi (PubMed:15210699). Displays a metal-independent phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP (PubMed:15210699). Without metal or in the presence of Mg(2+), this protein hydrolyzes 2',3'-cyclic substrates with the formation of 2'-nucleotides, whereas in the presence of Ni(2+), it also produces some 3'-nucleotides (PubMed:15210699). These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases (PubMed:15210699). {ECO:0000250|UniProtKB:O28126, ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:22076379, ECO:0000269|PubMed:3516995}.
|
Escherichia coli (strain K12)
|
P06968
|
DUT_ECOLI
|
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ
|
3.6.1.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15208312};
|
dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]; protein homotrimerization [GO:0070207]
|
cytosol [GO:0005829]; protein-containing complex [GO:0032991]
|
dUTP diphosphatase activity [GO:0004170]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]
|
PF00692;
|
2.70.40.10;
|
DUTPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1311056, ECO:0000305|PubMed:9261872}.
|
CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:9261872};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 uM for dUTP {ECO:0000269|PubMed:9261872}; Note=kcat is 5.15 sec(-1). {ECO:0000269|PubMed:9261872};
|
PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
| null | null |
FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000269|PubMed:9261872}.
|
Escherichia coli (strain K12)
|
P06971
|
FHUA_ECOLI
|
MARSKTAQPKHSLRKIAVVVATAVSGMSVYAQAAVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF
| null | null |
intracellular iron ion homeostasis [GO:0006879]; siderophore transmembrane transport [GO:0044718]
|
cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495]
|
iron ion binding [GO:0005506]; protein domain specific binding [GO:0019904]; siderophore uptake transmembrane transporter activity [GO:0015344]; signaling receptor activity [GO:0038023]; toxic substance binding [GO:0015643]; virion binding [GO:0046790]
|
PF07715;PF00593;
|
2.40.170.20;2.170.130.10;
|
TonB-dependent receptor family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:8916906, ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}; Multi-pass membrane protein {ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}.
| null | null | null | null | null |
FUNCTION: Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane (PubMed:1089064, PubMed:2066336). In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1 (PubMed:1089064, PubMed:2066336, PubMed:353030, PubMed:8617231). The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system (PubMed:12427941, PubMed:353030, PubMed:9353297). {ECO:0000269|PubMed:1089064, ECO:0000269|PubMed:12427941, ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:353030, ECO:0000269|PubMed:8617231, ECO:0000269|PubMed:9353297}.
|
Escherichia coli (strain K12)
|
P06972
|
FHUB_ECOLI
|
MSKRIALFPALLLALLVIVATALTWMNFSQALPRSQWAQAAWSPDIDVIEQMIFHYSLLPRLAISLLVGAGLGLVGVLFQQVLRNPLAEPTTLGVATGAQLGITVTTLWAIPGAMASQFAAQAGACVVGLIVFGVAWGKRLSPVTLILAGLVVSLYCGAINQLLVIFHHDQLQSMFLWSTGTLTQTDWGGVERLWPQLLGGVMLTLLLLRPLTLMGLDDGVARNLGLALSLARLAALSLAIVISALLVNAVGIIGFIGLFAPLLAKMLGARRLLPRLMLASLIGALILWLSDQIILWLTRVWMEVSTGSVTALIGAPLLLWLLPRLRSISAPDMKVNDRVAAERQHVLAFALAGGVLLLMAVVVALSFGRDAHGWTWASGALLEDLMPWRWPRIMAALFAGVMLAVAGCIIQRLTGNPMASPEVLGISSGAAFGVVLMLFLVPGNAFGWLLPAGSLGAAVTLLIIMIAAGRGGFSPHRMLLAGMALSTAFTMLLMMLQASGDPRMAQVLTWISGSTYNATDAQVWRTGIVMVILLAITPLCRRWLTILPLGGDTARAVGMALTPTRIALLLLAACLTATATMTIGPLSFVGLMAPHIARMMGFRRTMPHIVISALVGGLLLVFADWCGRMVLFPFQIPAGLLSTFIGAPYFIYLLRKQSR
| null | null |
iron ion import across plasma membrane [GO:0098711]; siderophore-dependent iron import into cell [GO:0033214]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; plasma membrane [GO:0005886]
|
transmembrane transporter activity [GO:0022857]
|
PF01032;
|
1.10.3470.10;
|
Binding-protein-dependent transport system permease family, FecCD subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:15919996}.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:1551849, ECO:0000269|PubMed:3020380, ECO:0000269|PubMed:34887516}.
|
Escherichia coli (strain K12)
|
P06974
|
FLIM_ECOLI
|
MGDSILSQAEIDALLNGDSEVKDEPTASVSGESDIRPYDPNTQRRVVRERLQALEIINERFARHFRMGLFNLLRRSPDITVGAIRIQPYHEFARNLPVPTNLNLIHLKPLRGTGLVVFSPSLVFIAVDNLFGGDGRFPTKVEGREFTHTEQRVINRMLKLALEGYSDAWKAINPLEVEYVRSEMQVKFTNITTSPNDIVVNTPFHVEIGNLTGEFNICLPFSMIEPLRELLVNPPLENSRNEDQNWRDNLVRQVQHSQLELVANFADISLRLSQILKLNPGDVLPIEKPDRIIAHVDGVPVLTSQYGTLNGQYALRIEHLINPILNSLNEEQPK
| null | null |
bacterial-type flagellum-dependent swarming motility [GO:0071978]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935]; positive chemotaxis [GO:0050918]
|
bacterial-type flagellum [GO:0009288]; bacterial-type flagellum basal body, C ring [GO:0009433]; bacterial-type flagellum rotor complex [GO:0120107]; plasma membrane [GO:0005886]
|
cytoskeletal motor activity [GO:0003774]
|
PF02154;PF01052;
|
3.40.1550.10;2.30.330.10;
|
FliM family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. Bacterial flagellum basal body.
| null | null | null | null | null |
FUNCTION: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
|
Escherichia coli (strain K12)
|
P06983
|
HEM3_ECOLI
|
MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAREILAEVYNGDAPA
|
2.5.1.61
|
COFACTOR: Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Note=Binds 1 dipyrromethane group covalently.;
|
heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782]; tetrapyrrole biosynthetic process [GO:0033014]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
hydroxymethylbilane synthase activity [GO:0004418]
|
PF01379;PF03900;
|
3.40.190.10;3.30.160.40;
|
HMBS family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61; Evidence={ECO:0000269|PubMed:3052434};
| null |
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. {ECO:0000305|PubMed:3052434}.
| null | null |
FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000269|PubMed:3529035}.
|
Escherichia coli (strain K12)
|
P06988
|
HISX_ECOLI
|
MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALREYSAKFDKTTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQKLPPVDVETQPGVRCQQVTRPVASVGLYIPGGSAPLFSTVLMLATPASIAGCKKVVLCSPPPIADEILYAAQLCGVQDVFNVGGAQAIAALAFGTESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPDFVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQALNASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFLGDWSPESAGDYASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGFSALASTIETLAAAERLTAHKNAVTLRVNALKEQA
|
1.1.1.23
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11842181}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11842181};
|
histidine biosynthetic process [GO:0000105]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
histidinol dehydrogenase activity [GO:0004399]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270]
|
PF00815;
|
1.20.5.1300;3.40.50.1980;
|
Histidinol dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
| null |
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. {ECO:0000255|HAMAP-Rule:MF_01024}.
| null | null |
FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000255|HAMAP-Rule:MF_01024}.
|
Escherichia coli (strain K12)
|
P06992
|
RSMA_ECOLI
|
MNNRVHQGHLARKRFGQNFLNDQFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLDQLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTFNFGELAEKMGQPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCNVIPVLEVPPSAFTPPPKVDSAVVRLVPHATMPHPVKDVRVLSRITTEAFNQRRKTIRNSLGNLFSVEVLTGMGIDPAMRAENISVAQYCQMANYLAENAPLQES
|
2.1.1.182
| null |
maturation of SSU-rRNA [GO:0030490]; response to antibiotic [GO:0046677]; ribosomal small subunit assembly [GO:0000028]; rRNA base methylation [GO:0070475]; rRNA methylation [GO:0031167]; rRNA processing [GO:0006364]
|
cytosol [GO:0005829]
|
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity [GO:0052908]; double-stranded DNA binding [GO:0003690]; mRNA binding [GO:0003729]; ribosomal small subunit binding [GO:0043024]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179]
|
PF00398;
|
1.10.8.100;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, rRNA adenine N(6)-methyltransferase family, RsmA subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182;
| null | null | null | null |
FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and may play a role in protection of DNA against oxidative stress. {ECO:0000269|PubMed:18990185, ECO:0000269|PubMed:19223326, ECO:0000269|PubMed:3905517}.
|
Escherichia coli (strain K12)
|
P06993
|
MALT_ECOLI
|
MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIGWYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWHSPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSARRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFCYHPLFGNFLRQRCQWELAAELPEIHRAAAESWMAQGFPSEAIHHALAAGDALMLRDILLNHAWSLFNHSELSLLEESLKALPWDSLLENPQLVLLQAWLMQSQHRYGEVNTLLARAEHEIKDIREDTMHAEFNALRAQVAINDGNPDEAERLAKLALEELPPGWFYSRIVATSVLGEVLHCKGELTRSLALMQQTEQMARQHDVWHYALWSLIQQSEILFAQGFLQTAWETQEKAFQLINEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIEVLSSYQPQQQLQCLAMLIQCSLARGDLDNARSQLNRLENLLGNGKYHSDWISNANKVRVIYWQMTGDKAAAANWLRHTAKPEFANNHFLQGQWRNIARAQILLGEFEPAEIVLEELNENARSLRLMSDLNRNLLLLNQLYWQAGRKSDAQRVLLDALKLANRTGFISHFVIEGEAMAQQLRQLIQLNTLPELEQHRAQRILREINQHHRHKFAHFDENFVERLLNHPEVPELIRTSPLTQREWQVLGLIYSGYSNEQIAGELEVAATTIKTHIRNLYQKLGVAHRQDAVQHAQQLLKMMGYGV
| null | null |
positive regulation of carbohydrate metabolic process [GO:0045913]; positive regulation of DNA-templated transcription [GO:0045893]
| null |
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; trisaccharide binding [GO:0048031]
|
PF00196;PF17874;
|
3.40.50.300;1.25.40.10;1.10.10.10;
|
MalT family
| null | null | null | null | null | null | null |
FUNCTION: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides (PubMed:2524384, PubMed:2538630, PubMed:3305511, PubMed:7040340). Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box (5'-GGA[TG]GA-3') (PubMed:2524384, PubMed:2538630). Displays weak ATPase activity, but this activity is not required for promoter binding (PubMed:2524384). {ECO:0000269|PubMed:2524384, ECO:0000269|PubMed:2538630, ECO:0000269|PubMed:3305511, ECO:0000269|PubMed:7040340}.
|
Escherichia coli (strain K12)
|
P06996
|
OMPC_ECOLI
|
MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF
| null | null |
DNA damage response [GO:0006974]; monoatomic ion transmembrane transport [GO:0034220]; receptor-mediated virion attachment to host cell [GO:0046813]
|
cell outer membrane [GO:0009279]; pore complex [GO:0046930]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; porin activity [GO:0015288]; virus receptor activity [GO:0001618]
|
PF00267;
|
2.40.160.10;
|
Gram-negative porin family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269|PubMed:16949612}.
| null | null | null | null | null |
FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane.; FUNCTION: (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF. {ECO:0000305|PubMed:27723824}.; FUNCTION: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity. {ECO:0000269|PubMed:27723824}.
|
Escherichia coli (strain K12)
|
P06999
|
PFKB_ECOLI
|
MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR
|
2.7.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16866375};
|
DNA damage response [GO:0006974]; glycolytic process [GO:0006096]
|
cytosol [GO:0005829]
|
6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; tagatose-6-phosphate kinase activity [GO:0009024]
|
PF00294;
|
3.40.1190.20;
|
Carbohydrate kinase PfkB family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000269|PubMed:16866375, ECO:0000269|PubMed:23823238};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for ATP {ECO:0000269|PubMed:23823238}; KM=6 uM for fructose 6-phosphate {ECO:0000269|PubMed:23823238};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
| null | null |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000269|PubMed:16866375}.
|
Escherichia coli (strain K12)
|
P07001
|
PNTA_ECOLI
|
MRIGIPRERLTNETRVAATPKTVEQLLKLGFTVAVESGAGQLASFDDKAFVQAGAEIVEGNSVWQSEIILKVNAPLDDEIALLNPGTTLVSFIWPAQNPELMQKLAERNVTVMAMDSVPRISRAQSLDALSSMANIAGYRAIVEAAHEFGRFFTGQITAAGKVPPAKVMVIGAGVAGLAAIGAANSLGAIVRAFDTRPEVKEQVQSMGAEFLELDFKEEAGSGDGYAKVMSDAFIKAEMELFAAQAKEVDIIVTTALIPGKPAPKLITREMVDSMKAGSVIVDLAAQNGGNCEYTVPGEIFTTENGVKVIGYTDLPGRLPTQSSQLYGTNLVNLLKLLCKEKDGNITVDFDDVVIRGVTVIRAGEITWPAPPIQVSAQPQAAQKAAPEVKTEEKCTCSPWRKYALMALAIILFGWMASVAPKEFLGHFTVFALACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGQGGWVSFLSFIAVLIASINIFGGFTVTQRMLKMFRKN
|
7.1.1.1
| null |
NADPH regeneration [GO:0006740]; proton export across plasma membrane [GO:0120029]
|
plasma membrane [GO:0005886]
|
NAD(P)+ transhydrogenase (AB-specific) activity [GO:0008750]; NAD(P)+ transhydrogenase activity [GO:0008746]; NADP binding [GO:0050661]; protein dimerization activity [GO:0046983]
|
PF01262;PF05222;PF12769;
|
3.40.50.720;
|
AlaDH/PNT family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+); Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1; Evidence={ECO:0000269|PubMed:16083909};
| null | null | null | null |
FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. {ECO:0000269|PubMed:16083909}.
|
Escherichia coli (strain K12)
|
P07003
|
POXB_ECOLI
|
MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGRGDEVIELAKTNWLR
|
1.2.5.1
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6752142}; Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:6752142}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6286628, ECO:0000269|PubMed:6752142}; Note=Binds 1 Mg(2+) ion per subunit; Mn(2+) is also functional. The Me2+-thiamine diphosphate complex is the true cofactor. {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:6286628, ECO:0000269|PubMed:6752142}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6286628}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:6286628};
|
pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; pyruvate dehydrogenase (quinone) activity [GO:0052737]; thiamine pyrophosphate binding [GO:0030976]; ubiquinone binding [GO:0048039]
|
PF02775;PF00205;PF02776;
|
3.40.50.970;3.40.50.1220;
|
TPP enzyme family
|
PTM: Activated by limited proteolytic digestion in vitro. This cleavage produces a peptide (alpha-peptide) and mimics the activation of enzyme by phospholipids (PubMed:334770, PubMed:334771, PubMed:3902830, PubMed:5336022). Protease activation and lipid-activation are mutually exclusive. Proteolytic cleavage results in the loss of the high affinity lipid-binding site of the enzyme; the cleaved protein is no longer activated by lipids or detergents (PubMed:2663858, PubMed:334771). The proteolytically cleaved enzyme does not represent a functional cleavage in vivo (PubMed:3527254). {ECO:0000269|PubMed:2663858, ECO:0000269|PubMed:334770, ECO:0000269|PubMed:334771, ECO:0000269|PubMed:3527254, ECO:0000269|PubMed:3902830, ECO:0000269|PubMed:5336022}.
|
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2; Xref=Rhea:RHEA:27405, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389, ChEBI:CHEBI:16526, ChEBI:CHEBI:17976, ChEBI:CHEBI:30089; EC=1.2.5.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858, ECO:0000269|PubMed:3527254, ECO:0000269|PubMed:365232, ECO:0000269|PubMed:6286628, ECO:0000269|PubMed:6752142, ECO:0000305|PubMed:5336022};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 mM for pyruvate, non-activated form {ECO:0000269|PubMed:18988747}; KM=12 mM for pyruvate, activated form {ECO:0000269|PubMed:18988747}; Note=kcat is 7 sec(-1) for non-activated, 200 sec(-1) for activated form. {ECO:0000269|PubMed:18988747};
| null | null | null |
FUNCTION: A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone (By similarity) (PubMed:18988747, PubMed:2663858, PubMed:365232). The main pathway for acetate production during stationary phase (PubMed:16080684). {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:16080684, ECO:0000269|PubMed:18988747, ECO:0000269|PubMed:2663858, ECO:0000269|PubMed:365232}.
|
Escherichia coli (strain K12)
|
P07004
|
PROA_ECOLI
|
MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSEIILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESVEIAEALKVIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAKVVAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGIGDYTIRA
|
1.2.1.41
| null |
L-proline biosynthetic process [GO:0055129]
|
cytosol [GO:0005829]
|
glutamate-5-semialdehyde dehydrogenase activity [GO:0004350]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]
|
PF00171;
| null |
Gamma-glutamyl phosphate reductase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
|
CATALYTIC ACTIVITY: Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; Evidence={ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7034716, ECO:0000269|PubMed:7035170};
| null |
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7035170}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:7035170};
| null |
FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7034716, ECO:0000269|PubMed:7035170}.
|
Escherichia coli (strain K12)
|
P07012
|
RF2_ECOLI
|
MFEINPVNNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAVVDTLDQMKQGLEDVSGLLELAVEADDEETFNEAVAELDALEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLERMYLRWAESRGFKTEIIEESEGEVAGIKSVTIKISGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLRIDVYRTSGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEASLKAGL
| null | null |
translational termination [GO:0006415]
|
cytosol [GO:0005829]
|
translation release factor activity, codon specific [GO:0016149]
|
PF03462;PF00472;
|
3.30.160.20;3.30.70.1660;1.20.58.410;
|
Prokaryotic/mitochondrial release factor family
|
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced. {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:17932046}.
|
SUBCELLULAR LOCATION: Cytoplasm. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). {ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27934701}.
| null | null | null | null | null |
FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center (PTC) and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). A TnaC-stalled ribosome binds RF2, but the active GGQ motif is prevented from engaging with the PTC by TnaC (PubMed:34504068). {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:17932046, ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875, ECO:0000269|PubMed:34504068, ECO:0000305|PubMed:22857598}.
|
Escherichia coli (strain K12)
|
P07013
|
PRIB_ECOLI
|
MTNRLVLSGTVCRAPLRKVSPSGIPHCQFVLEHRSVQEEAGFHRQAWCQMPVIVSGHENQAITHSITVGSRITVQGFISCHKAKNGLSKMVLHAEQIELIDSGD
| null | null |
DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; plasmid maintenance [GO:0006276]; replication fork processing [GO:0031297]; response to radiation [GO:0009314]
|
DnaB-DnaC-DnaT-PriA-PriB complex [GO:1990158]; pre-primosome complex [GO:1990099]; primosome complex [GO:1990077]
|
identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]
|
PF00436;
|
2.40.50.140;
|
PriB family
| null | null | null | null | null | null | null |
FUNCTION: Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT. {ECO:0000255|HAMAP-Rule:MF_00720, ECO:0000269|PubMed:1646811, ECO:0000269|PubMed:1856227, ECO:0000269|PubMed:8366072}.
|
Escherichia coli (strain K12)
|
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