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ENPP1_RAT
ID   ENPP1_RAT               Reviewed;         906 AA.
AC   Q924C3; Q91XQ3; Q920C8;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1;
DE            Short=E-NPP 1;
DE   AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 1;
DE   AltName: Full=Plasma-cell membrane glycoprotein PC-1;
DE   Includes:
DE     RecName: Full=Alkaline phosphodiesterase I;
DE              EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
DE   Includes:
DE     RecName: Full=Nucleotide pyrophosphatase;
DE              Short=NPPase;
DE              EC=3.6.1.9 {ECO:0000250|UniProtKB:P06802};
DE     AltName: Full=Nucleotide diphosphatase {ECO:0000305};
DE   Contains:
DE     RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form {ECO:0000305};
GN   Name=Enpp1 {ECO:0000312|RGD:628825}; Synonyms=Npps, Pc1, Pdnp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS.
RC   STRAIN=Lewis, Louvain, and Wistar;
RX   PubMed=12121276; DOI=10.1046/j.1365-2370.2002.00330.x;
RA   Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.;
RT   "Structural basis of allotypes of ecto-nucleotide
RT   pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein PC-1)
RT   in the mouse and rat, and analysis of allele-specific xenogeneic
RT   antibodies.";
RL   Eur. J. Immunogenet. 29:307-313(2002).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND THR-238, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Nucleotide pyrophosphatase that generates diphosphate (PPi)
CC       and functions in bone mineralization and soft tissue calcification by
CC       regulating pyrophosphate levels. PPi inhibits bone mineralization and
CC       soft tissue calcification by binding to nascent hydroxyapatite
CC       crystals, thereby preventing further growth of these crystals.
CC       Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside
CC       5' triphosphates such as GTP, CTP and UTP to their corresponding
CC       monophosphates with release of pyrophosphate, as well as diadenosine
CC       polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the
CC       regulation of the availability of nucleotide sugars in the endoplasmic
CC       reticulum and Golgi, and the regulation of purinergic signaling.
CC       Inhibits ectopic joint calcification and maintains articular
CC       chondrocytes by repressing hedgehog signaling; it is however unclear
CC       whether hedgehog inhibition is direct or indirect (By similarity).
CC       Appears to modulate insulin sensitivity. Also involved in melanogenesis
CC       (By similarity). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a
CC       second messenger that activates TMEM173/STING and triggers type-I
CC       interferon production (By similarity). 2',3'-cGAMP degradation takes
CC       place in the lumen or extracellular space, and not in the cytosol where
CC       it is produced; the role of 2',3'-cGAMP hydrolysis is therefore
CC       unclear. Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3'-3'-
CC       cGAMP (By similarity). {ECO:0000250|UniProtKB:P06802,
CC       ECO:0000250|UniProtKB:P22413}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC         3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC         EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:P06802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = diphosphate + GMP + H(+); Xref=Rhea:RHEA:29391,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58115; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P06802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + H2O = CMP + diphosphate + H(+); Xref=Rhea:RHEA:27762,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:60377; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P06802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2',3'-cGAMP + 2 H2O = AMP + GMP + 2 H(+);
CC         Xref=Rhea:RHEA:58808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:143093, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP +
CC         2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P22413};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P06802};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06802};
CC   -!- ACTIVITY REGULATION: At low concentrations of ATP, a phosphorylated
CC       intermediate is formed which inhibits further hydrolysis.
CC       {ECO:0000250|UniProtKB:P06802}.
CC   -!- SUBUNIT: Ectonucleotide pyrophosphatase/phosphodiesterase family member
CC       1: Homodimer (By similarity). Ectonucleotide
CC       pyrophosphatase/phosphodiesterase family member 1: Interacts with INSR;
CC       leading to inhibit INSR autophosphorylation and subsequent activation
CC       of INSR kinase activity (By similarity). Ectonucleotide
CC       pyrophosphatase/phosphodiesterase family member 1, secreted form:
CC       Monomeric (By similarity). {ECO:0000250|UniProtKB:P06802,
CC       ECO:0000250|UniProtKB:P22413}.
CC   -!- SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase
CC       family member 1]: Cell membrane {ECO:0000250|UniProtKB:P06802}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:P06802}.
CC       Basolateral cell membrane {ECO:0000250|UniProtKB:P06802}; Single-pass
CC       type II membrane protein {ECO:0000250|UniProtKB:P06802}. Note=Targeted
CC       to the basolateral membrane in polarized epithelial cells and in
CC       hepatocytes, and to matrix vesicles in osteoblasts.
CC       {ECO:0000250|UniProtKB:P06802}.
CC   -!- SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase
CC       family member 1, secreted form]: Secreted
CC       {ECO:0000250|UniProtKB:P06802}. Note=Secreted following proteolytic
CC       cleavage. {ECO:0000250|UniProtKB:P06802}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q924C3-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q924C3-2; Sequence=VSP_006749;
CC   -!- DOMAIN: The di-leucine motif is required for basolateral targeting in
CC       polarized epithelial cells, and for targeting to matrix vesicles
CC       derived from mineralizing cells. {ECO:0000250|UniProtKB:P06802}.
CC   -!- PTM: The secreted form is produced through cleavage at Lys-85 by
CC       intracellular processing. {ECO:0000250|UniProtKB:P06802}.
CC   -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AF340185; AAK69653.1; -; mRNA.
DR   EMBL; AF340186; AAK69654.1; -; mRNA.
DR   EMBL; AF320054; AAL26912.1; -; mRNA.
DR   RefSeq; NP_445987.1; NM_053535.1. [Q924C3-1]
DR   AlphaFoldDB; Q924C3; -.
DR   SMR; Q924C3; -.
DR   IntAct; Q924C3; 6.
DR   STRING; 10116.ENSRNOP00000019519; -.
DR   ChEMBL; CHEMBL4295913; -.
DR   GlyGen; Q924C3; 6 sites.
DR   iPTMnet; Q924C3; -.
DR   PhosphoSitePlus; Q924C3; -.
DR   PaxDb; Q924C3; -.
DR   PRIDE; Q924C3; -.
DR   GeneID; 85496; -.
DR   KEGG; rno:85496; -.
DR   CTD; 5167; -.
DR   RGD; 628825; Enpp1.
DR   eggNOG; KOG2645; Eukaryota.
DR   InParanoid; Q924C3; -.
DR   OrthoDB; 999163at2759; -.
DR   PhylomeDB; Q924C3; -.
DR   BRENDA; 3.1.4.1; 5301.
DR   BRENDA; 3.6.1.9; 5301.
DR   Reactome; R-RNO-196843; Vitamin B2 (riboflavin) metabolism.
DR   SABIO-RK; Q924C3; -.
DR   PRO; PR:Q924C3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR   GO; GO:0097441; C:basal dendrite; IDA:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044297; C:cell body; IDA:RGD.
DR   GO; GO:0042995; C:cell projection; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0045202; C:synapse; IDA:RGD.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; ISO:RGD.
DR   GO; GO:0047693; F:ATP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0106177; F:cyclic-GMP-AMP hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004527; F:exonuclease activity; ISO:RGD.
DR   GO; GO:0036219; F:GTP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005158; F:insulin receptor binding; ISO:RGD.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004551; F:nucleotide diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; ISO:RGD.
DR   GO; GO:0004528; F:phosphodiesterase I activity; IDA:RGD.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; ISO:RGD.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR   GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR   GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR   GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR   GO; GO:0007568; P:aging; ISO:RGD.
DR   GO; GO:0035904; P:aorta development; ISO:RGD.
DR   GO; GO:1902742; P:apoptotic process involved in development; ISO:RGD.
DR   GO; GO:0060840; P:artery development; ISO:RGD.
DR   GO; GO:0061975; P:articular cartilage development; ISO:RGD.
DR   GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR   GO; GO:0031103; P:axon regeneration; ISO:RGD.
DR   GO; GO:0001922; P:B-1 B cell homeostasis; ISO:RGD.
DR   GO; GO:0031214; P:biomineral tissue development; ISO:RGD.
DR   GO; GO:0110148; P:biomineralization; ISO:RGD.
DR   GO; GO:0060348; P:bone development; ISO:RGD.
DR   GO; GO:0098868; P:bone growth; ISO:RGD.
DR   GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR   GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:RGD.
DR   GO; GO:0046849; P:bone remodeling; ISO:RGD.
DR   GO; GO:0045453; P:bone resorption; ISO:RGD.
DR   GO; GO:0060346; P:bone trabecula formation; ISO:RGD.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR   GO; GO:0051216; P:cartilage development; ISO:RGD.
DR   GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0019725; P:cellular homeostasis; ISO:RGD.
DR   GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:RGD.
DR   GO; GO:0071468; P:cellular response to acidic pH; IEP:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:1904384; P:cellular response to sodium phosphate; ISO:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0071529; P:cementum mineralization; ISO:RGD.
DR   GO; GO:0022010; P:central nervous system myelination; ISO:RGD.
DR   GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR   GO; GO:0038065; P:collagen-activated signaling pathway; ISO:RGD.
DR   GO; GO:0042832; P:defense response to protozoan; ISO:RGD.
DR   GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR   GO; GO:0071344; P:diphosphate metabolic process; ISO:RGD.
DR   GO; GO:0060350; P:endochondral bone morphogenesis; ISO:RGD.
DR   GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR   GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR   GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR   GO; GO:0060613; P:fat pad development; ISO:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0046323; P:glucose import; ISO:RGD.
DR   GO; GO:0006096; P:glycolytic process; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; ISO:RGD.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR   GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISO:RGD.
DR   GO; GO:0030505; P:inorganic diphosphate transport; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0002269; P:leukocyte activation involved in inflammatory response; ISO:RGD.
DR   GO; GO:0036076; P:ligamentous ossification; ISO:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0030225; P:macrophage differentiation; ISO:RGD.
DR   GO; GO:0010960; P:magnesium ion homeostasis; ISO:RGD.
DR   GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0014004; P:microglia differentiation; ISO:RGD.
DR   GO; GO:1904124; P:microglial cell migration; ISO:RGD.
DR   GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; ISO:RGD.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0070254; P:mucus secretion; ISO:RGD.
DR   GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR   GO; GO:0046325; P:negative regulation of glucose import; ISO:RGD.
DR   GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISO:RGD.
DR   GO; GO:1990787; P:negative regulation of hh target transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
DR   GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:RGD.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:RGD.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:RGD.
DR   GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR   GO; GO:0021772; P:olfactory bulb development; IEP:RGD.
DR   GO; GO:0097252; P:oligodendrocyte apoptotic process; ISO:RGD.
DR   GO; GO:0019634; P:organic phosphonate metabolic process; ISO:RGD.
DR   GO; GO:0001503; P:ossification; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR   GO; GO:0055062; P:phosphate ion homeostasis; ISO:RGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:RGD.
DR   GO; GO:0002317; P:plasma cell differentiation; ISO:RGD.
DR   GO; GO:0035128; P:post-embryonic forelimb morphogenesis; ISO:RGD.
DR   GO; GO:0006471; P:protein ADP-ribosylation; ISO:RGD.
DR   GO; GO:0140289; P:protein mono-ADP-ribosylation; ISO:RGD.
DR   GO; GO:0070212; P:protein poly-ADP-ribosylation; ISO:RGD.
DR   GO; GO:0030500; P:regulation of bone mineralization; IBA:GO_Central.
DR   GO; GO:0033198; P:response to ATP; ISO:RGD.
DR   GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR   GO; GO:0140459; P:response to Gram-positive bacterium; ISO:RGD.
DR   GO; GO:0010035; P:response to inorganic substance; ISO:RGD.
DR   GO; GO:0032868; P:response to insulin; ISO:RGD.
DR   GO; GO:0033591; P:response to L-ascorbic acid; ISO:RGD.
DR   GO; GO:0032026; P:response to magnesium ion; ISO:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0036119; P:response to platelet-derived growth factor; ISO:RGD.
DR   GO; GO:1904383; P:response to sodium phosphate; ISO:RGD.
DR   GO; GO:0034516; P:response to vitamin B6; ISO:RGD.
DR   GO; GO:0009611; P:response to wounding; ISO:RGD.
DR   GO; GO:0050954; P:sensory perception of mechanical stimulus; ISO:RGD.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR   GO; GO:0050951; P:sensory perception of temperature stimulus; ISO:RGD.
DR   GO; GO:0030730; P:sequestering of triglyceride; ISO:RGD.
DR   GO; GO:0043588; P:skin development; ISO:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0021510; P:spinal cord development; ISO:RGD.
DR   GO; GO:0021756; P:striatum development; IEP:RGD.
DR   GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR   GO; GO:0034505; P:tooth mineralization; ISO:RGD.
DR   GO; GO:1904738; P:vascular associated smooth muscle cell migration; ISO:RGD.
DR   GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; ISO:RGD.
DR   GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR   GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
DR   GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR   Gene3D; 3.40.570.10; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR029890; ENPP1.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR020436; SMB_chordata.
DR   InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR   InterPro; IPR001212; Somatomedin_B_dom.
DR   PANTHER; PTHR10151:SF77; PTHR10151:SF77; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF01033; Somatomedin_B; 2.
DR   PRINTS; PR00022; SOMATOMEDINB.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SMART; SM00201; SO; 2.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   SUPFAM; SSF54060; SSF54060; 1.
DR   SUPFAM; SSF90188; SSF90188; 2.
DR   PROSITE; PS00524; SMB_1; 2.
DR   PROSITE; PS50958; SMB_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Biomineralization; Calcium; Cell membrane;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..906
FT                   /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT                   family member 1"
FT                   /id="PRO_0000188566"
FT   CHAIN           85..906
FT                   /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT                   family member 1, secreted form"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT                   /id="PRO_0000447135"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..906
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          86..126
FT                   /note="SMB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DOMAIN          127..170
FT                   /note="SMB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..573
FT                   /note="Phosphodiesterase"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   REGION          579..628
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   REGION          635..906
FT                   /note="Nuclease"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   MOTIF           27..34
FT                   /note="Di-leucine motif"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   ACT_SITE        238
FT                   /note="AMP-threonine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         200
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         238
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         238
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         238
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         238
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         259
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         259
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         259
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         259
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         272
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         277
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         277
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         277
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         322
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         322
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         322
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         322
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         358
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         358
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         358
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         358
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         362
FT                   /ligand="2',3'-cGAMP"
FT                   /ligand_id="ChEBI:CHEBI:143093"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         406
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         406
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         406
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         406
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         406
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         514
FT                   /ligand="2',3'-cGAMP"
FT                   /ligand_id="ChEBI:CHEBI:143093"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         517
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         517
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         517
FT                   /ligand="dTMP"
FT                   /ligand_id="ChEBI:CHEBI:63528"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         517
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         517
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         781
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         783
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         785
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         787
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   BINDING         789
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   SITE            84..85
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P06802"
FT   SITE            896
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         238
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        90..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        94..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        102..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        108..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        131..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        136..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        146..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        152..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        177..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        185..397
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        413..512
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        462..849
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        596..653
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        607..707
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        609..692
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        819..829
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   VAR_SEQ         630
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:12121276"
FT                   /id="VSP_006749"
FT   VARIANT         440..442
FT                   /note="RPT -> NPP (in strain: Wistar)"
FT   VARIANT         457
FT                   /note="A -> T (in strain: Lewis)"
FT   VARIANT         555
FT                   /note="M -> I (in strain: Lewis)"
FT   VARIANT         568
FT                   /note="E -> G (in strain: Wistar)"
FT   VARIANT         583
FT                   /note="T -> I (in strain: Lewis)"
FT   VARIANT         592
FT                   /note="F -> V (in strain: Lewis)"
FT   VARIANT         624
FT                   /note="N -> K (in strain: Lewis)"
FT   VARIANT         640
FT                   /note="N -> H (in strain: Lewis)"
FT   VARIANT         774
FT                   /note="V -> I (in strain: Lewis)"
FT   VARIANT         806
FT                   /note="N -> I (in strain: Lewis)"
FT   VARIANT         850
FT                   /note="T -> I (in strain: Lewis)"
FT   VARIANT         898
FT                   /note="H -> Q (in strain: Lewis)"
SQ   SEQUENCE   906 AA;  102942 MW;  71F56780B279A919 CRC64;
     MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART AKDPNTYKVL
     SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE
     TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKAHNDCCI NYSSVCQEKK SWVEEACETI
     DAPQCPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP
     NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG
     TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY TLYLEEPDSS
     GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN
     KYLGDVNNVK VVYGPAARLR PTEVPETYYS FNYEALAKNL SCRETNQHFR PYLKHFLPKR
     LHFAKNDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG
     AEVDSFENIE VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS
     VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH RVCLLHQQQF
     LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP LSPMHKCSYY KSTSKLSYGF
     LTPPRLNRVS RQIYSEALLT SNIVPMYQSF QVIWQYLHDT VLRRYAQERN GVNVVSGPVF
     DFDYDGRYDS SEILKQNTRV IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP
     HRPDNIESCT HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP
     IFSQED
 
 
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