ID   ENTP1_RAT               Reviewed;         511 AA.
AC   P97687;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000305};
DE            EC=3.6.1.5 {ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928, ECO:0000269|PubMed:9364474};
DE   AltName: Full=ATP diphosphohydrolase {ECO:0000250|UniProtKB:P49961};
DE            Short=ATP-DPH {ECO:0000250|UniProtKB:P49961};
DE            Short=ATPDase {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Ecto-ATP diphosphohydrolase 1 {ECO:0000250|UniProtKB:P49961};
DE            Short=Ecto-ATPDase 1;
DE            Short=Ecto-ATPase 1;
DE   AltName: Full=Ecto-apyrase {ECO:0000303|PubMed:9221928};
DE   AltName: Full=Lymphoid cell activation antigen {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Nucleoside triphosphate diphosphohydrolase 1 {ECO:0000303|PubMed:22100451};
DE            Short=NTPDase1 {ECO:0000303|PubMed:22100451};
DE   AltName: CD_antigen=CD39 {ECO:0000303|PubMed:9221928};
GN   Name=Entpd1 {ECO:0000312|RGD:69265};
GN   Synonyms=Cd39 {ECO:0000303|PubMed:9221928};
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], CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP   GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RX   PubMed=9221928; DOI=10.1016/s0169-328x(97)00066-1;
RA   Wang T.-F., Rosenberg P.A., Guidotti G.;
RT   "Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase
RT   (CD39) gene.";
RL   Brain Res. Mol. Brain Res. 47:295-302(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 432-511, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9364474; DOI=10.1016/s0028-3908(97)00115-9;
RA   Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.;
RT   "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat
RT   brain.";
RL   Neuropharmacology 36:1189-1200(1997).
RN   [3] {ECO:0007744|PDB:3ZX0, ECO:0007744|PDB:3ZX2, ECO:0007744|PDB:3ZX3}
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, DISULFIDE BONDS, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22100451; DOI=10.1016/j.jmb.2011.10.050;
RA   Zebisch M., Krauss M., Schafer P., Strater N.;
RT   "Crystallographic evidence for a domain motion in rat nucleoside
RT   triphosphate diphosphohydrolase (NTPDase) 1.";
RL   J. Mol. Biol. 415:288-306(2012).
CC   -!- FUNCTION: Catalyzes the hydrolysis of both di- and triphosphate
CC       nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide
CC       monophosphates (NMPs) in two distinct successive phosphate-releasing
CC       steps, with NDPs as intermediates and participates in the regulation of
CC       extracellular levels of nucleotides (PubMed:9221928, PubMed:9364474,
CC       PubMed:22100451). By hydrolyzing proinflammatory ATP and platelet-
CC       activating ADP to AMP, it blocks platelet aggregation and supports
CC       blood flow (By similarity). {ECO:0000250|UniProtKB:P49961,
CC       ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC       ECO:0000269|PubMed:9364474}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58043;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000269|PubMed:22100451, ECO:0000269|PubMed:9221928,
CC         ECO:0000269|PubMed:9364474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58069, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate;
CC         Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58280, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58280;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP;
CC         Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000269|PubMed:22100451};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:9221928};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9221928};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.7 uM for ADP {ECO:0000269|PubMed:22100451};
CC         KM=10 uM for UTP {ECO:0000269|PubMed:22100451};
CC         KM=11.3 uM for UDP {ECO:0000269|PubMed:22100451};
CC         KM=9 uM for GTP {ECO:0000269|PubMed:22100451};
CC         KM=11.4 uM for GDP {ECO:0000269|PubMed:22100451};
CC         KM=48.8 uM for GDP (with 100 uM AMP) {ECO:0000269|PubMed:22100451};
CC         KM=13.1 uM for GDP (with 100 uM UMP) {ECO:0000269|PubMed:22100451};
CC         KM=149 uM for GDP (with 100 muM hexaammonium heptamolybdate
CC         tetrahydrate) {ECO:0000269|PubMed:22100451};
CC         KM=10.8 uM for ITP {ECO:0000269|PubMed:22100451};
CC         KM=10.5 uM for IDP {ECO:0000269|PubMed:22100451};
CC         KM=749.5 uM for thiamine(1+) diphosphate
CC         {ECO:0000269|PubMed:22100451};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9MYU4}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P49961}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P49961}. Membrane, caveola
CC       {ECO:0000250|UniProtKB:P49961}.
CC   -!- TISSUE SPECIFICITY: Expressed in primary neurons and astrocytes,
CC       kidney, liver, muscle, thymus, lung and spleen.
CC       {ECO:0000269|PubMed:9221928}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9221928}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P49961}.
CC   -!- PTM: Palmitoylated on Cys-13; which is required for caveola targeting.
CC       {ECO:0000250|UniProtKB:P49961}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; U81295; AAC53195.1; -; mRNA.
DR   EMBL; Y15685; CAA75730.1; -; mRNA.
DR   PDB; 3ZX0; X-ray; 2.50 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR   PDB; 3ZX2; X-ray; 1.81 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR   PDB; 3ZX3; X-ray; 1.70 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR   PDBsum; 3ZX0; -.
DR   PDBsum; 3ZX2; -.
DR   PDBsum; 3ZX3; -.
DR   AlphaFoldDB; P97687; -.
DR   SMR; P97687; -.
DR   STRING; 10116.ENSRNOP00000051602; -.
DR   BindingDB; P97687; -.
DR   ChEMBL; CHEMBL2767; -.
DR   GuidetoPHARMACOLOGY; 2888; -.
DR   GlyCosmos; P97687; 7 sites, No reported glycans.
DR   GlyGen; P97687; 7 sites.
DR   iPTMnet; P97687; -.
DR   PhosphoSitePlus; P97687; -.
DR   SwissPalm; P97687; -.
DR   PaxDb; 10116-ENSRNOP00000051602; -.
DR   AGR; RGD:69265; -.
DR   RGD; 69265; Entpd1.
DR   eggNOG; KOG1386; Eukaryota.
DR   InParanoid; P97687; -.
DR   PhylomeDB; P97687; -.
DR   BRENDA; 3.6.1.5; 5301.
DR   BRENDA; 3.6.1.6; 5301.
DR   Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR   SABIO-RK; P97687; -.
DR   PRO; PR:P97687; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005604; C:basement membrane; ISO:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR   GO; GO:0043262; F:ADP phosphatase activity; IDA:RGD.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR   GO; GO:0036384; F:CDP phosphatase activity; IEA:RHEA.
DR   GO; GO:0043273; F:CTPase activity; IEA:RHEA.
DR   GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:1990003; F:IDP phosphatase activity; IEA:RHEA.
DR   GO; GO:0103023; F:ITPase activity; IEA:RHEA.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046032; P:ADP catabolic process; ISO:RGD.
DR   GO; GO:0071275; P:cellular response to aluminum ion; IEP:RGD.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEP:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IMP:RGD.
DR   GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0030168; P:platelet activation; ISO:RGD.
DR   GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0009181; P:purine ribonucleoside diphosphate catabolic process; ISO:RGD.
DR   GO; GO:0033198; P:response to ATP; IEP:RGD.
DR   GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
DR   GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR   GO; GO:1903576; P:response to L-arginine; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0010238; P:response to proline; IEP:RGD.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF32; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 1; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Calcium; Disulfide bond; Glycoprotein;
KW   Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..511
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT                   /id="PRO_0000209904"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        500..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          46..171
FT                   /note="N-terminal lobe"
FT   REGION          205..441
FT                   /note="C-terminal lobe"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O35795"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..108
FT                   /evidence="ECO:0000269|PubMed:22100451"
FT   DISULFID        254..300
FT                   /evidence="ECO:0000269|PubMed:22100451"
FT   DISULFID        281..324
FT                   /evidence="ECO:0000269|PubMed:22100451"
FT   DISULFID        337..342
FT                   /evidence="ECO:0000269|PubMed:22100451"
FT   DISULFID        391..414
FT                   /evidence="ECO:0000269|PubMed:22100451"
FT   STRAND          47..55
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          60..68
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           91..94
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           101..115
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           132..140
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           142..157
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           171..185
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          209..213
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          215..222
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          235..240
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          243..253
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           257..268
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           292..295
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           299..304
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           321..329
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          338..344
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          356..360
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           361..372
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           380..391
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           395..401
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           413..425
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   HELIX           432..437
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          438..440
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          442..444
FT                   /evidence="ECO:0007829|PDB:3ZX3"
FT   STRAND          447..451
FT                   /evidence="ECO:0007829|PDB:3ZX2"
FT   HELIX           452..459
FT                   /evidence="ECO:0007829|PDB:3ZX3"
SQ   SEQUENCE   511 AA;  57408 MW;  4CC123D3E644C193 CRC64;
     MEDIKDSKVK RFCSKNILII LGFSSVLAVI ALIAVGLTHN KPLPENVKYG IVLDAGSSHT
     NLYIYKWPAE KENDTGVVQL LEECQVKGPG ISKYAQKTDE IAAYLAECMK MSTERIPASK
     QHQTPVYLGA TAGMRLLRME SKQSADEVLA AVSRSLKSYP FDFQGAKIIT GQEEGAYGWI
     TINYLLGRFT QEQSWLNFIS DSQKQATFGA LDLGGSSTQV TFVPLNQTLE APETSLQFRL
     YGTDYTVYTH SFLCYGKDQA LWQKLAQDIQ VSSGGILKDP CFYPGYKKVV NVSELYGTPC
     TKRFEKKLPF NQFQVQGTGD YEQCHQSILK FFNNSHCPYS QCAFNGVFLP PLQGSFGAFS
     AFYFVMDFFK KMANDSVSSQ EKMTEITKNF CSKPWEEVKA SYPTVKEKYL SEYCFSGTYI
     LSLLLQGYNF TGTSWDQIHF MGKIKDSNAG WTLGYMLNLT NMIPAEQPLS PPLPHSTYIS
     LMVLFSLVLV AMVITGLFIF SKPSYFWKEA V
//