ID   ENTP1_BOVIN             Reviewed;         513 AA.
AC   O18956;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000250|UniProtKB:P49961};
DE            EC=3.6.1.5 {ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
DE   AltName: Full=Lymphoid cell activation antigen {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Nucleoside triphosphate diphosphohydrolase 1 {ECO:0000250|UniProtKB:P97687};
DE            Short=NTPDase1 {ECO:0000250|UniProtKB:P97687};
DE   AltName: CD_antigen=CD39 {ECO:0000250|UniProtKB:P49961};
GN   Name=ENTPD1 {ECO:0000250|UniProtKB:P49961};
GN   Synonyms=CD39 {ECO:0000250|UniProtKB:P49961};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic endothelium;
RA   Chang A.S., Garcia R.L., Chang S.M., Schilling W.P.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 97-103; 123-133; 136-140; 145-168 AND 459-471.
RC   TISSUE=Aorta;
RX   PubMed=8955160; DOI=10.1074/jbc.271.51.33116;
RA   Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J.,
RA   Beaudoin A.R., Bach F.H., Robson S.C.;
RT   "Identification and characterization of CD39/vascular ATP
RT   diphosphohydrolase.";
RL   J. Biol. Chem. 271:33116-33122(1996).
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. By hydrolyzing proinflammatory ATP
CC       and platelet-activating ADP to AMP, it blocks platelet aggregation and
CC       supports blood flow. {ECO:0000250|UniProtKB:P49961}.
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
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:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
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:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P97687}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF005940; AAB62382.1; -; mRNA.
DR   RefSeq; NP_776961.1; NM_174536.2.
DR   AlphaFoldDB; O18956; -.
DR   SMR; O18956; -.
DR   STRING; 9913.ENSBTAP00000071303; -.
DR   BindingDB; O18956; -.
DR   ChEMBL; CHEMBL2766; -.
DR   GlyCosmos; O18956; 7 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000045026; -.
DR   GeneID; 282223; -.
DR   KEGG; bta:282223; -.
DR   CTD; 953; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   InParanoid; O18956; -.
DR   SABIO-RK; O18956; -.
DR   PRO; PR:O18956; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043262; F:ADP phosphatase activity; IEA:RHEA.
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; IEA:RHEA.
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: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; ISS:UniProtKB.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
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   ATP-binding; Calcium; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT                   /id="PRO_0000209901"
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..481
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        503..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        255..300
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        281..327
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        340..345
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        393..416
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   CONFLICT        97
FT                   /note="K -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101..103
FT                   /note="INV -> CGF (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="K -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  58114 MW;  20FE98F27B6D2F96 CRC64;
     MEDRRESELK VFCSKNILSI LGFSCIIAVI ALLALGLTQN KALPENVKFG IVLDAGSSHT
     SLYIYRWPAE KENDTGVVTQ IEESNVKGPG ISGFAKKVNE INVYLTACME RAQKVIPSIQ
     HMETPVYLGA TAGMRLLRME NKQMADKILA AVASSISEYP FDFQGARIIS GQEEGAYGWI
     TVNYLLGKFT QKLSWFNLKP SKDDTQETYG ALDLGGASTQ ITFVPQNETT ESPNNNLYFR
     LYGKNYSVYT HSFLCYGKDQ ALLQKLALGL QGTNGIIHEP CFHSRYMRKI KMSVLNEGFC
     TKRHELNSSF YPLVDIEIRG AGNFQRCRQS IIQLFNTSYC PYSSCSFNGV FLPPLHGQFG
     AFSAFYYVME FLNLTSEESV SVEQLTEKLE EFCAQRWEEV QKNFGEVKEK YLSEYCFSGT
     YILVLLLNGY HFTAESWKNI HFMNKVRSTD VGWTLGYMLN LTNKIPAEEP MSPPLPHSTY
     VFLMVLFSLI LLAVIIVGIV VFHKPSYFWK DMV
//