ID H2NB45_PONAB Unreviewed; 517 AA.
AC H2NB45;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00039600};
DE EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
DE AltName: Full=ATP diphosphohydrolase {ECO:0000256|ARBA:ARBA00044314};
DE AltName: Full=Ecto-ATP diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00042147};
DE AltName: Full=Ecto-apyrase {ECO:0000256|ARBA:ARBA00042196};
DE AltName: Full=Lymphoid cell activation antigen {ECO:0000256|ARBA:ARBA00041335};
DE AltName: Full=Nucleoside triphosphate diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00044280};
GN Name=ENTPD1 {ECO:0000313|Ensembl:ENSPPYP00000002915.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000002915.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000002915.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000002915.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043682};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736;
CC Evidence={ECO:0000256|ARBA:ARBA00043682};
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:0000256|ARBA:ARBA00043678};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897;
CC Evidence={ECO:0000256|ARBA:ARBA00043678};
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:0000256|ARBA:ARBA00036139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000256|ARBA:ARBA00036139};
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:0000256|ARBA:ARBA00043702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC Evidence={ECO:0000256|ARBA:ARBA00043702};
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:0000256|ARBA:ARBA00034440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
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:0000256|ARBA:ARBA00043676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC Evidence={ECO:0000256|ARBA:ARBA00043676};
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:0000256|ARBA:ARBA00043680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909;
CC Evidence={ECO:0000256|ARBA:ARBA00043680};
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:0000256|ARBA:ARBA00043776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC Evidence={ECO:0000256|ARBA:ARBA00043776};
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:0000256|ARBA:ARBA00043654};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC Evidence={ECO:0000256|ARBA:ARBA00043654};
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:0000256|ARBA:ARBA00043766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905;
CC Evidence={ECO:0000256|ARBA:ARBA00043766};
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:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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:0000256|ARBA:ARBA00043688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000256|ARBA:ARBA00043688};
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:0000256|ARBA:ARBA00043752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331;
CC Evidence={ECO:0000256|ARBA:ARBA00043752};
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:0000256|ARBA:ARBA00043716};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC Evidence={ECO:0000256|ARBA:ARBA00043716};
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:0000256|ARBA:ARBA00043661};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901;
CC Evidence={ECO:0000256|ARBA:ARBA00043661};
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:0000256|ARBA:ARBA00043714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC Evidence={ECO:0000256|ARBA:ARBA00043714};
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:0000256|ARBA:ARBA00043753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC Evidence={ECO:0000256|ARBA:ARBA00043753};
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:0000256|ARBA:ARBA00043686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000256|ARBA:ARBA00043686};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR AlphaFoldDB; H2NB45; -.
DR Ensembl; ENSPPYT00000003017.3; ENSPPYP00000002915.3; ENSPPYG00000002511.3.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263542; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; H2NB45; -.
DR OMA; PYSHCAF; -.
DR TreeFam; TF332859; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 223..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 517 AA; 58781 MW; E2434D8715FFFE7D CRC64;
MKGTKDLTSQ QKESNVKTFC SKNILAILGF SSIIAVIALL AVGLTQNKAL PENVKYGIVL
DAGSSHTSLY IYKWPAEKEN DTGVVHQVEE CRVKGPGISK YVQKVNEIGI YLTDCMERAR
EVIPRSQHQE TPVYLGATAG MRLLRMESEE LADRVLDVVE RNLSNYPFDF QGARIITGQE
EGAYGWITIN YLLGKFSQKT RWFSIVPYET NNQETFGALD LGGASTQITF VPQNQTIESP
DNALQFRLYG KDYNVYTHSF LCYGKDQALW QKLAKDIQVA SNEILRDPCF HPGYKKVVNV
SDLYKTPCTK RFEMTIPFQQ FEIQGIGNYQ QCHQSILELF NTSYCPYSQC AFNGIFLPPP
QGDFGAFSAF YFVMKFLNLT SEKVSQEKVT EMMKKFCSQP WEEIKTSYAG VKEKYLSEYC
FSGTYILSLL LQGYHFTADS WEHIHFIGKI QGSDAGWTLG YMLNLTNMIP AEQPLSTPLS
HSTYVFLMVL FSLVLFTVAI IGLLMFHKPS YFWKDMV
//