ID Q6GP74_XENLA Unreviewed; 508 AA.
AC Q6GP74;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 74.
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.L {ECO:0000313|RefSeq:NP_001085737.1,
GN ECO:0000313|Xenbase:XB-GENE-945089};
GN Synonyms=entpd1 {ECO:0000313|RefSeq:NP_001085737.1,
GN ECO:0000313|Xenbase:XB-GENE-945089}, entpd1.S
GN {ECO:0000313|RefSeq:NP_001085737.1}, MGC80631
GN {ECO:0000313|EMBL:AAH73267.1}, NTPDase1
GN {ECO:0000313|RefSeq:NP_001085737.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH73267.1};
RN [1] {ECO:0000313|RefSeq:NP_001085737.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH73267.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000313|EMBL:AAH73267.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001085737.1}
RP IDENTIFICATION.
RG RefSeq;
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=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 -!- 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 EMBL; BC073267; AAH73267.1; -; mRNA.
DR RefSeq; NP_001085737.1; NM_001092268.1.
DR DNASU; 444164; -.
DR GeneID; 444164; -.
DR KEGG; xla:444164; -.
DR AGR; Xenbase:XB-GENE-945089; -.
DR CTD; 444164; -.
DR Xenbase; XB-GENE-945089; entpd1.L.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 444164; Expressed in pancreas and 16 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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:UP000186698};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 215..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 508 AA; 57050 MW; BD205818A06C523B CRC64;
MDEPKAAKQK RTCNKKVIFL LGALFPLGVI ALVTIAVVQN KPLPKNIKYG IVLDAGSSHT
SVYIYEWPSE KENDTGVVQQ INDCKVEGNG ISSYGHEPTK AGLSLQKCMN KARQVIPEMQ
QKETPVYLGA TAGMRLLRLN NATMAEEVLS SVENMLRSFP FDFQGARIIT GQEEGAYGWI
TINYLLGNFI QDSGWFKYMP NFKPTGTSGA LDLGGASTQI TFESKKEIES QENSLHFRLY
GKSYDVYTHS FLCYGKDQAL RLQIANSVPT ATDSILMDPC FNSGYRRNTS TSDLYSSPCI
SNLRISTAPS FLDVKGTGNY QLCKRNVEAI FDRTRCTYSH CSFNGIFQPT LDGTFGAFSA
YYFVMDFLKL TKGEISLDKV KETVERHCSK PWDEVKKEFP KIKEKYLSEY CFSGTYILTL
LEFGYGFNSE NWNDIRFLGK IKDSDAGWTL GYMLNLTNMI PAELPYSPPL SHATYTGLMA
AFSILLVCII LICWLTFRKP KCLHKGII
//
