ID M3WJX1_FELCA Unreviewed; 510 AA.
AC M3WJX1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 66.
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:ENSFCAP00000012994.6,
GN ECO:0000313|VGNC:VGNC:97418};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000012994.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000012994.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012994.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000012994.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012994.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000012994.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012994.6};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04000273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006938097.1; XM_006938035.3.
DR AlphaFoldDB; M3WJX1; -.
DR STRING; 9685.ENSFCAP00000012994; -.
DR PaxDb; 9685-ENSFCAP00000012994; -.
DR Ensembl; ENSFCAT00000014016.6; ENSFCAP00000012994.6; ENSFCAG00000014012.6.
DR GeneID; 101096356; -.
DR KEGG; fca:101096356; -.
DR CTD; 953; -.
DR VGNC; VGNC:97418; ENTPD1.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263542; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; M3WJX1; -.
DR OMA; PYSHCAF; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000014012; Expressed in testis and 11 other cell types or tissues.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
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; IEA:Ensembl.
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:UP000011712};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..499
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 216..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 510 AA; 57794 MW; 5B942B981808DA58 CRC64;
MEDRKESELK SFCSRNILII LGFSSIMAVI ALIAVGLTQN KPLPENVKYG IVLDAGSSHT
SLYIYKWPAE KENDTGVVHQ IEECKLKGPG ISRYAQRLNE IDAYLTECME RASQVIPKSQ
HQGTPVYLGA TAGMRLLRME NEHLADKVLS MVTKSLNNYH FDFHGARIIT GQEEGAYGWI
TINYLLGKFT QKLSWLNLKP NGGNSQGTYG ALDLGGASTQ ITFVPQNERI ESPSNALHFR
LYGKDYSVYT HSFLCYGKDQ ALRQKLAKDI QGTNGILRDP CFHPGYEIVM NVSELYSGPC
TKRFEMTLPF DEFLIQGTGN YQQCHESILE LFNTSYCPYS HCSFNGIFLP PLHGDFGAFS
AYYYVMEFLN FTSEETPTQE KVIDSMEKFC SQPWNELKTY FGDVKEKYLS EYCFSGAYIL
SLLLNGYHFT ADSWKNIHFM GKIHSSSVGW TLGYMLNLTN MIPAEEPLST PLSHSTYVFL
MVLFSLILVA VAIIGLFIFH KPSYFWKDMV
//
