ENTP7_XENTR
ID ENTP7_XENTR Reviewed; 610 AA.
AC Q28CF8; Q2QDC5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 7;
DE Short=NTPDase 7;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9NQZ7};
GN Name=entpd7; ORFNames=TGas060f02.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-595.
RX PubMed=16380227; DOI=10.1016/j.ygeno.2005.11.003;
RA Masse K., Eason R., Bhamra S., Dale N., Jones E.;
RT "Comparative genomic and expression analysis of the conserved NTPDase gene
RT family in Xenopus.";
RL Genomics 87:366-381(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates and
CC diphosphates in a calcium- or magnesium-dependent manner.
CC Preferentially hydrolyzes nucleoside 5'-triphosphates, with substrate
CC preference for UTP > GTP > CTP. Hydrolyzes ATP and nucleoside
CC diphosphates only to a minor extent. {ECO:0000250|UniProtKB:Q9NQZ7}.
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; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
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:Q9NQZ7};
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:Q9NQZ7};
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:Q9NQZ7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9NQZ7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; CR926412; CAJ81622.1; -; mRNA.
DR EMBL; DQ118412; ABA00734.1; -; mRNA.
DR RefSeq; NP_001015918.1; NM_001015918.2.
DR RefSeq; XP_012822005.1; XM_012966551.2.
DR AlphaFoldDB; Q28CF8; -.
DR SMR; Q28CF8; -.
DR STRING; 8364.ENSXETP00000008111; -.
DR PaxDb; Q28CF8; -.
DR GeneID; 548672; -.
DR KEGG; xtr:548672; -.
DR CTD; 57089; -.
DR Xenbase; XB-GENE-973424; entpd7.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; Q28CF8; -.
DR OrthoDB; 1337265at2759; -.
DR Reactome; R-XTR-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003746; Expressed in embryo and 14 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043273; F:CTPase activity; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0006254; P:CTP catabolic process; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; ISS:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
DR GO; GO:0046052; P:UTP catabolic process; ISS:UniProtKB.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..610
FT /note="Ectonucleoside triphosphate diphosphohydrolase 7"
FT /id="PRO_0000274422"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..555
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 454..483
FT /evidence="ECO:0000250"
FT CONFLICT 367
FT /note="I -> T (in Ref. 2; ABA00734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 69915 MW; F0CE835509566376 CRC64;
MARISFSCLF PASWHCSLPS VTQFSRQRVA LLIISVAVFI LVFAAVADLQ LWSSRAFRDR
QFRRYLDQIE DLEATDTKDT KLNYGVVVDC GSSGSRVFVY FWPPHNGNPH DLLDIKQMRD
RGSKPVVKKI KPGISTMALT PEKSSDYINP LLSFAASYIP KHKHKETPLY ILCTAGMRIL
PESQQIAILQ DLVKDVPQEF DFLFSEAHAE VISGKQEGVY AWISINFVLG RFDHVVDEED
AVVAVTIGTQ EESIIRKRTV GVIDMGGGSL QIAYEVPTTM TYPSVEHEEV AKSMLAEFNL
GCDLQHTEHV YRVYVTTFMG FGGNFARQRY EDMVFNDTIT KNRIQGQQIG VHPNSPLQDP
CLPVGLIDQV RRQSHDLHVL GKGNWDSCRQ QLEPLLLKSN DTQAYLNSVY QPSIDFSNSE
FYGFSEFFYC TEDVLRMGGI YNSQKFAKAA KEYCSMPWTT LQDRFNSGLY SSHADQHRLK
YQCFKSAWMF SILHNGFHFP HEYPNFKTAQ LVYDKEVQWT LGAILYKTRF LPLRDIRQES
SRPAHVSWFR ISFVYNHYLF FACILVVLLS IVLYILRLRR IHRRQARASA LDLLLMEEGV
HTVLEPGIPT
