ENTP7_PONAB
ID ENTP7_PONAB Reviewed; 604 AA.
AC Q5REF6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 7;
DE Short=NTPDase 7;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9NQZ7};
GN Name=ENTPD7;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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; CR857573; CAH89851.1; -; mRNA.
DR RefSeq; NP_001128973.1; NM_001135501.1.
DR AlphaFoldDB; Q5REF6; -.
DR SMR; Q5REF6; -.
DR STRING; 9601.ENSPPYP00000002967; -.
DR GeneID; 100190813; -.
DR KEGG; pon:100190813; -.
DR CTD; 57089; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; Q5REF6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043273; F:CTPase activity; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
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:0046052; P:UTP catabolic process; ISS:UniProtKB.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 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..604
FT /note="Ectonucleoside triphosphate diphosphohydrolase 7"
FT /id="PRO_0000274421"
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..546
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 448..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 604 AA; 68953 MW; 357B81FB02AED50F CRC64;
MARISFSYLC PASWYFTVPT VSPFLRQRVA FLGLFFISCL LLLMLIIDFR HWSASLPRDR
QYERYLARVG ELEATDTEDP NLNYGLVVDC GSSGSRIFVY FWPRHNGNPH DLLDIKQMRD
RNSQPVVKKI KPGISAMADT PEHASDYLRP LLSFAAAHVP VKKHKETPLY ILCTAGMRLL
PERKQLAILA DLVKDLPLEF DFLFSQSQAE VISGKQEGVY AWIGINFVLG RFDHEDESDA
EATQELAAGR RRTVGILDMG GASLQIAYEV PTSTSVLPAK QEEAAKILLA EFNLGCDVQH
TEHVYRVYVT TFLGFGGNFA RQRYEDLVLN ETLNKNRLLG QKTGLSPDNP FLDPCLPVGL
TDVVERNSQV LHVRGRGDWV SCRAMLSPLL ARSNTSQASL NGIYQSPIDF NNSEFYGFSE
FFYCTEDVLR IGGRYHGPTF AKAAQDYCGM AWSVLTQRFK NGLFSSHADE HRLKYQCFKS
AWMYQVLHEG FHFPYDYPNL RTAQLVYGRE VQWTLGAILY KTRFLPLRDL RQEGVRQAHG
SWFRLSFVYN HYLFFACILV VLLAIVLYLL RLRRIHHRQT RASAPLDLLW LEEVVPMMGV
QVGP
