ENTP8_BOVIN
ID ENTP8_BOVIN Reviewed; 495 AA.
AC A0JND9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8;
DE Short=E-NTPDase 8;
DE Short=NTPDase 8;
DE Short=NTPDase8;
DE EC=3.6.1.5;
GN Name=ENTPD8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Canalicular ectonucleoside NTPDase responsible for the main
CC hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the
CC hydrolysis of gamma- and beta-phosphate residues of nucleotides,
CC playing a central role in concentration of extracellular nucleotides.
CC Has activity toward ATP, ADP, UTP and UDP, but not toward AMP (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Ca(2+) or Mg(2+). Has lower efficiency with Mg(2+). {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The transmembranous domains are involved in regulation of
CC enzyme activity. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; BC126637; AAI26638.1; -; mRNA.
DR RefSeq; NP_001071395.1; NM_001077927.2.
DR AlphaFoldDB; A0JND9; -.
DR SMR; A0JND9; -.
DR STRING; 9913.ENSBTAP00000016080; -.
DR PaxDb; A0JND9; -.
DR GeneID; 515532; -.
DR KEGG; bta:515532; -.
DR CTD; 377841; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; A0JND9; -.
DR OrthoDB; 1337265at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
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:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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 ATP-binding; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="Ectonucleoside triphosphate diphosphohydrolase 8"
FT /id="PRO_0000306881"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..102
FT /evidence="ECO:0000250"
FT DISULFID 246..292
FT /evidence="ECO:0000250"
FT DISULFID 328..334
FT /evidence="ECO:0000250"
FT DISULFID 380..403
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 53240 MW; 99082624BE7045F7 CRC64;
MGLTWKQRVF TALLGAAAVS GLTALLLVLV GTMNVLLPPD TKFGIVFDAG SSHTSLFVYQ
WPANKENDTG IVSQALACQA EGPGISSYAS NPARVGESLQ GCLEEALALI PKAKHHETPM
FLGATAGMRL LSRKNRSQAE DVFAAVSRAL GQSPVDFRGA ELLTGQDEGA FGWITINYIL
GLLVKYSFSG EWIRPLEETL VGALDMGGAS TQITFVPGGP ILDKTAQATF RLYGADHTVY
THSYLCFGRD QALSRVLAEL VQASTGLLIR HPCYHSGYRG TLALASLYES PCAPAAPPDL
SQNLTVEGTG NPGACVEALR KLFNFSSCDG REDCAFAGVY QPPVQGQFYA FSNFYYTFNF
LNLTSKPSLS GANATIWEFC LRPWKLVEAS APPGQDRWLR DYCASGLYIL TLLVEGYGFS
EETWGGIEFR QQAGGADIGW TLGYMLNLTN LIPAEAPAQG WAQSFGVWAA GVVFVVLTLA
ATLGAVAVQV FWLQD
