ENTP8_RAT
ID ENTP8_RAT Reviewed; 494 AA.
AC Q5DRK1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=17095758; DOI=10.1152/ajpgi.00293.2006;
RA Fausther M., Lecka J., Kukulski F., Levesque S.A., Pelletier J.,
RA Zimmermann H., Dranoff J.A., Sevigny J.;
RT "Cloning, purification, and identification of the liver canalicular ecto-
RT ATPase as NTPDase8.";
RL Am. J. Physiol. 292:G785-G795(2007).
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:0000269|PubMed:17095758};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17095758}.
CC -!- TISSUE SPECIFICITY: Present in liver, and at lower level in jejunum and
CC kidney. Limited to the canalicular domain of hepatocytes (at protein
CC level). {ECO:0000269|PubMed:17095758}.
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; AY536920; AAT08794.1; -; mRNA.
DR RefSeq; NP_001028737.1; NM_001033565.1.
DR AlphaFoldDB; Q5DRK1; -.
DR SMR; Q5DRK1; -.
DR STRING; 10116.ENSRNOP00000012289; -.
DR ChEMBL; CHEMBL4295846; -.
DR GlyGen; Q5DRK1; 3 sites.
DR PaxDb; Q5DRK1; -.
DR GeneID; 613267; -.
DR KEGG; rno:613267; -.
DR UCSC; RGD:1561793; rat.
DR CTD; 377841; -.
DR RGD; 1561793; Entpd8.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; Q5DRK1; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q5DRK1; -.
DR BRENDA; 3.6.1.5; 5301.
DR BRENDA; 3.6.1.6; 5301.
DR Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; Q5DRK1; -.
DR PRO; PR:Q5DRK1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:RGD.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009133; P:nucleoside diphosphate biosynthetic process; ISO:RGD.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0009124; P:nucleoside monophosphate biosynthetic process; ISO:RGD.
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 1: Evidence at protein 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..494
FT /note="Ectonucleoside triphosphate diphosphohydrolase 8"
FT /id="PRO_0000306884"
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..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..102
FT /evidence="ECO:0000250"
FT DISULFID 245..291
FT /evidence="ECO:0000250"
FT DISULFID 328..334
FT /evidence="ECO:0000250"
FT DISULFID 380..402
FT /evidence="ECO:0000250"
SQ SEQUENCE 494 AA; 54330 MW; 1261896D24D06458 CRC64;
MRLSWKERVF MVLLGVAAAS GLTMLILILV KATNVLLPAD TKFGILFDAG SSHTSLFVYQ
WPANKEKDTG VVSQALACQV EGPGISSYTS DPTQAGESLK SCLQEALALI PQTQHPVTPA
FLGATAGMRL LSQKNSSQAQ DILAAVSQTL SRAPVDFWGA RILAGQDEGA FGWITVNYVL
GMLLKYSSGQ WILPEDGTLV GALDLGGAST QISFVPQGPI LDQSTQVTFR LYGANYSVYT
HSYLCFGRDQ ILRRLLAELV QSSQVARVRH PCYHSGYQAT LSLASLYDSP CVHTPDSLNY
TQNLTVEGIG NPGNCVAALR GLFNFSSCKG QEDCAFNGVY QPPVHGQFYA FSNFYYTFQF
LNLTSRQPLN IVNDTIWKFC QKPWRLVEDS YPGQERWLRD YCASGLYILV LLLEGYKFSE
ETWPNIQFQK QAGGTDIGWT LGFMLNLTGM IPAEALTQWR AQSYSIWIAG VVFAVLTLVA
ILGAAAVQLF WTQD
