ENTP8_MOUSE
ID ENTP8_MOUSE Reviewed; 497 AA.
AC Q8K0L2; A2AJ99; Q6UQ22;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=15122917; DOI=10.1021/bi0362222;
RA Bigonnesse F., Levesque S.A., Kukulski F., Lecka J., Robson S.C.,
RA Fernandes M.J., Sevigny J.;
RT "Cloning and characterization of mouse nucleoside triphosphate
RT diphosphohydrolase-8.";
RL Biochemistry 43:5511-5519(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC {ECO:0000269|PubMed:15122917}.
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:0000269|PubMed:15122917};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15122917};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15122917};
CC Note=Ca(2+) or Mg(2+). Has lower efficiency with Mg(2+).
CC {ECO:0000269|PubMed:15122917};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for ATP {ECO:0000269|PubMed:15122917};
CC KM=41 uM for ADP {ECO:0000269|PubMed:15122917};
CC KM=47 uM for UTP {ECO:0000269|PubMed:15122917};
CC KM=171 uM for UDP {ECO:0000269|PubMed:15122917};
CC pH dependence:
CC Optimum pH is 5.5-8.0. {ECO:0000269|PubMed:15122917};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K0L2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K0L2-2; Sequence=VSP_028560, VSP_028561;
CC -!- TISSUE SPECIFICITY: Expressed in liver, jejunum and kidney.
CC {ECO:0000269|PubMed:15122917}.
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; AY364442; AAQ84519.1; -; mRNA.
DR EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031143; AAH31143.2; -; mRNA.
DR CCDS; CCDS15748.1; -. [Q8K0L2-1]
DR RefSeq; NP_082369.1; NM_028093.1. [Q8K0L2-1]
DR RefSeq; XP_006498425.1; XM_006498362.3.
DR AlphaFoldDB; Q8K0L2; -.
DR SMR; Q8K0L2; -.
DR STRING; 10090.ENSMUSP00000110022; -.
DR GlyGen; Q8K0L2; 2 sites.
DR iPTMnet; Q8K0L2; -.
DR PhosphoSitePlus; Q8K0L2; -.
DR jPOST; Q8K0L2; -.
DR MaxQB; Q8K0L2; -.
DR PaxDb; Q8K0L2; -.
DR PRIDE; Q8K0L2; -.
DR ProteomicsDB; 275921; -. [Q8K0L2-1]
DR ProteomicsDB; 275922; -. [Q8K0L2-2]
DR Antibodypedia; 19016; 158 antibodies from 20 providers.
DR Ensembl; ENSMUST00000044078; ENSMUSP00000040628; ENSMUSG00000036813. [Q8K0L2-1]
DR Ensembl; ENSMUST00000114376; ENSMUSP00000110017; ENSMUSG00000036813. [Q8K0L2-2]
DR Ensembl; ENSMUST00000114380; ENSMUSP00000110022; ENSMUSG00000036813. [Q8K0L2-1]
DR GeneID; 72090; -.
DR KEGG; mmu:72090; -.
DR UCSC; uc008iqf.1; mouse. [Q8K0L2-1]
DR CTD; 377841; -.
DR MGI; MGI:1919340; Entpd8.
DR VEuPathDB; HostDB:ENSMUSG00000036813; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; Q8K0L2; -.
DR OMA; CLQTEPG; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q8K0L2; -.
DR TreeFam; TF332859; -.
DR BRENDA; 3.6.1.5; 3474.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; Q8K0L2; -.
DR BioGRID-ORCS; 72090; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Cant1; mouse.
DR PRO; PR:Q8K0L2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K0L2; protein.
DR Bgee; ENSMUSG00000036813; Expressed in small intestine Peyer's patch and 35 other tissues.
DR ExpressionAtlas; Q8K0L2; baseline and differential.
DR Genevisible; Q8K0L2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:MGI.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009133; P:nucleoside diphosphate biosynthetic process; IDA:MGI.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0009124; P:nucleoside monophosphate biosynthetic process; IDA:MGI.
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 Alternative splicing; ATP-binding; Calcium; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..497
FT /note="Ectonucleoside triphosphate diphosphohydrolase 8"
FT /id="PRO_0000306883"
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..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..102
FT /evidence="ECO:0000250"
FT DISULFID 245..294
FT /evidence="ECO:0000250"
FT DISULFID 331..337
FT /evidence="ECO:0000250"
FT DISULFID 383..405
FT /evidence="ECO:0000250"
FT VAR_SEQ 263..265
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028560"
FT VAR_SEQ 353..389
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028561"
FT CONFLICT 437
FT /note="D -> N (in Ref. 3; AAH31143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54650 MW; 00DE822B6EEB1BDF CRC64;
MGLSWKERVF MALLGVAAAS GLTMLVLILV KAINVLLPAD TKFGIVFDAG SSHTSLFVYQ
WPANKEKDTG VVSQALTCQI EGPGISSYTS DPTQAGESLK SCLEEALALI PQAQHPETPT
FLGSTAGMRL LSQKNSSQAR DILAAVSQTL SKSPVDFWGA KILAGQDEGA FGWITINYVL
GMLLKYSSGQ WILPEEGMLV GALDLGGAST QISFVPQGPI LDQSTQVTFR LYGANYSVYT
HSYLCFGRDQ ILNRLLAKLA QDRLSSQVAP VRHPCYHSGY QAILPLSSLY DSPCIHTTDS
LNHTQNLTVE GTGDPGNCVV ALRSLFNFSS CKGQKDCAFN GIYQPPVHGQ FYAFSNFYYT
FHFLNLTSRQ SLNTVNDTVW KFCQKPWKLV EVSYPGQERW LRDYCASGLY ILVLLLEGYK
FSEETWPNIQ FQKQAGDTDI GWTLGFMLNL TGMIPAEAPT HWRAQSYSIW TAGVVFAVLT
LVAILGAAAI QIFWTQD
