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Ectonucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) (NTPDase 8) (NTPDase8) (EC 3.6.1.5)

 ENTP8_MOUSE             Reviewed;         497 AA.
Q8K0L2; A2AJ99; Q6UQ22;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 3.
28-FEB-2018, entry version 105.
RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8;
Short=E-NTPDase 8;
Short=NTPDase 8;
Short=NTPDase8;
EC=3.6.1.5;
Name=Entpd8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=15122917; DOI=10.1021/bi0362222;
Bigonnesse F., Levesque S.A., Kukulski F., Lecka J., Robson S.C.,
Fernandes M.J., Sevigny J.;
"Cloning and characterization of mouse nucleoside triphosphate
diphosphohydrolase-8.";
Biochemistry 43:5511-5519(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Canalicular ectonucleoside NTPDase responsible for the
main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze
the hydrolysis of gamma- and beta-phosphate residues of
nucleotides, playing a central role in concentration of
extracellular nucleotides. Has activity toward ATP, ADP, UTP and
UDP, but not toward AMP. {ECO:0000269|PubMed:15122917}.
-!- CATALYTIC ACTIVITY: A nucleoside 5'-triphosphate + 2 H(2)O = a
nucleoside 5'-phosphate + 2 phosphate.
{ECO:0000269|PubMed:15122917}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15122917};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15122917};
Note=Ca(2+) or Mg(2+). Has lower efficiency with Mg(2+).
{ECO:0000269|PubMed:15122917};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13 uM for ATP {ECO:0000269|PubMed:15122917};
KM=41 uM for ADP {ECO:0000269|PubMed:15122917};
KM=47 uM for UTP {ECO:0000269|PubMed:15122917};
KM=171 uM for UDP {ECO:0000269|PubMed:15122917};
pH dependence:
Optimum pH is 5.5-8.0. {ECO:0000269|PubMed:15122917};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8K0L2-1; Sequence=Displayed;
Name=2;
IsoId=Q8K0L2-2; Sequence=VSP_028560, VSP_028561;
-!- TISSUE SPECIFICITY: Expressed in liver, jejunum and kidney.
{ECO:0000269|PubMed:15122917}.
-!- DOMAIN: The transmembranous domains are involved in regulation of
enzyme activity. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY364442; AAQ84519.1; -; mRNA.
EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031143; AAH31143.2; -; mRNA.
CCDS; CCDS15748.1; -. [Q8K0L2-1]
RefSeq; NP_082369.1; NM_028093.1. [Q8K0L2-1]
RefSeq; XP_006498425.1; XM_006498362.3. [Q8K0L2-1]
UniGene; Mm.33403; -.
ProteinModelPortal; Q8K0L2; -.
SMR; Q8K0L2; -.
STRING; 10090.ENSMUSP00000040628; -.
iPTMnet; Q8K0L2; -.
PhosphoSitePlus; Q8K0L2; -.
PaxDb; Q8K0L2; -.
PRIDE; Q8K0L2; -.
Ensembl; ENSMUST00000044078; ENSMUSP00000040628; ENSMUSG00000036813. [Q8K0L2-1]
Ensembl; ENSMUST00000114376; ENSMUSP00000110017; ENSMUSG00000036813. [Q8K0L2-2]
Ensembl; ENSMUST00000114380; ENSMUSP00000110022; ENSMUSG00000036813. [Q8K0L2-1]
GeneID; 72090; -.
KEGG; mmu:72090; -.
UCSC; uc008iqf.1; mouse. [Q8K0L2-1]
CTD; 377841; -.
MGI; MGI:1919340; Entpd8.
eggNOG; KOG1386; Eukaryota.
eggNOG; COG5371; LUCA.
GeneTree; ENSGT00550000074435; -.
HOGENOM; HOG000059572; -.
HOVERGEN; HBG018982; -.
InParanoid; Q8K0L2; -.
KO; K01510; -.
OMA; HLRDSCA; -.
OrthoDB; EOG091G05FZ; -.
PhylomeDB; Q8K0L2; -.
TreeFam; TF332859; -.
BRENDA; 3.6.1.5; 3474.
Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
SABIO-RK; Q8K0L2; -.
ChiTaRS; Cant1; mouse.
PRO; PR:Q8K0L2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000036813; -.
CleanEx; MM_ENTPD8; -.
ExpressionAtlas; Q8K0L2; baseline and differential.
Genevisible; Q8K0L2; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:MGI.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:MGI.
GO; GO:0009133; P:nucleoside diphosphate biosynthetic process; IDA:MGI.
GO; GO:0009124; P:nucleoside monophosphate biosynthetic process; IDA:MGI.
InterPro; IPR000407; GDA1_CD39_NTPase.
PANTHER; PTHR11782; PTHR11782; 1.
Pfam; PF01150; GDA1_CD39; 1.
PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 497 Ectonucleoside triphosphate
diphosphohydrolase 8.
/FTId=PRO_0000306883.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 473 Extracellular. {ECO:0000255}.
TRANSMEM 474 494 Helical. {ECO:0000255}.
TOPO_DOM 495 497 Cytoplasmic. {ECO:0000255}.
ACT_SITE 168 168 Proton acceptor. {ECO:0000250}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 102 {ECO:0000250}.
DISULFID 245 294 {ECO:0000250}.
DISULFID 331 337 {ECO:0000250}.
DISULFID 383 405 {ECO:0000250}.
VAR_SEQ 263 265 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_028560.
VAR_SEQ 353 389 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_028561.
CONFLICT 437 437 D -> N (in Ref. 3; AAH31143).
{ECO:0000305}.
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


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