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Ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase 5) (EC 3.6.1.6) (CD39 antigen-like 4) (ER-UDPase) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (EC 3.6.1.42) (Nucleoside diphosphatase) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5)

 ENTP5_MOUSE             Reviewed;         427 AA.
Q9WUZ9; O70214; Q544J4; Q8BR23; Q8CD29;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 127.
RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 5;
Short=NTPDase 5;
EC=3.6.1.6;
AltName: Full=CD39 antigen-like 4;
AltName: Full=ER-UDPase;
AltName: Full=Guanosine-diphosphatase ENTPD5;
Short=GDPase ENTPD5;
EC=3.6.1.42;
AltName: Full=Nucleoside diphosphatase;
AltName: Full=Uridine-diphosphatase ENTPD5;
Short=UDPase ENTPD5;
Flags: Precursor;
Name=Entpd5; Synonyms=Cd39l4;
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].
TISSUE=Testis;
PubMed=9457681; DOI=10.1007/s003359900710;
Chadwick B.P., Williamson J., Sheer D., Frischauf A.-M.;
"cDNA cloning and chromosomal mapping of a mouse gene with homology to
NTPases.";
Mamm. Genome 9:162-164(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
GLYCOSYLATION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=10369669; DOI=10.1093/emboj/18.12.3282;
Trombetta E.S., Helenius A.;
"Glycoprotein reglucosylation and nucleotide sugar utilization in the
secretory pathway: identification of a nucleoside diphosphatase in the
endoplasmic reticulum.";
EMBO J. 18:3282-3292(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=10506756;
DOI=10.1002/(SICI)1098-2744(199910)26:2<130::AID-MC7>3.0.CO;2-N;
Recio J.A., Zambrano N., de La Pena L., Powers C., Siwarski D.,
Huppi K., Notario V.;
"cDNA isolation, expression, and chromosomal localization of the mouse
pcph proto-oncogene.";
Mol. Carcinog. 26:130-136(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone, Corpora quadrigemina, Head, Kidney, Testis, Thymus, and
Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
DISRUPTION PHENOTYPE.
PubMed=19176496; DOI=10.1354/vp.08-VP-0201-R-AM;
Read R., Hansen G., Kramer J., Finch R., Li L., Vogel P.;
"Ectonucleoside triphosphate diphosphohydrolase type 5 (Entpd5)-
deficient mice develop progressive hepatopathy, hepatocellular tumors,
and spermatogenic arrest.";
Vet. Pathol. 46:491-504(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION,
INDUCTION, AND MUTAGENESIS OF GLU-171.
PubMed=21074248; DOI=10.1016/j.cell.2010.10.010;
Fang M., Shen Z., Huang S., Zhao L., Chen S., Mak T.W., Wang X.;
"The ER UDPase ENTPD5 promotes protein N-glycosylation, the Warburg
effect, and proliferation in the PTEN pathway.";
Cell 143:711-724(2010).
-!- FUNCTION: Uridine diphosphatase (UDPase) that promotes protein N-
glycosylation and ATP level regulation. UDP hydrolysis promotes
protein N-glycosylation and folding in the endoplasmic reticulum,
as well as elevated ATP consumption in the cytosol via an ATP
hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP
hydrolysis cycle that converts ATP to AMP and results in a
compensatory increase in aerobic glycolysis. The nucleotide
hydrolyzing preference is GDP > IDP > UDP, but not any other
nucleoside di-, mono- or triphosphates, nor thiamine
pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway
by promoting glycolysis in proliferating cells in response to
phosphoinositide 3-kinase (PI3K) signaling.
{ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}.
-!- CATALYTIC ACTIVITY: GDP + H(2)O = GMP + phosphate.
{ECO:0000269|PubMed:21074248}.
-!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a
nucleoside phosphate + phosphate. {ECO:0000269|PubMed:21074248}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10369669};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10369669};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7. {ECO:0000269|PubMed:10369669};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Exists both as a monomer and a disulfide-linked
homodimer, the dimers are enzymatically inactive. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}.
Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: Expressed in response to phosphoinositide 3-kinase
(PI3K) signaling. Activation of PI3K results in FOXO
phosphorylation by AKT1 and loss of ENTPD5 transcriptional
repression. Up-regulated in PTEN-deficient cells.
{ECO:0000269|PubMed:21074248}.
-!- PTM: N-glycosylated; high-mannose type.
{ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}.
-!- DISRUPTION PHENOTYPE: Mice display hepatopathy and aspermia. The
hepatopathy is progressive and characterized by centrilobular
hepatocyte hypertrophy, oval cell proliferation, bile staining of
Kupffer cells, and hepatocyte degeneration with increasing
incidence and severity of degenerative lesions, development of
multiple foci of cellular alteration, and hepatocellular neoplasia
with age. {ECO:0000269|PubMed:19176496}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF006482; AAC05181.1; -; mRNA.
EMBL; AJ238636; CAB45533.1; -; mRNA.
EMBL; AF136571; AAK82949.1; -; mRNA.
EMBL; AK002618; BAB22234.1; -; mRNA.
EMBL; AK031581; BAC27461.1; -; mRNA.
EMBL; AK036641; BAC29515.1; -; mRNA.
EMBL; AK037736; BAC29861.1; -; mRNA.
EMBL; AK045828; BAC32507.1; -; mRNA.
EMBL; AK079267; BAC37592.1; -; mRNA.
EMBL; AK080265; BAC37862.1; -; mRNA.
EMBL; AK081435; BAC38219.1; -; mRNA.
EMBL; AK088455; BAC40362.1; -; mRNA.
EMBL; AK160950; BAE36110.1; -; mRNA.
EMBL; CH466590; EDL02793.1; -; Genomic_DNA.
EMBL; CH466590; EDL02796.1; -; Genomic_DNA.
EMBL; CH466590; EDL02797.1; -; Genomic_DNA.
EMBL; BC015247; AAH15247.1; -; mRNA.
CCDS; CCDS26045.1; -.
RefSeq; NP_001021385.1; NM_001026214.2.
RefSeq; NP_001272978.1; NM_001286049.1.
RefSeq; NP_001272987.1; NM_001286058.1.
RefSeq; NP_031673.2; NM_007647.3.
UniGene; Mm.10211; -.
ProteinModelPortal; Q9WUZ9; -.
SMR; Q9WUZ9; -.
MINT; MINT-1863980; -.
STRING; 10090.ENSMUSP00000071939; -.
iPTMnet; Q9WUZ9; -.
PhosphoSitePlus; Q9WUZ9; -.
EPD; Q9WUZ9; -.
MaxQB; Q9WUZ9; -.
PaxDb; Q9WUZ9; -.
PRIDE; Q9WUZ9; -.
Ensembl; ENSMUST00000021662; ENSMUSP00000021662; ENSMUSG00000021236.
Ensembl; ENSMUST00000110272; ENSMUSP00000105901; ENSMUSG00000021236.
Ensembl; ENSMUST00000117286; ENSMUSP00000114011; ENSMUSG00000021236.
Ensembl; ENSMUST00000120942; ENSMUSP00000112516; ENSMUSG00000021236.
Ensembl; ENSMUST00000122194; ENSMUSP00000113106; ENSMUSG00000021236.
GeneID; 12499; -.
KEGG; mmu:12499; -.
UCSC; uc007ofd.2; mouse.
CTD; 957; -.
MGI; MGI:1321385; Entpd5.
eggNOG; KOG1385; Eukaryota.
eggNOG; COG5371; LUCA.
GeneTree; ENSGT00510000046675; -.
HOGENOM; HOG000220904; -.
HOVERGEN; HBG018208; -.
InParanoid; Q9WUZ9; -.
KO; K01511; -.
Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
UniPathway; UPA00378; -.
ChiTaRS; Entpd5; mouse.
PRO; PR:Q9WUZ9; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021236; -.
CleanEx; MM_ENTPD5; -.
ExpressionAtlas; Q9WUZ9; baseline and differential.
Genevisible; Q9WUZ9; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
GO; GO:0017110; F:nucleoside-diphosphatase activity; ISO:MGI.
GO; GO:0045134; F:uridine-diphosphatase activity; IDA:UniProtKB.
GO; GO:0051084; P:'de novo' posttranslational protein folding; IMP:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; IMP:UniProtKB.
GO; GO:0016049; P:cell growth; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; IMP:UniProtKB.
GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
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;
Calcium; Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Hydrolase; Magnesium; Reference proteome; Secreted;
Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 427 Ectonucleoside triphosphate
diphosphohydrolase 5.
/FTId=PRO_0000019910.
ACT_SITE 171 171 Proton acceptor. {ECO:0000305}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 271 302 {ECO:0000250}.
DISULFID 362 376 {ECO:0000250}.
MUTAGEN 171 171 E->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:21074248}.
CONFLICT 218 218 Q -> K (in Ref. 4; BAC27461).
{ECO:0000305}.
CONFLICT 390 390 F -> L (in Ref. 1; AAC05181).
{ECO:0000305}.
CONFLICT 394 427 DGTLLQLTKKVNNIETGWALGATFHLLQSLGITS -> ERH
PLTAHKESEQHRDWLGLGGHLSPAPVSGHHQLRPSSTSEAC
ISEPVFSQEGVDSETFSDLSGKAWPETR (in Ref. 1;
AAC05181). {ECO:0000305}.
SEQUENCE 427 AA; 47102 MW; 2F9DA2C342C55577 CRC64;
MATSWGAVFM LIIACVGSTV FYREQQTWFE GVFLSSMCPI NVSAGTFYGI MFDAGSTGTR
IHVYTFVQKT AGQLPFLEGE IFDSVKPGLS AFVDQPKQGA ETVQELLEVA KDSIPRSHWE
RTPVVLKATA GLRLLPEQKA QALLLEVEEI FKNSPFLVPD GSVSIMDGSY EGILAWVTVN
FLTGQLHGRG QETVGTLDLG GASTQITFLP QFEKTLEQTP RGYLTSFEMF NSTFKLYTHS
YLGFGLKAAR LATLGALEAK GTDGHTFRSA CLPRWLEAEW IFGGVKYQYG GNQEGEMGFE
PCYAEVLRVV QGKLHQPEEV RGSAFYAFSY YYDRAADTHL IDYEKGGVLK VEDFERKARE
VCDNLGSFSS GSPFLCMDLT YITALLKDGF GFADGTLLQL TKKVNNIETG WALGATFHLL
QSLGITS


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