ENTP2_MOUSE
ID ENTP2_MOUSE Reviewed; 495 AA.
AC O55026; O35928; Q9DCR9;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 2;
DE Short=NTPDase 2;
DE EC=3.6.1.-;
DE AltName: Full=CD39 antigen-like 1;
DE AltName: Full=Ecto-ATP diphosphohydrolase 2;
DE Short=Ecto-ATPDase 2;
DE Short=Ecto-ATPase 2;
GN Name=Entpd2; Synonyms=Cd39l1;
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 SHORT).
RC TISSUE=Embryo;
RX PubMed=9271669; DOI=10.1007/s003359900534;
RA Chadwick B.P., Frischauf A.-M.;
RT "Cloning and mapping of a human and mouse gene with homology to ecto-ATPase
RT genes.";
RL Mamm. Genome 8:668-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Hepatoma;
RX PubMed=9624117; DOI=10.1074/jbc.273.25.15358;
RA Gao L., Dong L., Whitlock J.P. Jr.;
RT "A novel response to dioxin. Induction of ecto-ATPase gene expression.";
RL J. Biol. Chem. 273:15358-15365(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=CD-1; TISSUE=Heart;
RA Lavoie E.G., Lecka J., Sevigny J.;
RT "Cloning of mouse heart nucleoside triphosphate diphosphohydrolase-2.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-129.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: In the nervous system, could hydrolyze ATP and other
CC nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP
CC only to a marginal extent (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O55026-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O55026-2; Sequence=VSP_003611, VSP_003612;
CC -!- INDUCTION: By dioxin.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; U91511; AAB81014.1; -; mRNA.
DR EMBL; AF042811; AAC24347.1; -; mRNA.
DR EMBL; AY376711; AAQ86586.1; -; mRNA.
DR EMBL; AK002553; BAB22182.1; -; mRNA.
DR CCDS; CCDS15770.1; -. [O55026-1]
DR RefSeq; NP_033979.2; NM_009849.2. [O55026-1]
DR AlphaFoldDB; O55026; -.
DR SMR; O55026; -.
DR BioGRID; 198592; 1.
DR IntAct; O55026; 1.
DR MINT; O55026; -.
DR STRING; 10090.ENSMUSP00000028328; -.
DR GlyConnect; 2273; 13 N-Linked glycans (3 sites).
DR GlyGen; O55026; 6 sites, 13 N-linked glycans (3 sites).
DR iPTMnet; O55026; -.
DR PhosphoSitePlus; O55026; -.
DR MaxQB; O55026; -.
DR PaxDb; O55026; -.
DR PeptideAtlas; O55026; -.
DR PRIDE; O55026; -.
DR ProteomicsDB; 275917; -. [O55026-1]
DR ProteomicsDB; 275918; -. [O55026-2]
DR Antibodypedia; 2981; 220 antibodies from 32 providers.
DR DNASU; 12496; -.
DR Ensembl; ENSMUST00000028328; ENSMUSP00000028328; ENSMUSG00000015085. [O55026-1]
DR GeneID; 12496; -.
DR KEGG; mmu:12496; -.
DR UCSC; uc008irw.2; mouse. [O55026-1]
DR CTD; 954; -.
DR MGI; MGI:1096863; Entpd2.
DR VEuPathDB; HostDB:ENSMUSG00000015085; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; O55026; -.
DR OMA; QTWAELQ; -.
DR PhylomeDB; O55026; -.
DR TreeFam; TF332859; -.
DR BRENDA; 3.6.1.5; 3474.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; O55026; -.
DR BioGRID-ORCS; 12496; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Entpd2; mouse.
DR PRO; PR:O55026; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O55026; protein.
DR Bgee; ENSMUSG00000015085; Expressed in seminal vesicle and 198 other tissues.
DR ExpressionAtlas; O55026; baseline and differential.
DR Genevisible; O55026; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0031253; C:cell projection membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IDA:MGI.
DR GO; GO:0009181; P:purine ribonucleoside diphosphate catabolic 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; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="Ectonucleoside triphosphate diphosphohydrolase 2"
FT /id="PRO_0000209907"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..462
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT BINDING 204..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..99
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 242..284
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 265..310
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 323..328
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 377..399
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT VAR_SEQ 130..132
FT /note="LTS -> MAG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9271669"
FT /id="VSP_003611"
FT VAR_SEQ 133..495
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9271669"
FT /id="VSP_003612"
FT CONFLICT 400
FT /note="A -> T (in Ref. 2; AAC24347)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="R -> S (in Ref. 2; AAC24347)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> T (in Ref. 2; AAC24347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 54319 MW; A76468A0CBF86AAC CRC64;
MAGKLVSLVP PLLLAAVGLA GLLLLCVPTQ DVREPPALKY GIVLDAGSSH TSMFVYKWPA
DKENDTGIVG QHSSCDVRGG GISSYANDPS RAGQSLVECL EQALRDVPKD RYASTPLYLG
ATAGMRLLNL TSPEATAKVL EAVTQTLTRY PFDFRGARIL SGQDEGVFGW VTANYLLENF
IKYGWVGRWI RPRKGTLGAM DLGGASTQIT FETTSPSEDP DNEVHLRLYG QHYRVYTHSF
LCYGRDQVLQ RLLASALQIH RFHPCWPKGY STQVLLREVY QSPCTMGQRP QTFNSSATVS
LSGTSNAALC RDLVSGLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY TVDFLKTVMG
LPVGTLKQLE DATETTCNQT WAELQARVPG QQTRLPDYCA VAMFIHQLLS RGYRFDERSF
RGVVFEKKAA DTAVGWALGY MLNLTNLIPA DLPGLRKGTH FSSWVALLLL FTVLILAALV
LLLRQVRSAK SPGAL
