ENTP1_MOUSE
ID ENTP1_MOUSE Reviewed; 510 AA.
AC P55772;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1;
DE Short=NTPDase 1;
DE EC=3.6.1.5;
DE AltName: Full=Ecto-ATP diphosphohydrolase 1;
DE Short=Ecto-ATPDase 1;
DE Short=Ecto-ATPase 1;
DE AltName: Full=Ecto-apyrase;
DE AltName: Full=Lymphoid cell activation antigen;
DE AltName: CD_antigen=CD39;
GN Name=Entpd1; Synonyms=Cd39;
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].
RX PubMed=7930580;
RA Maliszewski C.R., Delespesse G.J.T., Schoenborn M.A., Armitage R.J.,
RA Fanslow W.C., Nakajima T., Baker E., Sutherland G.R., Poindexter K.,
RA Birks C., Alpert A., Friend D., Gimpel S.D., Gayle R.B. III;
RT "The CD39 lymphoid cell activation antigen. Molecular cloning and
RT structural characterization.";
RL J. Immunol. 153:3574-3583(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9730622; DOI=10.1159/000015049;
RA Schoenborn M.A., Jenkins N.A., Copeland N.G., Gilbert D.J., Gayle R.B. III,
RA Maliszewski C.R.;
RT "Gene structure and chromosome location of mouse Cd39 coding for an ecto-
RT apyrase.";
RL Cytogenet. Cell Genet. 81:287-289(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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. Could also be
CC implicated in the prevention of platelet aggregation by hydrolyzing
CC platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF037366; AAB92259.1; -; mRNA.
DR EMBL; AF041818; AAC83203.1; -; Genomic_DNA.
DR EMBL; AF041812; AAC83203.1; JOINED; Genomic_DNA.
DR EMBL; AF041813; AAC83203.1; JOINED; Genomic_DNA.
DR EMBL; AF041814; AAC83203.1; JOINED; Genomic_DNA.
DR EMBL; AF041815; AAC83203.1; JOINED; Genomic_DNA.
DR EMBL; AF041816; AAC83203.1; JOINED; Genomic_DNA.
DR EMBL; AF041817; AAC83203.1; JOINED; Genomic_DNA.
DR CCDS; CCDS50434.1; -.
DR RefSeq; NP_033978.1; NM_009848.4.
DR AlphaFoldDB; P55772; -.
DR SMR; P55772; -.
DR STRING; 10090.ENSMUSP00000107850; -.
DR BindingDB; P55772; -.
DR ChEMBL; CHEMBL4739681; -.
DR GlyGen; P55772; 6 sites.
DR iPTMnet; P55772; -.
DR PhosphoSitePlus; P55772; -.
DR EPD; P55772; -.
DR jPOST; P55772; -.
DR PaxDb; P55772; -.
DR PRIDE; P55772; -.
DR ProteomicsDB; 275457; -.
DR Antibodypedia; 2888; 907 antibodies from 43 providers.
DR DNASU; 12495; -.
DR Ensembl; ENSMUST00000112231; ENSMUSP00000107850; ENSMUSG00000048120.
DR GeneID; 12495; -.
DR KEGG; mmu:12495; -.
DR UCSC; uc008hlf.2; mouse.
DR CTD; 953; -.
DR MGI; MGI:102805; Entpd1.
DR VEuPathDB; HostDB:ENSMUSG00000048120; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; P55772; -.
DR OMA; YPFNFQG; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; P55772; -.
DR TreeFam; TF332859; -.
DR BRENDA; 3.6.1.5; 3474.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; P55772; -.
DR BioGRID-ORCS; 12495; 1 hit in 60 CRISPR screens.
DR ChiTaRS; Entpd1; mouse.
DR PRO; PR:P55772; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P55772; protein.
DR Bgee; ENSMUSG00000048120; Expressed in ectoplacental cone and 185 other tissues.
DR ExpressionAtlas; P55772; baseline and differential.
DR Genevisible; P55772; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
DR GO; GO:0005615; C:extracellular space; 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:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IMP:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
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: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:0046032; P:ADP catabolic process; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; ISO: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 ATP-binding; Calcium; Disulfide bond; Glycoprotein; Hydrolase; Magnesium;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..510
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT /id="PRO_0000209903"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..108
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 254..300
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 281..324
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 337..342
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 391..414
FT /evidence="ECO:0000250|UniProtKB:P97687"
SQ SEQUENCE 510 AA; 57205 MW; 8E6A6113D2E13930 CRC64;
MEDIKDSKVK RFCSKNILII LGFTSILAVI ALIAVGLTQN KPLPENVKYG IVLDAGSSHT
NLYIYKWPAE KENDTGVVQQ LEECQVKGPG ISKYAQKTDE IGAYLAECME LSTELIPTSK
HHQTPVYLGA TAGMRLLRME SEQSADEVLA AVSTSLKSYP FDFQGAKIIT GQEEGAYGWI
TINYLLGRFT QEQSWLSLIS DSQKQETFGA LDLGGASTQI TFVPQNSTIE SPENSLQFRL
YGEDYTVYTH SFLCYGKDQA LWQKLAKDIQ VSSGGVLKDP CFNPGYEKVV NVSELYGTPC
TKRFEKKLPF DQFRIQGTGD YEQCHQSILE LFNNSHCPYS QCAFNGVFLP PLHGSFGAFS
AFYFVMDFFK KVAKNSVISQ EKMTEITKNF CSKSWEETKT SYPSVKEKYL SEYCFSGAYI
LSLLQGYNFT DSSWEQIHFM GKIKDSNAGW TLGYMLNLTN MIPAEQPLSP PLPHSTYIGL
MVLFSLLLVA VAITGLFIYS KPSYFWKEAV
