ENTP3_MOUSE
ID ENTP3_MOUSE Reviewed; 529 AA.
AC Q8BFW6; E9PYV0; Q3TC04; Q3TDX3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 3 {ECO:0000303|PubMed:15130768};
DE Short=NTPDase 3 {ECO:0000303|Ref.2};
DE EC=3.6.1.5 {ECO:0000269|PubMed:15130768};
DE AltName: Full=Ecto-ATP diphosphohydrolase 3;
DE Short=Ecto-ATPDase 3;
DE Short=Ecto-ATPase 3;
GN Name=Entpd3 {ECO:0000312|MGI:MGI:1321386};
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=CD-1; TISSUE=Spleen;
RX PubMed=15130768; DOI=10.1016/j.bcp.2004.02.012;
RA Lavoie E.G., Kukulski F., Levesque S.A., Lecka J., Sevigny J.;
RT "Cloning and characterization of mouse nucleoside triphosphate
RT diphosphohydrolase-3.";
RL Biochem. Pharmacol. 67:1917-1926(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Crawford P.A., Kirley T.L.;
RT "Sequencing of mouse brain NTPDase3.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Oviduct;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [6] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Catalyzes the hydrolysis of nucleoside triphosphates and
CC diphosphates (PubMed:15130768). Has a threefold preference for the
CC hydrolysis of ATP and UTP over ADP and UDP (PubMed:15130768).
CC {ECO:0000269|PubMed:15130768}.
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:15130768};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15130768};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15130768};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 mM for ATP (at pH 7.4) {ECO:0000269|PubMed:15130768};
CC KM=10 mM for UTP (at pH 7.4) {ECO:0000269|PubMed:15130768};
CC KM=19 mM for ADP (at pH 7.4) {ECO:0000269|PubMed:15130768};
CC KM=27 mM for UDP (at pH 7.4) {ECO:0000269|PubMed:15130768};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15130768};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AY376710; AAQ86585.1; -; mRNA.
DR EMBL; AY714060; AAU13839.1; -; mRNA.
DR EMBL; AK046218; BAC32641.1; -; mRNA.
DR EMBL; AK087561; BAC39928.1; -; mRNA.
DR EMBL; AK169947; BAE41475.1; -; mRNA.
DR EMBL; AK170974; BAE42153.1; -; mRNA.
DR EMBL; BC079871; AAH79871.1; -; mRNA.
DR RefSeq; NP_848791.2; NM_178676.4.
DR AlphaFoldDB; Q8BFW6; -.
DR SMR; Q8BFW6; -.
DR STRING; 10090.ENSMUSP00000036830; -.
DR GlyConnect; 2274; 3 N-Linked glycans (1 site).
DR GlyGen; Q8BFW6; 1 site, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8BFW6; -.
DR MaxQB; Q8BFW6; -.
DR PaxDb; Q8BFW6; -.
DR PRIDE; Q8BFW6; -.
DR ProteomicsDB; 330510; -.
DR Antibodypedia; 29006; 272 antibodies from 32 providers.
DR DNASU; 215446; -.
DR Ensembl; ENSMUST00000047687; ENSMUSP00000036830; ENSMUSG00000041608.
DR GeneID; 215446; -.
DR KEGG; mmu:215446; -.
DR UCSC; uc009scq.2; mouse.
DR CTD; 956; -.
DR MGI; MGI:1321386; Entpd3.
DR VEuPathDB; HostDB:ENSMUSG00000041608; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; Q8BFW6; -.
DR OMA; IMGNFLE; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q8BFW6; -.
DR TreeFam; TF332859; -.
DR BRENDA; 3.6.1.5; 3474.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; Q8BFW6; -.
DR BioGRID-ORCS; 215446; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Entpd3; mouse.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BFW6; protein.
DR Bgee; ENSMUSG00000041608; Expressed in humerus cartilage element and 158 other tissues.
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: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: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:0009134; P:nucleoside diphosphate catabolic process; IDA:MGI.
DR GO; GO:0009143; P:nucleoside triphosphate 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; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..529
FT /note="Ectonucleoside triphosphate diphosphohydrolase 3"
FT /id="PRO_0000455156"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..485
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT BINDING 222..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..116
FT /evidence="ECO:0000250|UniProtKB:O75355"
FT DISULFID 261..308
FT /evidence="ECO:0000250|UniProtKB:O75355"
FT DISULFID 289..334
FT /evidence="ECO:0000250|UniProtKB:O75355"
FT DISULFID 347..353
FT /evidence="ECO:0000250|UniProtKB:O75355"
FT DISULFID 399..422
FT /evidence="ECO:0000250|UniProtKB:O75355"
SQ SEQUENCE 529 AA; 58984 MW; E34F5EF187484F2C CRC64;
MFTVMTRQPC EQAGFRALSR TPAIVTLVVL LVSIVVLVTL TLIQIRHPQV LPPGLKYGVV
LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF RCSVKGSGIS SYENNPQDAP KAFEDCILKV
KEQVPEHLHG STRIYLGATA GMRLLRLQNE TAAREVLESI QSYFKSQPFD FRGAQIISGQ
EEGVYGWITA NYIMGNFLEK NLWHMWVHPH GVDTTGALDL GGASTQISFV AGEKMEPNAS
DTVQVSLYGY TYTLYTHSFQ CYGQNEAEKK FLAMLLQSPS TEANISNPCY PQGYSTAFTL
GHVFGSLCTE KQRPESYNSS KSVTFMGTGD PRLCREKVAS VFDFNACQEQ DACSFDGIYQ
PKVQGPFVAF AGFYYTASAL NLSGSFSLTS FNDSSWDFCR HTWSELPALL SRFDETYARS
YCFSAHYIYH LLVNGYKFTE ETWPQIRFEK EVGNSSIAWS LGYMLSLTNQ IPAGSPLIHL
PIQPPVFMGV LAFFTAIALL CLAFLLYLCS SFRTKERSEN AFDQAVDSD
