ENTP7_MOUSE
ID ENTP7_MOUSE Reviewed; 606 AA.
AC Q3TCT4; B9EHD3; Q3TM04; Q571A5; Q9ET10;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 7;
DE Short=NTPDase 7;
DE EC=3.6.1.15 {ECO:0000269|PubMed:23241884};
DE AltName: Full=Lysosomal apyrase-like protein 1 {ECO:0000303|PubMed:11278936};
GN Name=Entpd7; Synonyms=Kiaa4066, Lalp1 {ECO:0000303|PubMed:11278936};
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 1), AND TISSUE SPECIFICITY.
RX PubMed=11278936; DOI=10.1074/jbc.m011569200;
RA Shi J.-D., Kukar T., Wang C.-Y., Li Q.-Z., Cruz P.E., Davoodi-Semiromi A.,
RA Yang P., Gu Y., Lian W., Wu D.H., She J.-X.;
RT "Molecular cloning and characterization of a novel mammalian endo-apyrase
RT (LALP1).";
RL J. Biol. Chem. 276:17474-17478(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-606 (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=23241884; DOI=10.4049/jimmunol.1103067;
RA Kusu T., Kayama H., Kinoshita M., Jeon S.G., Ueda Y., Goto Y., Okumura R.,
RA Saiga H., Kurakawa T., Ikeda K., Maeda Y., Nishimura J., Arima Y.,
RA Atarashi K., Honda K., Murakami M., Kunisawa J., Kiyono H., Okumura M.,
RA Yamamoto M., Takeda K.;
RT "Ecto-nucleoside triphosphate diphosphohydrolase 7 controls Th17 cell
RT responses through regulation of luminal ATP in the small intestine.";
RL J. Immunol. 190:774-783(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates and
CC diphosphates in a calcium- or magnesium-dependent manner.
CC Preferentially hydrolyzes nucleoside 5'-triphosphates, with substrate
CC preference for UTP > GTP > CTP. Hydrolyzes nucleoside diphosphates only
CC to a minor extent (By similarity). In contrast to its human ortholog is
CC able to hydrolyze ATP. In the epithelial cells of small intestine
CC controls luminal ATP levels, therefore regulating Th17-cell development
CC (PubMed:23241884). {ECO:0000250|UniProtKB:Q9NQZ7,
CC ECO:0000269|PubMed:23241884}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000269|PubMed:23241884};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23241884};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NQZ7};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9NQZ7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TCT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TCT4-2; Sequence=VSP_022743, VSP_022744;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in brain,
CC kidney, liver, testis and small intestin. Weakly expressed in lung,
CC thymus and heart. {ECO:0000269|PubMed:11278936,
CC ECO:0000269|PubMed:23241884}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are born at the normal Mendelian
CC ratios and grow healthily until 16 week of age. Normal lymphocyte
CC development is observed. However deficient mice shown an increased in
CC ATP concentrations in the small intestinal lumen and increased numbers
CC of IL-17-producing Th17 cells in the small intestinal lamina propria.
CC They show increased resistance to Citrobacter rodentium infection and
CC increased susceptibility to experimental autoimmune encephalomyelitis.
CC {ECO:0000269|PubMed:23241884}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF288221; AAG01009.1; -; mRNA.
DR EMBL; AK147401; BAE27889.1; -; mRNA.
DR EMBL; AK166220; BAE38638.1; -; mRNA.
DR EMBL; AK170546; BAE41871.1; -; mRNA.
DR EMBL; BC137709; AAI37710.1; -; mRNA.
DR EMBL; BC137717; AAI37718.1; -; mRNA.
DR EMBL; AK220284; BAD90209.1; -; mRNA.
DR CCDS; CCDS29835.1; -. [Q3TCT4-1]
DR RefSeq; NP_444333.3; NM_053103.5. [Q3TCT4-1]
DR AlphaFoldDB; Q3TCT4; -.
DR SMR; Q3TCT4; -.
DR STRING; 10090.ENSMUSP00000079864; -.
DR GlyGen; Q3TCT4; 1 site.
DR PhosphoSitePlus; Q3TCT4; -.
DR EPD; Q3TCT4; -.
DR MaxQB; Q3TCT4; -.
DR PaxDb; Q3TCT4; -.
DR PeptideAtlas; Q3TCT4; -.
DR PRIDE; Q3TCT4; -.
DR ProteomicsDB; 275919; -. [Q3TCT4-1]
DR ProteomicsDB; 275920; -. [Q3TCT4-2]
DR Antibodypedia; 3066; 109 antibodies from 21 providers.
DR DNASU; 93685; -.
DR Ensembl; ENSMUST00000081079; ENSMUSP00000079864; ENSMUSG00000025192. [Q3TCT4-1]
DR GeneID; 93685; -.
DR KEGG; mmu:93685; -.
DR UCSC; uc008hor.2; mouse. [Q3TCT4-2]
DR UCSC; uc008hos.2; mouse. [Q3TCT4-1]
DR CTD; 57089; -.
DR MGI; MGI:2135885; Entpd7.
DR VEuPathDB; HostDB:ENSMUSG00000025192; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244974; -.
DR HOGENOM; CLU_010246_6_0_1; -.
DR InParanoid; Q3TCT4; -.
DR OMA; WLINMLH; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q3TCT4; -.
DR TreeFam; TF354343; -.
DR BRENDA; 3.6.1.5; 3474.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR BioGRID-ORCS; 93685; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Entpd7; mouse.
DR PRO; PR:Q3TCT4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3TCT4; protein.
DR Bgee; ENSMUSG00000025192; Expressed in small intestine Peyer's patch and 190 other tissues.
DR Genevisible; Q3TCT4; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0043273; F:CTPase activity; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; ISO:MGI.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0006254; P:CTP catabolic process; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; ISS:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; ISO:MGI.
DR GO; GO:0009203; P:ribonucleoside triphosphate catabolic process; ISO:MGI.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; IMP:UniProtKB.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
DR GO; GO:0046052; P:UTP catabolic process; ISS:UniProtKB.
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; Calcium; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..606
FT /note="Ectonucleoside triphosphate diphosphohydrolase 7"
FT /id="PRO_0000274420"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..548
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 448..477
FT /evidence="ECO:0000250"
FT VAR_SEQ 338..354
FT /note="LLGQKTGLSPDNPFLDP -> YNVARLQPLGRNSSTQL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022743"
FT VAR_SEQ 355..606
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022744"
FT CONFLICT 22
FT /note="S -> R (in Ref. 1; AAG01009)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="K -> R (in Ref. 2; BAE38638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 68974 MW; FD574C72FAA7848A CRC64;
MARISFSYLC PASWYFTVPT VSPFLRQRVA FLGLFFIPCV LLLLLIMDLR HWATSLPRDR
QYERYLARVG DLEATNTEDP NLNYGLVVDC GSSGSRIFVY FWPRHNGNPH DLLDIKQMRD
RNSQPVVKKI KPGISAMADT PEHASDYLRP LLSFAAAHVP VKKHRETPLY ILCTAGMRLL
PERQQLAILA DLVKDLPLEF DFLFSQSQAE VISGKQEGVY AWIGINFVLG RFDHEDESDS
DTSVDSAAGR RRTVGILDMG GASLQIAYEV PTSASDLPPK QEEAAKILLA EFNLGCDVQH
TEHVYRVYVT TFLGFGGNFA RQRYEDLVLN ETLNKNRLLG QKTGLSPDNP FLDPCLPVGL
TDMVKRNNQV LHFRGKGDWA SCRTLLSPLL ARSNTSQASL NGIYQSPIDF NNSEFYGFSE
FFYCTEDVLR IGGHYHGPTF AKAAQDYCGM AWPVLAQRFK NGLFSSHADE HRLKYQCFKS
AWMYEVLHEG FHFPYDYPNL QTAQLVYDRE VQWTLGAILY KTRFLPLRDL RQGQGGVRPA
HGSWLRLSFV YNHYLFFACT LVVLLAIVLY LLRIHRIHRR QTRASAPLDL LWIEQVVPMI
GVQVGP
