ENTP7_HUMAN
ID ENTP7_HUMAN Reviewed; 604 AA.
AC Q9NQZ7; B2RB83; B3KP21; D3DR64;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 7;
DE Short=NTPDase 7;
DE EC=3.6.1.15 {ECO:0000269|PubMed:11278936};
DE AltName: Full=Lysosomal apyrase-like protein 1;
GN Name=ENTPD7; Synonyms=LALP1 {ECO:0000303|PubMed:11278936};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, COFACTOR, AND
RP SUBCELLULAR LOCATION.
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], AND VARIANT ALA-276.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 ATP and nucleoside
CC diphosphates only to a minor extent. {ECO:0000269|PubMed:11278936}.
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:11278936};
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:0000269|PubMed:11278936};
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:0000269|PubMed:11278936};
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:0000269|PubMed:11278936};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11278936};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11278936};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11278936}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF269255; AAF90135.1; -; mRNA.
DR EMBL; AK055540; BAG51533.1; -; mRNA.
DR EMBL; AK314542; BAG37130.1; -; mRNA.
DR EMBL; AL133353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49861.1; -; Genomic_DNA.
DR EMBL; BC119008; AAI19009.1; -; mRNA.
DR EMBL; BC122857; AAI22858.1; -; mRNA.
DR CCDS; CCDS7480.1; -.
DR RefSeq; NP_065087.1; NM_020354.3.
DR AlphaFoldDB; Q9NQZ7; -.
DR SMR; Q9NQZ7; -.
DR BioGRID; 121358; 52.
DR IntAct; Q9NQZ7; 23.
DR STRING; 9606.ENSP00000359520; -.
DR GlyGen; Q9NQZ7; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQZ7; -.
DR PhosphoSitePlus; Q9NQZ7; -.
DR BioMuta; ENTPD7; -.
DR DMDM; 74752912; -.
DR EPD; Q9NQZ7; -.
DR jPOST; Q9NQZ7; -.
DR MassIVE; Q9NQZ7; -.
DR MaxQB; Q9NQZ7; -.
DR PaxDb; Q9NQZ7; -.
DR PeptideAtlas; Q9NQZ7; -.
DR PRIDE; Q9NQZ7; -.
DR ProteomicsDB; 82238; -.
DR Antibodypedia; 3066; 109 antibodies from 21 providers.
DR DNASU; 57089; -.
DR Ensembl; ENST00000370489.5; ENSP00000359520.4; ENSG00000198018.7.
DR GeneID; 57089; -.
DR KEGG; hsa:57089; -.
DR MANE-Select; ENST00000370489.5; ENSP00000359520.4; NM_020354.5; NP_065087.1.
DR UCSC; uc001kqa.5; human.
DR CTD; 57089; -.
DR GeneCards; ENTPD7; -.
DR HGNC; HGNC:19745; ENTPD7.
DR HPA; ENSG00000198018; Tissue enhanced (intestine).
DR MIM; 616753; gene.
DR neXtProt; NX_Q9NQZ7; -.
DR OpenTargets; ENSG00000198018; -.
DR PharmGKB; PA134993462; -.
DR VEuPathDB; HostDB:ENSG00000198018; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244974; -.
DR HOGENOM; CLU_010246_6_0_1; -.
DR InParanoid; Q9NQZ7; -.
DR OMA; WLINMLH; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9NQZ7; -.
DR TreeFam; TF354343; -.
DR BRENDA; 3.6.1.5; 2681.
DR PathwayCommons; Q9NQZ7; -.
DR Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SignaLink; Q9NQZ7; -.
DR BioGRID-ORCS; 57089; 20 hits in 1078 CRISPR screens.
DR ChiTaRS; ENTPD7; human.
DR GenomeRNAi; 57089; -.
DR Pharos; Q9NQZ7; Tbio.
DR PRO; PR:Q9NQZ7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NQZ7; protein.
DR Bgee; ENSG00000198018; Expressed in jejunal mucosa and 141 other tissues.
DR ExpressionAtlas; Q9NQZ7; baseline and differential.
DR Genevisible; Q9NQZ7; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
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:0043273; F:CTPase activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA: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; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; IDA:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; IEA:Ensembl.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
DR GO; GO:0046052; P:UTP catabolic process; IDA: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 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..604
FT /note="Ectonucleoside triphosphate diphosphohydrolase 7"
FT /id="PRO_0000274419"
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..546
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..604
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 VARIANT 276
FT /note="V -> A (in dbSNP:rs11190245)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_030287"
SQ SEQUENCE 604 AA; 68960 MW; 6B73997A8AB318D8 CRC64;
MARISFSYLC PASWYFTVPT VSPFLRQRVA FLGLFFISCL LLLMLIIDFR HWSASLPRDR
QYERYLARVG ELEATDTEDP NLNYGLVVDC GSSGSRIFVY FWPRHNGNPH DLLDIKQMRD
RNSQPVVKKI KPGISAMADT PEHASDYLRP LLSFAAAHVP VKKHKETPLY ILCTAGMRLL
PERKQLAILA DLVKDLPLEF DFLFSQSQAE VISGKQEGVY AWIGINFVLG RFDHEDESDA
EATQELAAGR RRTVGILDMG GASLQIAYEV PTSTSVLPAK QEEAAKILLA EFNLGCDVQH
TEHVYRVYVT TFLGFGGNFA RQRYEDLVLN ETLNKNRLLG QKTGLSPDNP FLDPCLPVGL
TDVVERNSQV LHVRGRGDWV SCGAMLSPLL ARSNTSQASL NGIYQSPIDF NNSEFYGFSE
FFYCTEDVLR IGGRYHGPTF AKAAQDYCGM AWSVLTQRFK NGLFSSHADE HRLKYQCFKS
AWMYQVLHEG FHFPYDYPNL RTAQLVYDRE VQWTLGAILY KTRFLPLRDL RQEGVRQAHG
SWFRLSFVYN HYLFFACILV VLLAIFLYLL RLRRIHHRQT RASAPLDLLW LEEVVPMMGV
QVGP
