ENTP1_HUMAN
ID ENTP1_HUMAN Reviewed; 510 AA.
AC P49961; A9Z1X8; B4DWB9; B4E1X1; B7Z599; G3XAF6; Q5T561; Q5T562; Q86VV3;
AC Q9UQQ9; Q9Y3Q9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 202.
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 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] (ISOFORM 1).
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 [MRNA] (ISOFORM 1).
RC TISSUE=Umbilical vein;
RX PubMed=8996251; DOI=10.1084/jem.185.1.153;
RA Robson S.C., Kaczmarek E., Siegel J.B., Candinas D., Koziak K., Millan M.,
RA Hancock W.W., Bach F.H.;
RT "Loss of ATP diphosphohydrolase activity with endothelial cell
RT activation.";
RL J. Exp. Med. 185:153-163(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta;
RX PubMed=10405171; DOI=10.1016/s0014-5793(99)00751-6;
RA Matsumoto M., Sakurai Y., Kokubo T., Yagi H., Makita K., Matsui T.,
RA Titani K., Fujimura Y., Narita N.;
RT "The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and
RT II.";
RL FEBS Lett. 453:335-340(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5 AND 6).
RC TISSUE=Brain, Synovium, Trachea, and Uterus;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 240-242; 162-166; 185-189; 210-223; 243-249 AND
RP 288-297.
RC TISSUE=Placenta;
RX PubMed=8529670; DOI=10.1111/j.1432-1033.1995.066_c.x;
RA Christoforidis S., Papamarcaki T., Galaris D., Kellner R., Tsolas O.;
RT "Purification and properties of human placental ATP diphosphohydrolase.";
RL Eur. J. Biochem. 234:66-74(1995).
RN [9]
RP PROTEIN SEQUENCE OF 1-30; 49-65; 94-97; 88-93; 193-223; 245-265; 382-385
RP AND 399-405 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=9846014; DOI=10.1016/s0925-5710(98)00080-2;
RA Makita K., Shimoyama T., Sakurai Y., Yagi H., Matsumoto M., Narita N.,
RA Sakamoto Y., Saito S., Ikeda Y., Suzuki M., Titani K., Fujimura Y.;
RT "Placental ecto-ATP diphosphohydrolase: its structural feature distinct
RT from CD39, localization and inhibition on shear-induced platelet
RT aggregation.";
RL Int. J. Hematol. 68:297-310(1998).
RN [10]
RP FUNCTION, AND COFACTOR.
RX PubMed=8955160; DOI=10.1074/jbc.271.51.33116;
RA Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J.,
RA Beaudoin A.R., Bach F.H., Robson S.C.;
RT "Identification and characterization of CD39/vascular ATP
RT diphosphohydrolase.";
RL J. Biol. Chem. 271:33116-33122(1996).
RN [11]
RP CHARACTERIZATION.
RX PubMed=8626624; DOI=10.1074/jbc.271.17.10391;
RA Wang T.F., Guidotti G.;
RT "CD39 is an ecto-(Ca2+,Mg2+)-apyrase.";
RL J. Biol. Chem. 271:9898-9901(1996).
RN [12]
RP PALMITOYLATION AT CYS-13.
RX PubMed=10636909; DOI=10.1074/jbc.275.3.2057;
RA Koziak K., Kaczmarek E., Kittel A., Sevigny J., Blusztajn J.K.,
RA Schulte Am Esch J. II, Imai M., Guckelberger O., Goepfert C., Qawi I.,
RA Robson S.C.;
RT "Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to
RT caveolae.";
RL J. Biol. Chem. 275:2057-2062(2000).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73 AND ASN-292.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP VARIANT SPG64 ARG-210.
RX PubMed=24482476; DOI=10.1126/science.1247363;
RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA Gleeson J.G.;
RT "Exome sequencing links corticospinal motor neuron disease to common
RT neurodegenerative disorders.";
RL Science 343:506-511(2014).
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 {ECO:0000269|PubMed:8955160}.
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;
CC Evidence={ECO:0000269|PubMed:8955160};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8955160};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-7.5 with ATP as substrate, and 7.5-8.0 with ADP as
CC substrate.;
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- INTERACTION:
CC P49961; Q96S59: RANBP9; NbExp=5; IntAct=EBI-8074749, EBI-636085;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Vascular;
CC IsoId=P49961-1; Sequence=Displayed;
CC Name=2; Synonyms=Placental I;
CC IsoId=P49961-2; Sequence=VSP_003607;
CC Name=3; Synonyms=Placental II;
CC IsoId=P49961-3; Sequence=VSP_003607, VSP_003608, VSP_003609;
CC Name=4;
CC IsoId=P49961-4; Sequence=VSP_044284;
CC Name=5;
CC IsoId=P49961-5; Sequence=VSP_044283;
CC Name=6;
CC IsoId=P49961-6; Sequence=VSP_046050;
CC -!- TISSUE SPECIFICITY: Expressed primarily on activated lymphoid cells.
CC Also expressed in endothelial tissues. Isoform 1 and isoform 3 are
CC present in both placenta and umbilical vein, whereas isoform 2 is
CC present in placenta only.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Palmitoylated in the N-terminal part.
CC {ECO:0000269|PubMed:10636909}.
CC -!- DISEASE: Spastic paraplegia 64, autosomal recessive (SPG64)
CC [MIM:615683]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body.
CC {ECO:0000269|PubMed:24482476}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; S73813; AAB32152.1; -; mRNA.
DR EMBL; U87967; AAB47572.1; -; mRNA.
DR EMBL; AK304836; BAG65580.1; -; mRNA.
DR EMBL; AJ133133; CAB41886.1; -; mRNA.
DR EMBL; AJ133134; CAB41887.1; -; mRNA.
DR EMBL; AK298648; BAH12835.1; -; mRNA.
DR EMBL; AK301459; BAG62981.1; -; mRNA.
DR EMBL; AK304018; BAG64933.1; -; mRNA.
DR EMBL; AK316009; BAH14380.1; -; mRNA.
DR EMBL; AL356632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49988.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49989.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49990.1; -; Genomic_DNA.
DR EMBL; BC047664; AAH47664.1; -; mRNA.
DR CCDS; CCDS41554.1; -. [P49961-2]
DR CCDS; CCDS53556.1; -. [P49961-6]
DR CCDS; CCDS53557.1; -. [P49961-5]
DR CCDS; CCDS7444.1; -. [P49961-1]
DR PIR; I56242; I56242.
DR RefSeq; NP_001091645.1; NM_001098175.1. [P49961-2]
DR RefSeq; NP_001157650.1; NM_001164178.1. [P49961-6]
DR RefSeq; NP_001157653.1; NM_001164181.1. [P49961-5]
DR RefSeq; NP_001157654.1; NM_001164182.1. [P49961-4]
DR RefSeq; NP_001157655.1; NM_001164183.1. [P49961-4]
DR RefSeq; NP_001299583.1; NM_001312654.1. [P49961-5]
DR RefSeq; NP_001307845.1; NM_001320916.1.
DR RefSeq; NP_001767.3; NM_001776.5. [P49961-1]
DR RefSeq; XP_011538673.1; XM_011540371.2. [P49961-2]
DR RefSeq; XP_011538679.1; XM_011540377.2. [P49961-5]
DR RefSeq; XP_016872448.1; XM_017016959.1. [P49961-4]
DR AlphaFoldDB; P49961; -.
DR SMR; P49961; -.
DR BioGRID; 107391; 14.
DR CORUM; P49961; -.
DR IntAct; P49961; 1.
DR MINT; P49961; -.
DR STRING; 9606.ENSP00000360250; -.
DR BindingDB; P49961; -.
DR ChEMBL; CHEMBL5722; -.
DR GuidetoPHARMACOLOGY; 2888; -.
DR GlyConnect; 1192; 2 N-Linked glycans (2 sites).
DR GlyGen; P49961; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P49961; -.
DR PhosphoSitePlus; P49961; -.
DR SwissPalm; P49961; -.
DR BioMuta; ENTPD1; -.
DR DMDM; 1705710; -.
DR jPOST; P49961; -.
DR MassIVE; P49961; -.
DR MaxQB; P49961; -.
DR PaxDb; P49961; -.
DR PeptideAtlas; P49961; -.
DR PRIDE; P49961; -.
DR ProteomicsDB; 33734; -.
DR ProteomicsDB; 56188; -. [P49961-1]
DR ProteomicsDB; 56189; -. [P49961-2]
DR ProteomicsDB; 56190; -. [P49961-3]
DR ProteomicsDB; 6672; -.
DR ProteomicsDB; 70071; -.
DR Antibodypedia; 2888; 907 antibodies from 43 providers.
DR CPTC; P49961; 1 antibody.
DR DNASU; 953; -.
DR Ensembl; ENST00000371205.5; ENSP00000360248.4; ENSG00000138185.20. [P49961-1]
DR Ensembl; ENST00000371207.8; ENSP00000360250.3; ENSG00000138185.20. [P49961-6]
DR Ensembl; ENST00000453258.6; ENSP00000390955.2; ENSG00000138185.20. [P49961-2]
DR Ensembl; ENST00000543964.6; ENSP00000442968.1; ENSG00000138185.20. [P49961-5]
DR GeneID; 953; -.
DR KEGG; hsa:953; -.
DR MANE-Select; ENST00000371205.5; ENSP00000360248.4; NM_001776.6; NP_001767.3.
DR UCSC; uc001klh.5; human. [P49961-1]
DR CTD; 953; -.
DR DisGeNET; 953; -.
DR GeneCards; ENTPD1; -.
DR HGNC; HGNC:3363; ENTPD1.
DR HPA; ENSG00000138185; Low tissue specificity.
DR MalaCards; ENTPD1; -.
DR MIM; 601752; gene.
DR MIM; 615683; phenotype.
DR neXtProt; NX_P49961; -.
DR OpenTargets; ENSG00000138185; -.
DR Orphanet; 401810; Autosomal recessive spastic paraplegia type 64.
DR PharmGKB; PA27798; -.
DR VEuPathDB; HostDB:ENSG00000138185; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; P49961; -.
DR OMA; YPFNFQG; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; P49961; -.
DR TreeFam; TF332859; -.
DR BioCyc; MetaCyc:HS06471-MON; -.
DR BRENDA; 3.6.1.5; 2681.
DR PathwayCommons; P49961; -.
DR Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SABIO-RK; P49961; -.
DR SignaLink; P49961; -.
DR BioGRID-ORCS; 953; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; ENTPD1; human.
DR GeneWiki; ENTPD1; -.
DR GenomeRNAi; 953; -.
DR Pharos; P49961; Tchem.
DR PRO; PR:P49961; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P49961; protein.
DR Bgee; ENSG00000138185; Expressed in saphenous vein and 203 other tissues.
DR ExpressionAtlas; P49961; baseline and differential.
DR Genevisible; P49961; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein;
KW Hereditary spastic paraplegia; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW Neurodegeneration; Nucleotide-binding; Palmitate; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT /id="PRO_0000209902"
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 LIPID 13
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10636909"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
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 255..301
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 282..325
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 338..343
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 390..413
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_044284"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044283"
FT VAR_SEQ 1..5
FT /note="MEDTK -> MGREELFLTFSFSSGFQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046050"
FT VAR_SEQ 1..4
FT /note="MEDT -> MKGTKDLTSQQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10405171"
FT /id="VSP_003607"
FT VAR_SEQ 272..299
FT /note="VASNEILRDPCFHPGYKKVVNVSDLYKT -> ASITQSRPAPFTSAPPAPTS
FT CCFLFQIQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10405171"
FT /id="VSP_003608"
FT VAR_SEQ 300..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10405171"
FT /id="VSP_003609"
FT VARIANT 210
FT /note="G -> R (in SPG64; dbSNP:rs1566229309)"
FT /evidence="ECO:0000269|PubMed:24482476"
FT /id="VAR_071082"
FT VARIANT 293
FT /note="V -> I (in dbSNP:rs3793744)"
FT /id="VAR_022099"
FT CONFLICT 57..58
FT /note="SS -> G (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> K (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="T -> TGET (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="V -> Y (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="M -> I (in Ref. 4; BAG62981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57965 MW; BAD87D2499649159 CRC64;
MEDTKESNVK TFCSKNILAI LGFSSIIAVI ALLAVGLTQN KALPENVKYG IVLDAGSSHT
SLYIYKWPAE KENDTGVVHQ VEECRVKGPG ISKFVQKVNE IGIYLTDCME RAREVIPRSQ
HQETPVYLGA TAGMRLLRME SEELADRVLD VVERSLSNYP FDFQGARIIT GQEEGAYGWI
TINYLLGKFS QKTRWFSIVP YETNNQETFG ALDLGGASTQ VTFVPQNQTI ESPDNALQFR
LYGKDYNVYT HSFLCYGKDQ ALWQKLAKDI QVASNEILRD PCFHPGYKKV VNVSDLYKTP
CTKRFEMTLP FQQFEIQGIG NYQQCHQSIL ELFNTSYCPY SQCAFNGIFL PPLQGDFGAF
SAFYFVMKFL NLTSEKVSQE KVTEMMKKFC AQPWEEIKTS YAGVKEKYLS EYCFSGTYIL
SLLLQGYHFT ADSWEHIHFI GKIQGSDAGW TLGYMLNLTN MIPAEQPLST PLSHSTYVFL
MVLFSLVLFT VAIIGLLIFH KPSYFWKDMV
