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Ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) (EC 3.6.1.5) (Ecto-ATP diphosphohydrolase 1) (Ecto-ATPDase 1) (Ecto-ATPase 1) (Ecto-apyrase) (Lymphoid cell activation antigen) (CD antigen CD39)

 ENTP1_HUMAN             Reviewed;         510 AA.
P49961; A9Z1X8; B4DWB9; B4E1X1; B7Z599; G3XAF6; Q5T561; Q5T562;
Q86VV3; Q9UQQ9; Q9Y3Q9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1;
Short=NTPDase 1;
EC=3.6.1.5;
AltName: Full=Ecto-ATP diphosphohydrolase 1;
Short=Ecto-ATPDase 1;
Short=Ecto-ATPase 1;
AltName: Full=Ecto-apyrase;
AltName: Full=Lymphoid cell activation antigen;
AltName: CD_antigen=CD39;
Name=ENTPD1; Synonyms=CD39;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7930580;
Maliszewski C.R., Delespesse G.J.T., Schoenborn M.A., Armitage R.J.,
Fanslow W.C., Nakajima T., Baker E., Sutherland G.R., Poindexter K.,
Birks C., Alpert A., Friend D., Gimpel S.D., Gayle R.B. III;
"The CD39 lymphoid cell activation antigen. Molecular cloning and
structural characterization.";
J. Immunol. 153:3574-3583(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein;
PubMed=8996251; DOI=10.1084/jem.185.1.153;
Robson S.C., Kaczmarek E., Siegel J.B., Candinas D., Koziak K.,
Millan M., Hancock W.W., Bach F.H.;
"Loss of ATP diphosphohydrolase activity with endothelial cell
activation.";
J. Exp. Med. 185:153-163(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Placenta;
PubMed=10405171; DOI=10.1016/S0014-5793(99)00751-6;
Matsumoto M., Sakurai Y., Kokubo T., Yagi H., Makita K., Matsui T.,
Titani K., Fujimura Y., Narita N.;
"The cDNA cloning of human placental ecto-ATP diphosphohydrolases I
and II.";
FEBS Lett. 453:335-340(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5 AND 6).
TISSUE=Brain, Synovium, Trachea, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 240-242; 162-166; 185-189; 210-223; 243-249 AND
288-297.
TISSUE=Placenta;
PubMed=8529670; DOI=10.1111/j.1432-1033.1995.066_c.x;
Christoforidis S., Papamarcaki T., Galaris D., Kellner R., Tsolas O.;
"Purification and properties of human placental ATP
diphosphohydrolase.";
Eur. J. Biochem. 234:66-74(1995).
[9]
PROTEIN SEQUENCE OF 1-30; 49-65; 94-97; 88-93; 193-223; 245-265;
382-385 AND 399-405 (ISOFORM 2).
TISSUE=Placenta;
PubMed=9846014; DOI=10.1016/S0925-5710(98)00080-2;
Makita K., Shimoyama T., Sakurai Y., Yagi H., Matsumoto M., Narita N.,
Sakamoto Y., Saito S., Ikeda Y., Suzuki M., Titani K., Fujimura Y.;
"Placental ecto-ATP diphosphohydrolase: its structural feature
distinct from CD39, localization and inhibition on shear-induced
platelet aggregation.";
Int. J. Hematol. 68:297-310(1998).
[10]
FUNCTION, AND COFACTOR.
PubMed=8955160; DOI=10.1074/jbc.271.51.33116;
Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J.,
Beaudoin A.R., Bach F.H., Robson S.C.;
"Identification and characterization of CD39/vascular ATP
diphosphohydrolase.";
J. Biol. Chem. 271:33116-33122(1996).
[11]
CHARACTERIZATION.
PubMed=8626624; DOI=10.1074/jbc.271.17.10391;
Wang T.F., Guidotti G.;
"CD39 is an ecto-(Ca2+,Mg2+)-apyrase.";
J. Biol. Chem. 271:9898-9901(1996).
[12]
PALMITOYLATION AT CYS-13.
PubMed=10636909; DOI=10.1074/jbc.275.3.2057;
Koziak K., Kaczmarek E., Kittel A., Sevigny J., Blusztajn J.K.,
Schulte Am Esch J. II, Imai M., Guckelberger O., Goepfert C., Qawi I.,
Robson S.C.;
"Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to
caveolae.";
J. Biol. Chem. 275:2057-2062(2000).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73 AND ASN-292.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
VARIANT SPG64 ARG-210.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
-!- FUNCTION: In the nervous system, could hydrolyze ATP and other
nucleotides to regulate purinergic neurotransmission. Could also
be implicated in the prevention of platelet aggregation by
hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP
equally well. {ECO:0000269|PubMed:8955160}.
-!- CATALYTIC ACTIVITY: A nucleoside 5'-triphosphate + 2 H(2)O = a
nucleoside 5'-phosphate + 2 phosphate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:8955160};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8955160};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0-7.5 with ATP as substrate, and 7.5-8.0 with
ADP as substrate.;
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
-!- INTERACTION:
Q96S59:RANBP9; NbExp=5; IntAct=EBI-8074749, EBI-636085;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Vascular;
IsoId=P49961-1; Sequence=Displayed;
Name=2; Synonyms=Placental I;
IsoId=P49961-2; Sequence=VSP_003607;
Name=3; Synonyms=Placental II;
IsoId=P49961-3; Sequence=VSP_003607, VSP_003608, VSP_003609;
Name=4;
IsoId=P49961-4; Sequence=VSP_044284;
Name=5;
IsoId=P49961-5; Sequence=VSP_044283;
Name=6;
IsoId=P49961-6; Sequence=VSP_046050;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed primarily on activated lymphoid
cells. Also expressed in endothelial tissues. Isoform 1 and
isoform 3 are present in both placenta and umbilical vein, whereas
isoform 2 is present in placenta only.
-!- PTM: The N-terminus is blocked.
-!- PTM: Palmitoylated in the N-terminal part.
{ECO:0000269|PubMed:10636909}.
-!- DISEASE: Spastic paraplegia 64, autosomal recessive (SPG64)
[MIM:615683]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:24482476}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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EMBL; S73813; AAB32152.1; -; mRNA.
EMBL; U87967; AAB47572.1; -; mRNA.
EMBL; AK304836; BAG65580.1; -; mRNA.
EMBL; AJ133133; CAB41886.1; -; mRNA.
EMBL; AJ133134; CAB41887.1; -; mRNA.
EMBL; AK298648; BAH12835.1; -; mRNA.
EMBL; AK301459; BAG62981.1; -; mRNA.
EMBL; AK304018; BAG64933.1; -; mRNA.
EMBL; AK316009; BAH14380.1; -; mRNA.
EMBL; AL356632; CAI16771.1; -; Genomic_DNA.
EMBL; AL365273; CAI16771.1; JOINED; Genomic_DNA.
EMBL; AL365273; CAH73752.1; -; Genomic_DNA.
EMBL; AL365273; CAH73753.1; -; Genomic_DNA.
EMBL; AL356632; CAH73753.1; JOINED; Genomic_DNA.
EMBL; AL365273; CAH73754.1; -; Genomic_DNA.
EMBL; AL356632; CAH73754.1; JOINED; Genomic_DNA.
EMBL; AL356632; CAI16770.1; -; Genomic_DNA.
EMBL; AL365273; CAI16770.1; JOINED; Genomic_DNA.
EMBL; CH471066; EAW49988.1; -; Genomic_DNA.
EMBL; CH471066; EAW49989.1; -; Genomic_DNA.
EMBL; CH471066; EAW49990.1; -; Genomic_DNA.
EMBL; BC047664; AAH47664.1; -; mRNA.
CCDS; CCDS41554.1; -. [P49961-2]
CCDS; CCDS53556.1; -. [P49961-6]
CCDS; CCDS53557.1; -. [P49961-5]
CCDS; CCDS53558.1; -. [P49961-4]
CCDS; CCDS7444.1; -. [P49961-1]
PIR; I56242; I56242.
RefSeq; NP_001091645.1; NM_001098175.1. [P49961-2]
RefSeq; NP_001157650.1; NM_001164178.1. [P49961-6]
RefSeq; NP_001157653.1; NM_001164181.1. [P49961-5]
RefSeq; NP_001157654.1; NM_001164182.1. [P49961-4]
RefSeq; NP_001157655.1; NM_001164183.1. [P49961-4]
RefSeq; NP_001299583.1; NM_001312654.1. [P49961-5]
RefSeq; NP_001307845.1; NM_001320916.1.
RefSeq; NP_001767.3; NM_001776.5. [P49961-1]
RefSeq; XP_011538673.1; XM_011540371.2. [P49961-2]
RefSeq; XP_011538679.1; XM_011540377.2. [P49961-5]
RefSeq; XP_016872448.1; XM_017016959.1. [P49961-4]
UniGene; Hs.576612; -.
UniGene; Hs.722260; -.
ProteinModelPortal; P49961; -.
SMR; P49961; -.
BioGrid; 107391; 1.
CORUM; P49961; -.
IntAct; P49961; 1.
MINT; MINT-8215689; -.
STRING; 9606.ENSP00000360250; -.
BindingDB; P49961; -.
ChEMBL; CHEMBL5722; -.
GuidetoPHARMACOLOGY; 2888; -.
iPTMnet; P49961; -.
PhosphoSitePlus; P49961; -.
SwissPalm; P49961; -.
BioMuta; ENTPD1; -.
DMDM; 1705710; -.
MaxQB; P49961; -.
PaxDb; P49961; -.
PeptideAtlas; P49961; -.
PRIDE; P49961; -.
DNASU; 953; -.
Ensembl; ENST00000371205; ENSP00000360248; ENSG00000138185. [P49961-1]
Ensembl; ENST00000371207; ENSP00000360250; ENSG00000138185. [P49961-6]
Ensembl; ENST00000453258; ENSP00000390955; ENSG00000138185. [P49961-2]
Ensembl; ENST00000543964; ENSP00000442968; ENSG00000138185. [P49961-5]
GeneID; 953; -.
KEGG; hsa:953; -.
UCSC; uc001klh.5; human. [P49961-1]
CTD; 953; -.
DisGeNET; 953; -.
EuPathDB; HostDB:ENSG00000138185.17; -.
EuPathDB; HostDB:ENSG00000282889.1; -.
GeneCards; ENTPD1; -.
HGNC; HGNC:3363; ENTPD1.
HPA; CAB002494; -.
HPA; HPA014067; -.
MalaCards; ENTPD1; -.
MIM; 601752; gene.
MIM; 615683; phenotype.
neXtProt; NX_P49961; -.
OpenTargets; ENSG00000138185; -.
Orphanet; 401810; Autosomal recessive spastic paraplegia type 64.
PharmGKB; PA27798; -.
eggNOG; KOG1386; Eukaryota.
eggNOG; COG5371; LUCA.
GeneTree; ENSGT00550000074435; -.
HOGENOM; HOG000059572; -.
HOVERGEN; HBG018982; -.
InParanoid; P49961; -.
KO; K01510; -.
OMA; KPSYFWK; -.
OrthoDB; EOG091G05FZ; -.
PhylomeDB; P49961; -.
TreeFam; TF332859; -.
BioCyc; MetaCyc:HS06471-MONOMER; -.
Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
ChiTaRS; ENTPD1; human.
GeneWiki; ENTPD1; -.
GenomeRNAi; 953; -.
PRO; PR:P49961; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138185; -.
CleanEx; HS_ENTPD1; -.
ExpressionAtlas; P49961; baseline and differential.
Genevisible; P49961; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0017110; F:nucleoside-diphosphatase activity; EXP:Reactome.
GO; GO:0017111; F:nucleoside-triphosphatase activity; EXP:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
InterPro; IPR000407; GDA1_CD39_NTPase.
PANTHER; PTHR11782; PTHR11782; 1.
Pfam; PF01150; GDA1_CD39; 1.
PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hereditary spastic paraplegia; Hydrolase; Lipoprotein;
Magnesium; Membrane; Neurodegeneration; Nucleotide-binding; Palmitate;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 510 Ectonucleoside triphosphate
diphosphohydrolase 1.
/FTId=PRO_0000209902.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 478 Extracellular. {ECO:0000255}.
TRANSMEM 479 499 Helical. {ECO:0000255}.
TOPO_DOM 500 510 Cytoplasmic. {ECO:0000255}.
ACT_SITE 174 174 Proton acceptor. {ECO:0000250}.
LIPID 13 13 S-palmitoyl cysteine.
{ECO:0000305|PubMed:10636909}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 84 108 {ECO:0000250}.
DISULFID 255 301 {ECO:0000250}.
DISULFID 282 325 {ECO:0000250}.
DISULFID 338 343 {ECO:0000250}.
DISULFID 390 413 {ECO:0000250}.
VAR_SEQ 1 138 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_044284.
VAR_SEQ 1 108 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044283.
VAR_SEQ 1 5 MEDTK -> MGREELFLTFSFSSGFQ (in isoform
6). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_046050.
VAR_SEQ 1 4 MEDT -> MKGTKDLTSQQ (in isoform 2 and
isoform 3).
{ECO:0000303|PubMed:10405171}.
/FTId=VSP_003607.
VAR_SEQ 272 299 VASNEILRDPCFHPGYKKVVNVSDLYKT -> ASITQSRPA
PFTSAPPAPTSCCFLFQIQ (in isoform 3).
{ECO:0000303|PubMed:10405171}.
/FTId=VSP_003608.
VAR_SEQ 300 510 Missing (in isoform 3).
{ECO:0000303|PubMed:10405171}.
/FTId=VSP_003609.
VARIANT 210 210 G -> R (in SPG64).
{ECO:0000269|PubMed:24482476}.
/FTId=VAR_071082.
VARIANT 293 293 V -> I (in dbSNP:rs3793744).
/FTId=VAR_022099.
CONFLICT 57 58 SS -> G (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 162 162 D -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 208 208 T -> TGET (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 248 248 V -> Y (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 481 481 M -> I (in Ref. 4; BAG62981).
{ECO:0000305}.
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


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