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Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 (E-NPP 1) (Membrane component chromosome 6 surface marker 1) (Phosphodiesterase I/nucleotide pyrophosphatase 1) (Plasma-cell membrane glycoprotein PC-1) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 ENPP1_HUMAN             Reviewed;         925 AA.
P22413; Q5T9R6; Q9NPZ3; Q9P1P6; Q9UP61; Q9Y6K3;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
22-NOV-2017, entry version 195.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1;
Short=E-NPP 1;
AltName: Full=Membrane component chromosome 6 surface marker 1;
AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 1;
AltName: Full=Plasma-cell membrane glycoprotein PC-1;
Includes:
RecName: Full=Alkaline phosphodiesterase I;
EC=3.1.4.1 {ECO:0000269|PubMed:8001561};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000269|PubMed:8001561};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=ENPP1; Synonyms=M6S1, NPPS, PC1, PDNP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin fibroblast;
PubMed=2211644;
Buckley M.F., Loveland K.A., McKinstry W.J., Garson O.M., Goding J.W.;
"Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human
molecule, amino acid sequence, and chromosomal location.";
J. Biol. Chem. 265:17506-17511(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Skin fibroblast;
PubMed=1315502; DOI=10.1016/0003-9861(92)90504-P;
Funakoshi I., Kato H., Horie K., Yano T., Hori Y., Kobayashi H.,
Inoue T., Suzuki H., Fukui S., Tsukahara M., Kajii T., Yamashina I.;
"Molecular cloning of cDNAs for human fibroblast nucleotide
pyrophosphatase.";
Arch. Biochem. Biophys. 295:180-187(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Bozzali M., Pizzuti A., Trischitta E.;
"Genomic structure of the human PC1 gene.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-185, AND VARIANT GLN-173.
PubMed=10480624; DOI=10.2337/diabetes.48.9.1881;
Pizzuti A., Frittitta L., Argiolas A., Baratta R., Goldfine I.D.,
Bozzali M., Ercolino T., Scarlato G., Iacoviello L., Vigneri R.,
Tassi V., Trischitta V.;
"A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding
region is strongly associated with insulin resistance.";
Diabetes 48:1881-1884(1999).
[7]
SUBCELLULAR LOCATION, TOPOLOGY, CATALYTIC ACTIVITY, FUNCTION, AND
GLYCOSYLATION.
PubMed=8001561; DOI=10.1111/j.1432-1033.1994.tb20068.x;
Belli S.I., Goding J.W.;
"Biochemical characterization of human PC-1, an enzyme possessing
alkaline phosphodiesterase I and nucleotide pyrophosphatase
activities.";
Eur. J. Biochem. 226:433-443(1994).
[8]
ACTIVE SITE.
PubMed=7737162; DOI=10.1111/j.1432-1033.1995.tb20308.x;
Belli S.I., Mercuri F.A., Sali A., Goding J.W.;
"Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide
pyrophosphatase) and analysis of the active site.";
Eur. J. Biochem. 228:669-676(1995).
[9]
TISSUE SPECIFICITY.
PubMed=9344668; DOI=10.1006/geno.1997.4949;
Piao J.-H., Goding J.W., Nakamura H., Sano K.;
"Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a
new member of the human phosphodiesterase I genes.";
Genomics 45:412-415(1997).
[10]
INTERACTION WITH INSR, AND FUNCTION IN INHIBITION OF INSR KINASE
ACTIVITY.
PubMed=10615944; DOI=10.2337/diabetes.49.1.13;
Maddux B.A., Goldfine I.D.;
"Membrane glycoprotein PC-1 inhibition of insulin receptor function
occurs via direct interaction with the receptor alpha-subunit.";
Diabetes 49:13-19(2000).
[11]
CHARACTERIZATION, AND SUBCELLULAR LOCATION.
PubMed=11598187; DOI=10.1091/mbc.12.10.3004;
Bello V., Goding J.W., Greengrass V., Sali A., Dubljevic V.,
Lenoir C., Trugnan G., Maurice M.;
"Characterization of a di-leucine-based signal in the cytoplasmic tail
of the nucleotide-pyrophosphatase NPP1 that mediates basolateral
targeting but not endocytosis.";
Mol. Biol. Cell 12:3004-3015(2001).
[12]
SUBCELLULAR LOCATION.
PubMed=15072822; DOI=10.1016/j.canlet.2003.11.002;
Yano Y., Hayashi Y., Sano K., Nagano H., Nakaji M., Seo Y.,
Ninomiya T., Yoon S., Yokozaki H., Kasuga M.;
"Expression and localization of ecto-nucleotide
pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-
NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic
bile duct diseases.";
Cancer Lett. 207:139-147(2004).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-341.
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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-341; ASN-643 AND ASN-748.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
STRUCTURE BY NMR OF 147-189.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the somatomedin B domain of human
ectonucleotide pyrophosphatase/phosphodiesterase family member.";
Submitted (OCT-2007) to the PDB data bank.
[17]
VARIANTS OPLL PRO-91 AND PHE-287, AND VARIANTS GLN-173; HIS-268 AND
PRO-779.
PubMed=10453738; DOI=10.1007/s004390050993;
Nakamura I., Ikegawa S., Okawa A., Okuda S., Koshizuka Y.,
Kawaguchi H., Nakamura K., Koyama T., Goto S., Toguchida J.,
Matsushita M., Ochi T., Takaoka K., Nakamura Y.;
"Association of the human NPPS gene with ossification of the posterior
longitudinal ligament of the spine (OPLL).";
Hum. Genet. 104:492-497(1999).
[18]
VARIANT GACI1 PHE-579, AND VARIANT CYS-774.
PubMed=12881724; DOI=10.1038/ng1221;
Rutsch F., Ruf N., Vaingankar S., Toliat M.R., Suk A., Hohne W.,
Schauer G., Lehmann M., Roscioli T., Schnabel D., Epplen J.T.,
Knisely A., Superti-Furga A., McGill J., Filippone M., Sinaiko A.R.,
Vallance H., Hinrichs B., Smith W., Ferre M., Terkeltaub R.,
Nuernberg P.;
"Mutations in ENPP1 are associated with 'idiopathic' infantile
arterial calcification.";
Nat. Genet. 34:379-381(2003).
[19]
VARIANTS GACI1 VAL-342 AND PHE-371.
PubMed=15940697; DOI=10.1002/ajmg.a.30800;
Cheng K.-S., Chen M.-R., Ruf N., Lin S.-P., Rutsch F.;
"Generalized arterial calcification of infancy: different clinical
courses in two affected siblings.";
Am. J. Med. Genet. A 136:210-213(2005).
[20]
VARIANT GLN-173, AND INVOLVEMENT IN NIDDM.
PubMed=16186408; DOI=10.2337/diabetes.54.10.3021;
Bacci S., Ludovico O., Prudente S., Zhang Y.Y., Di Paola R.,
Mangiacotti D., Rauseo A., Nolan D., Duffy J., Fini G., Salvemini L.,
Amico C., Vigna C., Pellegrini F., Menzaghi C., Doria A.,
Trischitta V.;
"The K121Q polymorphism of the ENPP1/PC-1 gene is associated with
insulin resistance/atherogenic phenotypes, including earlier onset of
type 2 diabetes and myocardial infarction.";
Diabetes 54:3021-3025(2005).
[21]
VARIANTS GACI1 LEU-250; TYR-252 DEL; THR-305; VAL-342 AND PHE-371, AND
VARIANT CYS-774.
PubMed=15605415; DOI=10.1002/humu.9297;
Ruf N., Uhlenberg B., Terkeltaub R., Nurnberg P., Rutsch F.;
"The mutational spectrum oENPP1 as arising after the analysis of 23
unrelated patients with generalized arterial calcification of infancy
(GACI).";
Hum. Mutat. 25:98-98(2005).
[22]
VARIANTS GACI1 ARG-126; TYR-216; GLU-242; LEU-250; ASN-276; THR-305;
VAL-342; LYS-349; PHE-371; GLN-456; CYS-471; TRP-481; PRO-500;
ARG-504; CYS-513; CYS-570; PHE-579; CYS-659; ARG-726; ARG-777;
SER-792; HIS-804 AND TRP-888, AND VARIANTS VAL-611; LYS-668; CYS-774
AND HIS-821.
PubMed=20016754; DOI=10.1161/CIRCGENETICS.108.797704;
GACI Study Group;
Rutsch F., Boeyer P., Nitschke Y., Ruf N., Lorenz-Depierieux B.,
Wittkampf T., Weissen-Plenz G., Fischer R.J., Mughal Z., Gregory J.W.,
Davies J.H., Loirat C., Strom T.M., Schnabel D., Nuernberg P.,
Terkeltaub R.;
"Hypophosphatemia, hyperphosphaturia, and bisphosphonate treatment are
associated with survival beyond infancy in generalized arterial
calcification of infancy.";
Circ. Cardiovasc. Genet. 1:133-140(2008).
[23]
VARIANT ARHR2 VAL-266.
PubMed=20137773; DOI=10.1016/j.ajhg.2010.01.006;
Lorenz-Depiereux B., Schnabel D., Tiosano D., Hausler G., Strom T.M.;
"Loss-of-function ENPP1 mutations cause both generalized arterial
calcification of infancy and autosomal-recessive hypophosphatemic
rickets.";
Am. J. Hum. Genet. 86:267-272(2010).
[24]
VARIANT ARHR2 SER-901, AND CHARACTERIZATION OF VARIANT ARHR2 SER-901.
PubMed=20137772; DOI=10.1016/j.ajhg.2010.01.010;
Levy-Litan V., Hershkovitz E., Avizov L., Leventhal N., Bercovich D.,
Chalifa-Caspi V., Manor E., Buriakovsky S., Hadad Y., Goding J.,
Parvari R.;
"Autosomal-recessive hypophosphatemic rickets is associated with an
inactivation mutation in the ENPP1 gene.";
Am. J. Hum. Genet. 86:273-278(2010).
[25]
VARIANT GLN-173.
PubMed=20034067; DOI=10.1002/ajmg.a.33162;
Le Boulanger G., Labreze C., Croue A., Schurgers L.J., Chassaing N.,
Wittkampf T., Rutsch F., Martin L.;
"An unusual severe vascular case of pseudoxanthoma elasticum
presenting as generalized arterial calcification of infancy.";
Am. J. Med. Genet. A 152:118-123(2010).
[26]
VARIANT GACI1 VAL-218.
PubMed=23430823; DOI=10.1007/8904_2011_11;
Galletti S., Nitschke Y., Malavolti A.M., Aquilano G., Faldella G.,
Corvaglia L., Rutsch F.;
"Generalized arterial calcification of infancy: fatal clinical course
associated with a novel mutation in ENPP1.";
JIMD Rep. 1:23-27(2011).
[27]
VARIANTS GACI1 HIS-538 AND ARG-586.
PubMed=22209248; DOI=10.1016/j.ajhg.2011.11.020;
Nitschke Y., Baujat G., Botschen U., Wittkampf T., du Moulin M.,
Stella J., Le Merrer M., Guest G., Lambot K.,
Tazarourte-Pinturier M.F., Chassaing N., Roche O., Feenstra I.,
Loechner K., Deshpande C., Garber S.J., Chikarmane R., Steinmann B.,
Shahinyan T., Martorell L., Davies J., Smith W.E., Kahler S.G.,
McCulloch M., Wraige E., Loidi L., Hohne W., Martin L., Hadj-Rabia S.,
Terkeltaub R., Rutsch F.;
"Generalized arterial calcification of infancy and pseudoxanthoma
elasticum can be caused by mutations in either ENPP1 or ABCC6.";
Am. J. Hum. Genet. 90:25-39(2012).
[28]
VARIANTS COLED SER-149; SER-164 AND TYR-177.
PubMed=24075184; DOI=10.1016/j.ajhg.2013.08.007;
Eytan O., Morice-Picard F., Sarig O., Ezzedine K., Isakov O., Li Q.,
Ishida-Yamamoto A., Shomron N., Goldsmith T., Fuchs-Telem D., Adir N.,
Uitto J., Orlow S.J., Taieb A., Sprecher E.;
"Cole disease results from mutations in ENPP1.";
Am. J. Hum. Genet. 93:752-757(2013).
[29]
VARIANTS ARHR2 ASP-92; ARG-219 AND SER-792, AND INVOLVEMENT IN ARHR2.
PubMed=25741938; DOI=10.1515/jpem-2014-0531;
Steichen-Gersdorf E., Lorenz-Depiereux B., Strom T.M., Shaw N.J.;
"Early onset hearing loss in autosomal recessive hypophosphatemic
rickets caused by loss of function mutation in ENPP1.";
J. Pediatr. Endocrinol. Metab. 28:967-970(2015).
[30]
VARIANTS COLED ARG-133 AND SER-177.
PubMed=26617416; DOI=10.1111/bjd.14328;
Schlipf N.A., Traupe H., Gilaberte Y., Peitsch W.K., Hausser I.,
Oji V., Schmieder A., Schneider S.W., Demmer P., Roesler B.,
Fischer J.;
"Association of Cole disease with novel heterozygous mutations in the
somatomedin-B domains of the ENPP1 gene: necessary, but not always
sufficient.";
Br. J. Dermatol. 174:1152-1156(2016).
[31]
VARIANTS GACI1 ARG-195; SER-195 AND CYS-301, CHARACTERIZATION OF
VARIANTS GLN-173; LYS-668; CYS-774 AND HIS-821, CHARACTERIZATION OF
VARIANTS GACI1 ARG-195; SER-195; CYS-301; THR-305; CYS-471; ARG-504;
CYS-513; HIS-538; ARG-586; CYS-659; ARG-777 AND TRP-888, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=27467858; DOI=10.1002/humu.23057;
Stella J., Buers I., van de Wetering K., Hoehne W., Rutsch F.,
Nitschke Y.;
"Effects of Different Variants in the ENPP1 Gene on the Functional
Properties of Ectonucleotide Pyrophosphatase/Phosphodiesterase Family
Member 1.";
Hum. Mutat. 37:1190-1201(2016).
-!- FUNCTION: By generating PPi, plays a role in regulating
pyrophosphate levels, and functions in bone mineralization and
soft tissue calcification. PPi inhibits mineralization by binding
to nascent hydroxyapatite (HA) crystals, thereby preventing
further growth of these crystals. Preferentially hydrolyzes ATP,
but can also hydrolyze other nucleoside 5' triphosphates such as
GTP, CTP, TTP and UTP to their corresponding monophosphates with
release of pyrophosphate and diadenosine polyphosphates, and also
3',5'-cAMP to AMP. May also be involved in the regulation of the
availability of nucleotide sugars in the endoplasmic reticulum and
Golgi, and the regulation of purinergic signaling. Appears to
modulate insulin sensitivity and function.
{ECO:0000269|PubMed:10615944, ECO:0000269|PubMed:27467858,
ECO:0000269|PubMed:8001561}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000269|PubMed:8001561}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000269|PubMed:8001561}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P06802};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:P06802};
-!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
intermediate is formed which inhibits further hydrolysis.
-!- SUBUNIT: The secreted form is monomeric (By similarity).
Homodimer. Interacts with INSR. {ECO:0000250,
ECO:0000269|PubMed:10615944}.
-!- INTERACTION:
P06213:INSR; NbExp=2; IntAct=EBI-3197846, EBI-475899;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27467858};
Single-pass type II membrane protein. Basolateral cell membrane;
Single-pass type II membrane protein. Secreted {ECO:0000250}.
Note=The proteolytically processed form is secreted (By
similarity). Targeted to the basolateral membrane in polarized
epithelial cells and in hepatocytes, and to matrix vesicles in
osteoblasts. In bile duct cells and cancer cells, located to the
apical cytoplasmic side. {ECO:0000250,
ECO:0000269|PubMed:11598187, ECO:0000269|PubMed:15072822,
ECO:0000269|PubMed:8001561}.
-!- TISSUE SPECIFICITY: Expressed in plasma cells and also in a number
of non-lymphoid tissues, including the distal convoluted tubule of
the kidney, chondrocytes and epididymis.
{ECO:0000269|PubMed:9344668}.
-!- DOMAIN: The di-leucine motif is required for basolateral targeting
in epithelial cells, and for targeting to matrix vesicles derived
from mineralizing cells. {ECO:0000250}.
-!- PTM: Autophosphorylated as part of the catalytic cycle of
phosphodiesterase/pyrophosphatase activity.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:8001561}.
-!- PTM: A secreted form is produced through cleavage at Lys-103 by
intracellular processing. {ECO:0000250|UniProtKB:P06802}.
-!- DISEASE: Ossification of the posterior longitudinal ligament of
the spine (OPLL) [MIM:602475]: A calcification of the posterior
longitudinal ligament of the spinal column, usually at the level
of the cervical spine. Patients with OPLL frequently present with
a severe myelopathy that can lead to tetraparesis.
{ECO:0000269|PubMed:10453738}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arterial calcification of infancy, generalized, 1 (GACI1)
[MIM:208000]: A severe autosomal recessive disorder characterized
by calcification of the internal elastic lamina of muscular
arteries and stenosis due to myointimal proliferation. The
disorder is often fatal within the first 6 months of life because
of myocardial ischemia resulting in refractory heart failure.
{ECO:0000269|PubMed:12881724, ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:15940697, ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:22209248, ECO:0000269|PubMed:23430823,
ECO:0000269|PubMed:27467858}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16186408}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Hypophosphatemic rickets, autosomal recessive, 2 (ARHR2)
[MIM:613312]: A hereditary form of hypophosphatemic rickets, a
disorder of proximal renal tubule function that causes phosphate
loss, hypophosphatemia and skeletal deformities, including rickets
and osteomalacia unresponsive to vitamin D. Symptoms are bone
pain, fractures and growth abnormalities.
{ECO:0000269|PubMed:20137772, ECO:0000269|PubMed:20137773,
ECO:0000269|PubMed:25741938}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cole disease (COLED) [MIM:615522]: A rare autosomal
dominant genodermatosis characterized by punctate keratoderma
associated with irregularly shaped hypopigmented macules, which
are typically found over the arms and legs but not the trunk or
acral regions. Skin biopsies of palmoplantar lesions show
hyperorthokeratosis, hypergranulosis, and acanthosis.
Hypopigmented areas of skin, however, reveal a reduction in
melanin content in keratinocytes but not in melanocytes, as well
as hyperkeratosis and a normal number of melanocytes.
Ultrastructurally, melanocytes show a disproportionately large
number of melanosomes in the cytoplasm and dendrites, whereas
keratinocytes show a paucity of these organelles, suggestive of
impaired melanosome transfer. Some patients also exhibit
calcinosis cutis or calcific tendinopathy.
{ECO:0000269|PubMed:24075184, ECO:0000269|PubMed:26617416}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-53 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA63237.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH59375.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA02054.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M57736; AAA63237.1; ALT_INIT; mRNA.
EMBL; D12485; BAA02054.1; ALT_INIT; mRNA.
EMBL; AF110304; AAF36094.1; -; Genomic_DNA.
EMBL; AF110280; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110281; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110283; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110284; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110285; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110286; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110287; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110288; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110289; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110290; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110291; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110292; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110293; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110294; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110295; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110296; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110297; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110298; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110299; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110300; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110301; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110302; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AF110303; AAF36094.1; JOINED; Genomic_DNA.
EMBL; AJ242020; CAC39442.1; -; Genomic_DNA.
EMBL; AJ242021; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242022; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242023; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242024; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242025; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242026; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242027; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242028; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242029; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242030; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242031; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242032; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242033; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242034; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242035; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242036; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242037; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242038; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242039; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242040; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242041; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242042; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242043; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AJ242044; CAC39442.1; JOINED; Genomic_DNA.
EMBL; AL117378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC059375; AAH59375.2; ALT_INIT; mRNA.
EMBL; AF067177; AAD38420.1; -; Genomic_DNA.
EMBL; AF067178; AAD38421.1; -; Genomic_DNA.
CCDS; CCDS5150.2; -.
PIR; A39216; A39216.
RefSeq; NP_006199.2; NM_006208.2.
UniGene; Hs.527295; -.
PDB; 2YS0; NMR; -; A=147-189.
PDBsum; 2YS0; -.
ProteinModelPortal; P22413; -.
SMR; P22413; -.
BioGrid; 111193; 15.
IntAct; P22413; 4.
STRING; 9606.ENSP00000354238; -.
BindingDB; P22413; -.
ChEMBL; CHEMBL5925; -.
DrugBank; DB01143; Amifostine.
DrugBank; DB00811; Ribavirin.
iPTMnet; P22413; -.
PhosphoSitePlus; P22413; -.
BioMuta; ENPP1; -.
DMDM; 23503088; -.
EPD; P22413; -.
MaxQB; P22413; -.
PaxDb; P22413; -.
PeptideAtlas; P22413; -.
PRIDE; P22413; -.
Ensembl; ENST00000360971; ENSP00000354238; ENSG00000197594.
GeneID; 5167; -.
KEGG; hsa:5167; -.
UCSC; uc011ecf.2; human.
CTD; 5167; -.
DisGeNET; 5167; -.
EuPathDB; HostDB:ENSG00000197594.11; -.
GeneCards; ENPP1; -.
HGNC; HGNC:3356; ENPP1.
HPA; CAB032904; -.
HPA; HPA062066; -.
MalaCards; ENPP1; -.
MIM; 125853; phenotype.
MIM; 173335; gene.
MIM; 208000; phenotype.
MIM; 602475; phenotype.
MIM; 613312; phenotype.
MIM; 615522; phenotype.
neXtProt; NX_P22413; -.
OpenTargets; ENSG00000197594; -.
Orphanet; 289176; Autosomal recessive hypophosphatemic rickets.
Orphanet; 51608; Generalized arterial calcification of infancy.
Orphanet; 324561; Hypopigmentation-punctate palmoplantar keratoderma syndrome.
PharmGKB; PA27791; -.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
GeneTree; ENSGT00760000119157; -.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; P22413; -.
KO; K01513; -.
OMA; HFFIVLT; -.
OrthoDB; EOG091G017X; -.
PhylomeDB; P22413; -.
TreeFam; TF330032; -.
BRENDA; 3.6.1.9; 2681.
Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
SABIO-RK; P22413; -.
SIGNOR; P22413; -.
EvolutionaryTrace; P22413; -.
GeneWiki; Ectonucleotide_pyrophosphatase/phosphodiesterase_1; -.
GenomeRNAi; 5167; -.
PRO; PR:P22413; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000197594; -.
CleanEx; HS_ENPP1; -.
ExpressionAtlas; P22413; baseline and differential.
Genevisible; P22413; HS.
GO; GO:0016323; C:basolateral plasma membrane; NAS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IC:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004527; F:exonuclease activity; IDA:UniProtKB.
GO; GO:0005158; F:insulin receptor binding; IDA:BHF-UCL.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:BHF-UCL.
GO; GO:0004551; F:nucleotide diphosphatase activity; IDA:BHF-UCL.
GO; GO:0004528; F:phosphodiesterase I activity; IDA:UniProtKB.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:BHF-UCL.
GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0030643; P:cellular phosphate ion homeostasis; IDA:BHF-UCL.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0006091; P:generation of precursor metabolites and energy; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0030505; P:inorganic diphosphate transport; IDA:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:BHF-UCL.
GO; GO:0046325; P:negative regulation of glucose import; IDA:BHF-UCL.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; IDA:BHF-UCL.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:BHF-UCL.
GO; GO:0030500; P:regulation of bone mineralization; IC:BHF-UCL.
GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
GO; GO:0030730; P:sequestering of triglyceride; IDA:BHF-UCL.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR020436; Somatomedin_B_chordata.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
PRINTS; PR00022; SOMATOMEDINB.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 2.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 2.
PROSITE; PS00524; SMB_1; 2.
PROSITE; PS50958; SMB_2; 2.
1: Evidence at protein level;
3D-structure; Biomineralization; Calcium; Cell membrane;
Complete proteome; Diabetes mellitus; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Obesity; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 925 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 1.
/FTId=PRO_0000188564.
TOPO_DOM 1 76 Cytoplasmic. {ECO:0000255}.
TRANSMEM 77 97 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 98 925 Extracellular. {ECO:0000255}.
DOMAIN 104 144 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 145 189 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 191 591 Phosphodiesterase.
REGION 597 647 Linker. {ECO:0000250}.
REGION 654 925 Nuclease.
MOTIF 45 52 Di-leucine motif.
ACT_SITE 256 256 AMP-threonine intermediate.
{ECO:0000250|UniProtKB:P06802}.
METAL 218 218 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 256 256 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 376 376 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 380 380 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 423 423 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 424 424 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 535 535 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:P06802}.
METAL 800 800 Calcium. {ECO:0000250|UniProtKB:P06802}.
METAL 802 802 Calcium. {ECO:0000250|UniProtKB:P06802}.
METAL 804 804 Calcium. {ECO:0000250|UniProtKB:P06802}.
METAL 806 806 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P06802}.
METAL 808 808 Calcium. {ECO:0000250|UniProtKB:P06802}.
BINDING 277 277 Substrate.
{ECO:0000250|UniProtKB:P06802}.
BINDING 295 295 Substrate.
{ECO:0000250|UniProtKB:P06802}.
BINDING 340 340 Substrate.
{ECO:0000250|UniProtKB:P06802}.
SITE 102 103 Cleavage. {ECO:0000250|UniProtKB:P06802}.
SITE 915 915 Essential for catalytic activity.
{ECO:0000250}.
MOD_RES 256 256 Phosphothreonine.
{ECO:0000250|UniProtKB:Q924C3}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 585 585 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 643 643 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 700 700 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 731 731 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 748 748 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 108 122 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 112 140 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 120 133 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 126 132 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 149 166 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 154 184 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 164 177 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 170 176 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 195 241 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 203 415 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 431 530 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 480 868 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 614 672 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 626 726 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 628 711 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 838 848 {ECO:0000255|PROSITE-ProRule:PRU00350}.
VARIANT 91 91 L -> P (in OPLL).
{ECO:0000269|PubMed:10453738}.
/FTId=VAR_014141.
VARIANT 92 92 G -> D (in ARHR2).
{ECO:0000269|PubMed:25741938}.
/FTId=VAR_077255.
VARIANT 126 126 C -> R (in GACI1).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077256.
VARIANT 133 133 C -> R (in COLED).
{ECO:0000269|PubMed:26617416}.
/FTId=VAR_077257.
VARIANT 149 149 C -> S (in COLED; dbSNP:rs397518477).
{ECO:0000269|PubMed:24075184}.
/FTId=VAR_070782.
VARIANT 164 164 C -> S (in COLED; dbSNP:rs397518476).
{ECO:0000269|PubMed:24075184}.
/FTId=VAR_070783.
VARIANT 173 173 K -> Q (polymorphism; associated with
NIDDM; decreased nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs1044498).
{ECO:0000269|PubMed:10453738,
ECO:0000269|PubMed:10480624,
ECO:0000269|PubMed:16186408,
ECO:0000269|PubMed:20034067,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_008873.
VARIANT 177 177 C -> S (in COLED).
{ECO:0000269|PubMed:26617416}.
/FTId=VAR_077258.
VARIANT 177 177 C -> Y (in COLED; dbSNP:rs397518475).
{ECO:0000269|PubMed:24075184}.
/FTId=VAR_070784.
VARIANT 179 179 N -> S (in dbSNP:rs2273411).
/FTId=VAR_037432.
VARIANT 195 195 C -> R (in GACI1; loss of nucleotide
phosphodiesterase activity; loss of
localization to plasma membrane;
dbSNP:rs763457176).
{ECO:0000269|PubMed:27467858}.
/FTId=VAR_077259.
VARIANT 195 195 C -> S (in GACI1; loss of nucleotide
phosphodiesterase activity; loss of
localization to plasma membrane).
{ECO:0000269|PubMed:27467858}.
/FTId=VAR_077260.
VARIANT 216 216 S -> Y (in GACI1; unknown pathological
significance; dbSNP:rs760786509).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077261.
VARIANT 218 218 D -> V (in GACI1).
{ECO:0000269|PubMed:23430823}.
/FTId=VAR_077262.
VARIANT 219 219 G -> R (in ARHR2; unknown pathological
significance).
{ECO:0000269|PubMed:25741938}.
/FTId=VAR_077263.
VARIANT 242 242 G -> E (in GACI1; unknown pathological
significance).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077264.
VARIANT 250 250 P -> L (in GACI1; unknown pathological
significance; dbSNP:rs754659608).
{ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:20016754}.
/FTId=VAR_067910.
VARIANT 252 252 Missing (in GACI1).
{ECO:0000269|PubMed:15605415}.
/FTId=VAR_067911.
VARIANT 266 266 G -> V (in ARHR2; dbSNP:rs121908248).
{ECO:0000269|PubMed:20137773}.
/FTId=VAR_063719.
VARIANT 268 268 Y -> H (in dbSNP:rs17847050).
{ECO:0000269|PubMed:10453738}.
/FTId=VAR_014142.
VARIANT 276 276 D -> N (in GACI1; unknown pathological
significance; dbSNP:rs143771474).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077265.
VARIANT 287 287 S -> F (in OPLL; dbSNP:rs190947144).
{ECO:0000269|PubMed:10453738}.
/FTId=VAR_014143.
VARIANT 301 301 Y -> C (in GACI1; loss of nucleotide
phosphodiesterase activity; loss of
localization to plasma membrane).
{ECO:0000269|PubMed:27467858}.
/FTId=VAR_077266.
VARIANT 305 305 P -> T (in GACI1; loss of nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs374270497).
{ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_067912.
VARIANT 342 342 G -> V (in GACI1; dbSNP:rs121918025).
{ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:15940697,
ECO:0000269|PubMed:20016754}.
/FTId=VAR_037433.
VARIANT 349 349 R -> K (in GACI1; unknown pathological
significance; dbSNP:rs764735802).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077267.
VARIANT 371 371 Y -> F (in GACI1; unknown pathological
significance; dbSNP:rs121918026).
{ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:15940697,
ECO:0000269|PubMed:20016754}.
/FTId=VAR_037434.
VARIANT 456 456 R -> Q (in GACI1; dbSNP:rs765071179).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077268.
VARIANT 471 471 Y -> C (in GACI1; decreased nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs148462924).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077269.
VARIANT 481 481 R -> W (in GACI1; unknown pathological
significance; dbSNP:rs373044722).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077270.
VARIANT 500 500 H -> P (in GACI1).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077271.
VARIANT 504 504 S -> R (in GACI1; decreased nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077272.
VARIANT 513 513 Y -> C (in GACI1; loss of nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077273.
VARIANT 538 538 D -> H (in GACI1; loss of nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs387906673).
{ECO:0000269|PubMed:22209248,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_067913.
VARIANT 570 570 Y -> C (in GACI1; dbSNP:rs140248167).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077274.
VARIANT 579 579 L -> F (in GACI1; unknown pathological
significance; dbSNP:rs121918024).
{ECO:0000269|PubMed:12881724,
ECO:0000269|PubMed:20016754}.
/FTId=VAR_018514.
VARIANT 586 586 G -> R (in GACI1; loss of nucleotide
phosphodiesterase activity; loss of
localization to plasma membrane).
{ECO:0000269|PubMed:22209248,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_067914.
VARIANT 611 611 L -> V (in dbSNP:rs79079368).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077275.
VARIANT 659 659 Y -> C (in GACI1; decreased nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs143393727).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077276.
VARIANT 668 668 E -> K (polymorphism; no effect on
nucleotide phosphodiesterase activity; no
effect on localization to plasma
membrane; dbSNP:rs115371819).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077277.
VARIANT 726 726 C -> R (in GACI1).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077278.
VARIANT 774 774 R -> C (polymorphism; decreased
nucleotide phosphodiesterase activity; no
effect on localization to plasma
membrane; dbSNP:rs28933977).
{ECO:0000269|PubMed:12881724,
ECO:0000269|PubMed:15605415,
ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_018515.
VARIANT 777 777 H -> R (in GACI1; decreased nucleotide
phosphodiesterase activity; no effect on
localization to plasma membrane;
dbSNP:rs147346173).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077279.
VARIANT 779 779 T -> P (in dbSNP:rs1805138).
{ECO:0000269|PubMed:10453738}.
/FTId=VAR_014144.
VARIANT 792 792 N -> S (in ARHR2 and GACI1;
dbSNP:rs370184526).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:25741938}.
/FTId=VAR_077280.
VARIANT 804 804 D -> H (in GACI1).
{ECO:0000269|PubMed:20016754}.
/FTId=VAR_077281.
VARIANT 821 821 R -> H (polymorphism; decreased
nucleotide phosphodiesterase activity; no
effect on localization to plasma
membrane; dbSNP:rs367759638).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077282.
VARIANT 886 886 R -> T (in dbSNP:rs8192683).
/FTId=VAR_037435.
VARIANT 888 888 R -> W (in GACI1; loss of nucleotide
phosphodiesterase activity; loss of
localization to plasma membrane;
dbSNP:rs184483616).
{ECO:0000269|PubMed:20016754,
ECO:0000269|PubMed:27467858}.
/FTId=VAR_077283.
VARIANT 901 901 Y -> S (in ARHR2; loss of activity;
dbSNP:rs121908249).
{ECO:0000269|PubMed:20137772}.
/FTId=VAR_063720.
TURN 151 155 {ECO:0000244|PDB:2YS0}.
STRAND 163 165 {ECO:0000244|PDB:2YS0}.
HELIX 168 173 {ECO:0000244|PDB:2YS0}.
HELIX 180 183 {ECO:0000244|PDB:2YS0}.
SEQUENCE 925 AA; 104924 MW; 0ECAA063801CAFEB CRC64;
MERDGCAGGG SRGGEGGRAP REGPAGNGRD RGRSHAAEAP GDPQAAASLL APMDVGEEPL
EKAARARTAK DPNTYKVLSL VLSVCVLTTI LGCIFGLKPS CAKEVKSCKG RCFERTFGNC
RCDAACVELG NCCLDYQETC IEPEHIWTCN KFRCGEKRLT RSLCACSDDC KDKGDCCINY
SSVCQGEKSW VEEPCESINE PQCPAGFETP PTLLFSLDGF RAEYLHTWGG LLPVISKLKK
CGTYTKNMRP VYPTKTFPNH YSIVTGLYPE SHGIIDNKMY DPKMNASFSL KSKEKFNPEW
YKGEPIWVTA KYQGLKSGTF FWPGSDVEIN GIFPDIYKMY NGSVPFEERI LAVLQWLQLP
KDERPHFYTL YLEEPDSSGH SYGPVSSEVI KALQRVDGMV GMLMDGLKEL NLHRCLNLIL
ISDHGMEQGS CKKYIYLNKY LGDVKNIKVI YGPAARLRPS DVPDKYYSFN YEGIARNLSC
REPNQHFKPY LKHFLPKRLH FAKSDRIEPL TFYLDPQWQL ALNPSERKYC GSGFHGSDNV
FSNMQALFVG YGPGFKHGIE ADTFENIEVY NLMCDLLNLT PAPNNGTHGS LNHLLKNPVY
TPKHPKEVHP LVQCPFTRNP RDNLGCSCNP SILPIEDFQT QFNLTVAEEK IIKHETLPYG
RPRVLQKENT ICLLSQHQFM SGYSQDILMP LWTSYTVDRN DSFSTEDFSN CLYQDFRIPL
SPVHKCSFYK NNTKVSYGFL SPPQLNKNSS GIYSEALLTT NIVPMYQSFQ VIWRYFHDTL
LRKYAEERNG VNVVSGPVFD FDYDGRCDSL ENLRQKRRVI RNQEILIPTH FFIVLTSCKD
TSQTPLHCEN LDTLAFILPH RTDNSESCVH GKHDSSWVEE LLMLHRARIT DVEHITGLSF
YQQRKEPVSD ILKLKTHLPT FSQED


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