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Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 ENPP3_HUMAN             Reviewed;         875 AA.
O14638; Q5JTL3;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
18-JUL-2018, entry version 160.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
Short=E-NPP 3;
Short=NPP3 {ECO:0000303|PubMed:29717535};
AltName: Full=Phosphodiesterase I beta {ECO:0000303|PubMed:9344668};
Short=PD-Ibeta {ECO:0000303|PubMed:9344668};
AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3;
AltName: CD_antigen=CD203c {ECO:0000303|PubMed:11342463, ECO:0000303|PubMed:29717535};
Includes:
RecName: Full=Alkaline phosphodiesterase I;
EC=3.1.4.1 {ECO:0000269|PubMed:11342463};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000269|PubMed:29717535};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=ENPP3; Synonyms=PDNP3 {ECO:0000303|PubMed:9344668};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Prostate;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
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).
[4]
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.
[5]
PROTEIN SEQUENCE OF 393-405, IDENTIFICATION AS CD203C, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=11342463; DOI=10.1182/blood.V97.10.3303;
Buehring H.J., Seiffert M., Giesert C., Marxer A., Kanz L., Valent P.,
Sano K.;
"The basophil activation marker defined by antibody 97A6 is identical
to the ectonucleotide pyrophosphatase/phosphodiesterase 3.";
Blood 97:3303-3305(2001).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[7]
INDUCTION, AND POSSIBLE APPLICATION IN ALLERGY DIAGNOSIS.
PubMed=15031605; DOI=10.1159/000077351;
Buehring H.J., Streble A., Valent P.;
"The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell
activation and allergy diagnosis.";
Int. Arch. Allergy Immunol. 133:317-329(2004).
[8]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 48-875 IN COMPLEX WITH ZINC
AND ATP ANALOG, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, COFACTOR, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF THR-179;
LYS-204; ASN-227; GLU-275 AND ALA-336, GLYCOSYLATION AT ASN-236;
ASN-279; ASN-290; ASN-426; ASN-533; ASN-582; ASN-594; ASN-687; ASN-699
AND ASN-789, AND DISULFIDE BOND.
PubMed=29717535; DOI=10.1111/febs.14489;
Gorelik A., Randriamihaja A., Illes K., Nagar B.;
"Structural basis for nucleotide recognition by the ectoenzyme
CD203c.";
FEBS J. 0:0-0(2018).
-!- FUNCTION: Hydrolase that metabolizes extracellular nucleotides,
including ATP, GTP, UTP and CTP (PubMed:29717535). Limits mast
cell and basophil responses during inflammation and during the
chronic phases of allergic responses by eliminating the
extracellular ATP that functions as signaling molecule and
activates basophils and mast cells and induces the release of
inflammatory cytokines. Metabolizes extracellular ATP in the lumen
of the small intestine, and thereby prevents ATP-induced apoptosis
of intestinal plasmacytoid dendritic cells (By similarity). Has
also alkaline phosphodiesterase activity (PubMed:11342463).
{ECO:0000250|UniProtKB:Q6DYE8, ECO:0000269|PubMed:11342463,
ECO:0000269|PubMed:29717535}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000269|PubMed:11342463}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000269|PubMed:29717535}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:29717535};
Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:29717535};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=61.5 uM for ATP;
KM=120.3 uM for UTP;
KM=120.2 uM for CTP;
KM=123.7 uM for GTP;
-!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:29717535}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11342463};
Single-pass type II membrane protein {ECO:0000305}. Apical cell
membrane {ECO:0000269|PubMed:15072822}; Single-pass type II
membrane protein {ECO:0000305}. Secreted
{ECO:0000269|PubMed:15072822}. Note=Detected at the cell surface
of basophils (PubMed:11342463). Detected at the apical plasma
membrane of bile duct cells (PubMed:15072822). Located to the
apical surface in intestinal and kidney epithelial cells. Secreted
in serum, and in lumen of epithelial cells.
{ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:15072822}.
-!- TISSUE SPECIFICITY: Detected on bile ducts in liver, and in blood
serum (at protein level) (PubMed:15072822). Detected in prostate
and uterus (PubMed:9344668). Detected on basophils, but not
neutrophils (PubMed:11342463). {ECO:0000269|PubMed:11342463,
ECO:0000269|PubMed:15072822, ECO:0000269|PubMed:9344668}.
-!- INDUCTION: Up-regulated by stimulation by allergen or by cross-
linking with IgE. The IgE-mediated activation is enhanced by
tetradecanoyl phorbol acetate (TPA), a stimulator of the PKC
pathway, and inhibited by the P13 kinase inhibitors, LY294002 and
wortmannin. Up-regulated in invasive bile duct cancers.
{ECO:0000269|PubMed:15031605}.
-!- PTM: N-glycosylated. N-glycosylation is necessary for normal
transport to the cell membrane, but is not the apical targeting
signal. {ECO:0000250|UniProtKB:P97675}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD05192.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF005632; AAC51813.1; -; mRNA.
EMBL; EF560735; ABQ59045.1; -; mRNA.
EMBL; AC005587; AAD05192.1; ALT_SEQ; Genomic_DNA.
EMBL; AL121575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48045.1; -; Genomic_DNA.
CCDS; CCDS5148.1; -.
RefSeq; NP_005012.2; NM_005021.4.
UniGene; Hs.486489; -.
PDB; 6C01; X-ray; 2.30 A; A/B=48-875.
PDB; 6C02; X-ray; 1.94 A; A/B=48-875.
PDBsum; 6C01; -.
PDBsum; 6C02; -.
ProteinModelPortal; O14638; -.
SMR; O14638; -.
BioGrid; 111195; 1.
IntAct; O14638; 1.
MINT; O14638; -.
STRING; 9606.ENSP00000350265; -.
BindingDB; O14638; -.
ChEMBL; CHEMBL5580; -.
iPTMnet; O14638; -.
PhosphoSitePlus; O14638; -.
BioMuta; ENPP3; -.
MaxQB; O14638; -.
PaxDb; O14638; -.
PeptideAtlas; O14638; -.
PRIDE; O14638; -.
ProteomicsDB; 48132; -.
DNASU; 5169; -.
Ensembl; ENST00000357639; ENSP00000350265; ENSG00000154269.
Ensembl; ENST00000414305; ENSP00000406261; ENSG00000154269.
GeneID; 5169; -.
KEGG; hsa:5169; -.
UCSC; uc003qcu.5; human.
CTD; 5169; -.
DisGeNET; 5169; -.
EuPathDB; HostDB:ENSG00000154269.14; -.
GeneCards; ENPP3; -.
HGNC; HGNC:3358; ENPP3.
HPA; HPA043772; -.
MIM; 602182; gene.
neXtProt; NX_O14638; -.
OpenTargets; ENSG00000154269; -.
PharmGKB; PA27793; -.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
GeneTree; ENSGT00760000119157; -.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; O14638; -.
KO; K01513; -.
OMA; WDYFHSV; -.
OrthoDB; EOG091G017X; -.
PhylomeDB; O14638; -.
TreeFam; TF330032; -.
BRENDA; 3.6.1.9; 2681.
Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
ChiTaRS; ENPP3; human.
GeneWiki; ENPP3; -.
GenomeRNAi; 5169; -.
PRO; PR:O14638; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000154269; -.
CleanEx; HS_ENPP3; -.
ExpressionAtlas; O14638; baseline and differential.
Genevisible; O14638; HS.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
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:UniProtKB.
GO; GO:0004528; F:phosphodiesterase I activity; IMP:UniProtKB.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; IDA:UniProtKB.
GO; GO:0002276; P:basophil activation involved in immune response; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISS:UniProtKB.
GO; GO:0070667; P:negative regulation of mast cell proliferation; ISS: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:0006220; P:pyrimidine nucleotide metabolic process; IMP:UniProtKB.
Gene3D; 3.40.720.10; -; 3.
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; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
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; Calcium; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Polymorphism; Reference proteome; Repeat;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 875 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 3.
/FTId=PRO_0000188570.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 875 Extracellular. {ECO:0000255}.
DOMAIN 50 93 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 94 138 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 140 510 Phosphodiesterase.
REGION 605 875 Nuclease.
MOTIF 78 80 Cell attachment site. {ECO:0000255}.
ACT_SITE 205 205 Nucleophile.
{ECO:0000305|PubMed:29717535}.
METAL 167 167 Zinc 1; catalytic. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 205 205 Zinc 1; catalytic. {ECO:0000244|PDB:6C01,
ECO:0000269|PubMed:29717535}.
METAL 325 325 Zinc 2; catalytic. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 329 329 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 372 372 Zinc 1; catalytic. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 373 373 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 483 483 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 752 752 Calcium. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 754 754 Calcium. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 756 756 Calcium. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 758 758 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
METAL 760 760 Calcium. {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
BINDING 204 204 Substrate. {ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
BINDING 226 226 Substrate. {ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
BINDING 275 275 Substrate. {ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
BINDING 289 289 Substrate. {ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C01,
ECO:0000269|PubMed:29717535}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C01,
ECO:0000269|PubMed:29717535}.
CARBOHYD 687 687 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:29717535}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
DISULFID 54 71 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 58 89 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 69 82 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 75 81 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 98 115 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 103 133 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 113 126 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 119 125 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 144 190 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 152 364 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 380 478 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 429 818 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 562 623 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000269|PubMed:29717535}.
DISULFID 575 679 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 577 664 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
DISULFID 787 797 {ECO:0000244|PDB:6C01,
ECO:0000244|PDB:6C02,
ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:29717535}.
VARIANT 620 620 V -> M (in dbSNP:rs9321309).
/FTId=VAR_018516.
VARIANT 744 744 N -> H (in dbSNP:rs36094194).
/FTId=VAR_046538.
VARIANT 786 786 S -> N (in dbSNP:rs17601580).
/FTId=VAR_031253.
MUTAGEN 179 179 T->C: Causes the formation of covalently
linked homodimers in solution; when
associated with C-336.
{ECO:0000269|PubMed:29717535}.
MUTAGEN 204 204 K->A: Strongly decreases affinity for
nucleotides and slows their hydrolysis.
{ECO:0000269|PubMed:29717535}.
MUTAGEN 227 227 N->A: No effect on affinity for
nucleotides and enzyme activity.
{ECO:0000269|PubMed:29717535}.
MUTAGEN 275 275 E->A: No effect on substrate specificity.
Increases affinity for nucleotides and
slows their hydrolysis.
{ECO:0000269|PubMed:29717535}.
MUTAGEN 336 336 A->C: Causes the formation of covalently
linked homodimers in solution; when
associated with C-179.
{ECO:0000269|PubMed:29717535}.
CONFLICT 122 122 R -> K (in Ref. 1; AAC51813).
{ECO:0000305}.
HELIX 66 68 {ECO:0000244|PDB:6C02}.
HELIX 75 78 {ECO:0000244|PDB:6C02}.
HELIX 85 89 {ECO:0000244|PDB:6C02}.
HELIX 91 93 {ECO:0000244|PDB:6C02}.
TURN 100 104 {ECO:0000244|PDB:6C02}.
STRAND 112 114 {ECO:0000244|PDB:6C02}.
HELIX 119 122 {ECO:0000244|PDB:6C02}.
HELIX 129 132 {ECO:0000244|PDB:6C02}.
TURN 139 141 {ECO:0000244|PDB:6C02}.
HELIX 149 151 {ECO:0000244|PDB:6C01}.
STRAND 161 166 {ECO:0000244|PDB:6C02}.
HELIX 171 176 {ECO:0000244|PDB:6C02}.
HELIX 178 180 {ECO:0000244|PDB:6C02}.
HELIX 182 190 {ECO:0000244|PDB:6C02}.
STRAND 191 195 {ECO:0000244|PDB:6C02}.
HELIX 205 214 {ECO:0000244|PDB:6C02}.
HELIX 218 221 {ECO:0000244|PDB:6C02}.
STRAND 225 230 {ECO:0000244|PDB:6C02}.
TURN 231 234 {ECO:0000244|PDB:6C02}.
STRAND 235 237 {ECO:0000244|PDB:6C02}.
HELIX 242 245 {ECO:0000244|PDB:6C02}.
HELIX 247 249 {ECO:0000244|PDB:6C02}.
HELIX 255 261 {ECO:0000244|PDB:6C02}.
STRAND 266 270 {ECO:0000244|PDB:6C02}.
TURN 272 275 {ECO:0000244|PDB:6C02}.
STRAND 284 286 {ECO:0000244|PDB:6C01}.
HELIX 295 306 {ECO:0000244|PDB:6C02}.
HELIX 310 312 {ECO:0000244|PDB:6C02}.
STRAND 315 321 {ECO:0000244|PDB:6C02}.
HELIX 325 331 {ECO:0000244|PDB:6C02}.
STRAND 333 335 {ECO:0000244|PDB:6C02}.
HELIX 336 358 {ECO:0000244|PDB:6C02}.
TURN 362 364 {ECO:0000244|PDB:6C02}.
STRAND 366 370 {ECO:0000244|PDB:6C02}.
STRAND 382 385 {ECO:0000244|PDB:6C02}.
HELIX 386 388 {ECO:0000244|PDB:6C02}.
STRAND 396 399 {ECO:0000244|PDB:6C02}.
STRAND 401 403 {ECO:0000244|PDB:6C02}.
STRAND 405 410 {ECO:0000244|PDB:6C02}.
TURN 411 417 {ECO:0000244|PDB:6C02}.
HELIX 420 426 {ECO:0000244|PDB:6C02}.
TURN 427 429 {ECO:0000244|PDB:6C02}.
STRAND 435 440 {ECO:0000244|PDB:6C02}.
HELIX 441 443 {ECO:0000244|PDB:6C02}.
HELIX 446 448 {ECO:0000244|PDB:6C02}.
STRAND 458 463 {ECO:0000244|PDB:6C02}.
STRAND 468 472 {ECO:0000244|PDB:6C02}.
STRAND 479 482 {ECO:0000244|PDB:6C02}.
HELIX 490 492 {ECO:0000244|PDB:6C02}.
STRAND 496 500 {ECO:0000244|PDB:6C02}.
STRAND 505 509 {ECO:0000244|PDB:6C02}.
HELIX 514 516 {ECO:0000244|PDB:6C02}.
HELIX 517 525 {ECO:0000244|PDB:6C02}.
TURN 536 539 {ECO:0000244|PDB:6C02}.
HELIX 540 542 {ECO:0000244|PDB:6C02}.
STRAND 543 545 {ECO:0000244|PDB:6C02}.
HELIX 578 580 {ECO:0000244|PDB:6C02}.
HELIX 583 591 {ECO:0000244|PDB:6C02}.
HELIX 597 607 {ECO:0000244|PDB:6C02}.
STRAND 617 619 {ECO:0000244|PDB:6C02}.
STRAND 622 626 {ECO:0000244|PDB:6C02}.
STRAND 631 635 {ECO:0000244|PDB:6C02}.
TURN 636 639 {ECO:0000244|PDB:6C02}.
STRAND 640 648 {ECO:0000244|PDB:6C02}.
HELIX 673 675 {ECO:0000244|PDB:6C02}.
HELIX 679 684 {ECO:0000244|PDB:6C02}.
STRAND 689 694 {ECO:0000244|PDB:6C02}.
HELIX 696 698 {ECO:0000244|PDB:6C02}.
STRAND 700 703 {ECO:0000244|PDB:6C02}.
HELIX 704 708 {ECO:0000244|PDB:6C02}.
HELIX 711 713 {ECO:0000244|PDB:6C02}.
STRAND 714 717 {ECO:0000244|PDB:6C02}.
HELIX 719 730 {ECO:0000244|PDB:6C02}.
HELIX 732 739 {ECO:0000244|PDB:6C02}.
STRAND 742 750 {ECO:0000244|PDB:6C02}.
STRAND 756 758 {ECO:0000244|PDB:6C02}.
HELIX 762 764 {ECO:0000244|PDB:6C02}.
STRAND 778 789 {ECO:0000244|PDB:6C02}.
STRAND 801 809 {ECO:0000244|PDB:6C02}.
HELIX 815 817 {ECO:0000244|PDB:6C02}.
HELIX 824 826 {ECO:0000244|PDB:6C02}.
HELIX 828 834 {ECO:0000244|PDB:6C02}.
HELIX 839 846 {ECO:0000244|PDB:6C02}.
STRAND 847 849 {ECO:0000244|PDB:6C01}.
HELIX 858 866 {ECO:0000244|PDB:6C02}.
SEQUENCE 875 AA; 100124 MW; 629D2E33B4C45196 CRC64;
MESTLTLATE QPVKKNTLKK YKIACIVLLA LLVIMSLGLG LGLGLRKLEK QGSCRKKCFD
ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNK FRCGETRLEA SLCSCSDDCL
QRKDCCADYK SVCQGETSWL EENCDTAQQS QCPEGFDLPP VILFSMDGFR AEYLYTWDTL
MPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS
SKEQNNPAWW HGQPMWLTAM YQGLKAATYF WPGSEVAING SFPSIYMPYN GSVPFEERIS
TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG MLMEGLKQRN
LHNCVNIILL ADHGMDQTYC NKMEYMTDYF PRINFFYMYE GPAPRIRAHN IPHDFFSFNS
EEIVRNLSCR KPDQHFKPYL TPDLPKRLHY AKNVRIDKVH LFVDQQWLAV RSKSNTNCGG
GNHGYNNEFR SMEAIFLAHG PSFKEKTEVE PFENIEVYNL MCDLLRIQPA PNNGTHGSLN
HLLKVPFYEP SHAEEVSKFS VCGFANPLPT ESLDCFCPHL QNSTQLEQVN QMLNLTQEEI
TATVKVNLPF GRPRVLQKNV DHCLLYHREY VSGFGKAMRM PMWSSYTVPQ LGDTSPLPPT
VPDCLRADVR VPPSESQKCS FYLADKNITH GFLYPPASNR TSDSQYDALI TSNLVPMYEE
FRKMWDYFHS VLLIKHATER NGVNVVSGPI FDYNYDGHFD APDEITKHLA NTDVPIPTHY
FVVLTSCKNK SHTPENCPGW LDVLPFIIPH RPTNVESCPE GKPEALWVEE RFTAHIARVR
DVELLTGLDF YQDKVQPVSE ILQLKTYLPT FETTI


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