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Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 (E-NPP 1) (Lymphocyte antigen 41) (Ly-41) (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_MOUSE             Reviewed;         906 AA.
P06802; Q542E9; Q924C4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 4.
25-OCT-2017, entry version 179.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1;
Short=E-NPP 1;
AltName: Full=Lymphocyte antigen 41;
Short=Ly-41;
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:11027689, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:8223581};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000269|PubMed:11027689, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:8223581};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=Enpp1; Synonyms=Npps, Pc1, Pdnp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
TOPOLOGY, AND SUBUNIT.
STRAIN=BALB/cJ;
PubMed=3104326;
van Driel I.R., Goding J.W.;
"Plasma cell membrane glycoprotein PC-1. Primary structure deduced
from cDNA clones.";
J. Biol. Chem. 262:4882-4887(1987).
[2]
SEQUENCE REVISION TO 24; 46-47; 642 AND 693.
Goding J.W.;
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION, CATALYTIC
ACTIVITY, AND SUBCELLULAR LOCATION.
STRAIN=BALB/cJ; TISSUE=Plasmacytoma;
PubMed=1647027; DOI=10.1073/pnas.88.12.5192;
Rebbe N.F., Tong B.D., Finley E.M., Hickman S.;
"Identification of nucleotide pyrophosphatase/alkaline
phosphodiesterase I activity associated with the mouse plasma cell
differentiation antigen PC-1.";
Proc. Natl. Acad. Sci. U.S.A. 88:5192-5196(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-651 AND SER-680,
AND ALTERNATIVE SPLICING.
PubMed=12121276; DOI=10.1046/j.1365-2370.2002.00330.x;
Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.;
"Structural basis of allotypes of ecto-nucleotide
pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein
PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic
antibodies.";
Eur. J. Immunogenet. 29:307-313(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 168-188, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND GLYCOSYLATION.
PubMed=8223581; DOI=10.1111/j.1432-1033.1993.tb18261.x;
Belli S.I., van Driel I.R., Goding J.W.;
"Identification and characterization of a soluble form of the plasma
cell membrane glycoprotein PC-1 (5'-nucleotide phosphodiesterase).";
Eur. J. Biochem. 217:421-428(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 203-219.
PubMed=3001713; DOI=10.1073/pnas.82.24.8619;
van Driel I.R., Wilks A.F., Pietersz G.A., Goding J.W.;
"Murine plasma cell membrane antigen PC-1: molecular cloning of cDNA
and analysis of expression.";
Proc. Natl. Acad. Sci. U.S.A. 82:8619-8623(1985).
[8]
PROTEIN SEQUENCE OF 204-219; 332-351; 486-509; 716-725; 803-818 AND
855-867, AND SUBCELLULAR LOCATION.
PubMed=3917281;
Stearne P.A., van Driel I.R., Grego B., Simpson R.J., Goding J.W.;
"The murine plasma cell antigen PC-1: purification and partial amino
acid sequence.";
J. Immunol. 134:443-448(1985).
[9]
IDENTIFICATION OF POSSIBLE INITIATION SITE.
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).
[10]
DISEASE, AND FUNCTION.
PubMed=9662402; DOI=10.1038/956;
Okawa A., Nakamura I., Goto S., Moriya H., Nakamura Y., Ikegawa S.;
"Mutation in Npps in a mouse model of ossification of the posterior
longitudinal ligament of the spine.";
Nat. Genet. 19:271-273(1998).
[11]
ACTIVE SITE, METAL-BINDING, MUTAGENESIS OF ASP-200; LYS-237; THR-238;
PHE-239; ASP-358; HIS-362; ASP-405; HIS-406 AND HIS-517, AND CATALYTIC
ACTIVITY.
PubMed=11027689; DOI=10.1074/jbc.M007552200;
Gijsbers R., Ceulemans H., Stalmans W., Bollen M.;
"Structural and catalytic similarities between nucleotide
pyrophosphatases/phosphodiesterases and alkaline phosphatases.";
J. Biol. Chem. 276:1361-1368(2001).
[12]
DI-LEUCINE MOTIF, MUTAGENESIS OF ALA-28; SER-30; LEU-31 AND LEU-32,
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).
[13]
DI-LEUCINE MOTIF, MUTAGENESIS OF LEU-31; LEU-32; LEU-42 AND TYR-57,
AND SUBCELLULAR LOCATION.
PubMed=15075217; DOI=10.1152/ajpcell.00320.2003;
Vaingankar S.M., Fitzpatrick T.A., Johnson K., Goding J.W.,
Maurice M., Terkeltaub R.;
"Subcellular targeting and function of osteoblast nucleotide
pyrophosphatase phosphodiesterase 1.";
Am. J. Physiol. 286:C1177-C1187(2004).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267; ASN-323 AND ASN-624.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 92-906 IN COMPLEXES WITH
AMP; CMP; GMP; TMP; CALCIUM AND ZINC, GLYCOSYLATION AT ASN-267;
ASN-323 AND ASN-567, DISULFIDE BOND, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-239; HIS-242;
304-TRP--ASN-323; ASP-308 AND TYR-322, AND COFACTOR.
PubMed=23027977; DOI=10.1073/pnas.1208017109;
Kato K., Nishimasu H., Okudaira S., Mihara E., Ishitani R., Takagi J.,
Aoki J., Nureki O.;
"Crystal structure of Enpp1, an extracellular glycoprotein involved in
bone mineralization and insulin signaling.";
Proc. Natl. Acad. Sci. U.S.A. 109:16876-16881(2012).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 87-906 IN COMPLEX WITH
CALCIUM; PHOSPHATE AND ZINC, DISULFIDE BONDS, METAL-BINDING SITES,
SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-323; ASN-459;
ASN-567 AND ASN-624, AND COFACTOR.
PubMed=23041369; DOI=10.1016/j.str.2012.09.001;
Jansen S., Perrakis A., Ulens C., Winkler C., Andries M.,
Joosten R.P., Van Acker M., Luyten F.P., Moolenaar W.H., Bollen M.;
"Structure of NPP1, an ectonucleotide pyrophosphatase/
phosphodiesterase involved in tissue calcification.";
Structure 20:1948-1959(2012).
-!- FUNCTION: Appears to modulate insulin sensitivity (By similarity).
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.
{ECO:0000250|UniProtKB:P22413, ECO:0000269|PubMed:1647027,
ECO:0000269|PubMed:9662402}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000269|PubMed:11027689,
ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:8223581}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000269|PubMed:11027689,
ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:8223581}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:23041369};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369};
-!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
intermediate is formed which inhibits further hydrolysis.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=46 uM for ATP {ECO:0000269|PubMed:23027977};
KM=4.3 mM for UTP {ECO:0000269|PubMed:23027977};
KM=4.2 mM for GTP {ECO:0000269|PubMed:23027977};
KM=1.2 mM for CTP {ECO:0000269|PubMed:23027977};
-!- SUBUNIT: Homodimer. The secreted form is monomeric. Interacts with
INSR. {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-16016057, EBI-16016057;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Basolateral cell membrane; Single-pass type II membrane
protein. Secreted. Note=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 (By similarity). The
proteolytically processed form is secreted.
{ECO:0000250|UniProtKB:P22413}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=P06802-1; Sequence=Displayed;
Name=1;
IsoId=P06802-2; Sequence=VSP_006748;
-!- TISSUE SPECIFICITY: Selectively expressed on the surface of
antibody-secreting cells.
-!- DOMAIN: The di-leucine motif is required for basolateral targeting
in polarized epithelial cells, and for targeting to matrix
vesicles derived from mineralizing cells.
-!- PTM: The N-terminal is blocked.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1647027,
ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:8223581}.
-!- PTM: A secreted form is produced through cleavage at Lys-85 by
intracellular processing.
-!- DISEASE: Note=Defects in Enpp1 are the cause of the tiptoe walking
(ttw) phenotype. Ttw mice exhibit ossification of the spinal
ligaments. {ECO:0000269|PubMed:9662402}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
{ECO:0000305}.
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EMBL; J02700; AAA39893.2; -; mRNA.
EMBL; AF339910; AAK84174.1; -; mRNA.
EMBL; AK088857; BAC40616.1; -; mRNA.
EMBL; L04516; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
EMBL; M12552; AAA39892.1; -; mRNA.
CCDS; CCDS35870.1; -. [P06802-2]
CCDS; CCDS78802.1; -. [P06802-1]
PIR; A27410; A27410.
RefSeq; NP_001295256.1; NM_001308327.1.
UniGene; Mm.27254; -.
UniGene; Mm.478860; -.
PDB; 4B56; X-ray; 3.00 A; A/B=87-906.
PDB; 4GTW; X-ray; 2.70 A; A/B=92-906.
PDB; 4GTX; X-ray; 3.20 A; A/B=92-906.
PDB; 4GTY; X-ray; 3.19 A; A/B=92-906.
PDB; 4GTZ; X-ray; 3.19 A; A/B=92-906.
PDBsum; 4B56; -.
PDBsum; 4GTW; -.
PDBsum; 4GTX; -.
PDBsum; 4GTY; -.
PDBsum; 4GTZ; -.
ProteinModelPortal; P06802; -.
SMR; P06802; -.
DIP; DIP-59981N; -.
STRING; 10090.ENSMUSP00000101159; -.
iPTMnet; P06802; -.
PhosphoSitePlus; P06802; -.
SwissPalm; P06802; -.
MaxQB; P06802; -.
PaxDb; P06802; -.
PRIDE; P06802; -.
GeneID; 18605; -.
KEGG; mmu:18605; -.
CTD; 5167; -.
MGI; MGI:97370; Enpp1.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
HOGENOM; HOG000034646; -.
HOVERGEN; HBG051484; -.
InParanoid; P06802; -.
KO; K01513; -.
PhylomeDB; P06802; -.
BRENDA; 3.1.4.1; 3474.
BRENDA; 3.6.1.9; 3474.
SABIO-RK; P06802; -.
PRO; PR:P06802; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
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; ISO:MGI.
GO; GO:0004551; F:nucleotide diphosphatase activity; IDA:UniProtKB.
GO; GO:0004528; F:phosphodiesterase I activity; IDA:UniProtKB.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
GO; GO:0046034; P:ATP metabolic process; IDA:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0046849; P:bone remodeling; IMP:MGI.
GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:MGI.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0030505; P:inorganic diphosphate transport; ISO:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:MGI.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
GO; GO:0030730; P:sequestering of triglyceride; ISO:MGI.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom.
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; Alternative splicing; Biomineralization; Calcium;
Cell membrane; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal-anchor; Transmembrane; Transmembrane helix;
Zinc.
CHAIN 1 906 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 1.
/FTId=PRO_0000188565.
TOPO_DOM 1 58 Cytoplasmic. {ECO:0000255}.
TRANSMEM 59 79 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 80 906 Extracellular. {ECO:0000255}.
DOMAIN 86 126 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 127 171 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 173 573 Phosphodiesterase.
REGION 579 628 Linker.
REGION 635 906 Nuclease.
MOTIF 27 34 Di-leucine motif.
ACT_SITE 238 238 AMP-threonine intermediate.
{ECO:0000269|PubMed:11027689}.
METAL 200 200 Zinc 1; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 238 238 Zinc 1; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 358 358 Zinc 2; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 362 362 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 405 405 Zinc 1; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 406 406 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 517 517 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:23041369}.
METAL 781 781 Calcium. {ECO:0000269|PubMed:23041369}.
METAL 783 783 Calcium. {ECO:0000269|PubMed:23041369}.
METAL 785 785 Calcium. {ECO:0000269|PubMed:23041369}.
METAL 787 787 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:23041369}.
METAL 789 789 Calcium. {ECO:0000269|PubMed:23041369}.
BINDING 259 259 Substrate.
BINDING 277 277 Substrate.
BINDING 322 322 Substrate.
SITE 84 85 Cleavage.
SITE 896 896 Essential for catalytic activity.
{ECO:0000250}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:Q924C3}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000250|UniProtKB:Q924C3}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:23027977}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:23041369}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23041369}.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23027977,
ECO:0000269|PubMed:23041369}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:23041369}.
DISULFID 90 104 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 94 122 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 102 115 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 108 114 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 131 148 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 136 166 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 146 159 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 152 158 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 177 223
DISULFID 185 397
DISULFID 413 512
DISULFID 462 849
DISULFID 596 653
DISULFID 607 707
DISULFID 609 692
DISULFID 819 829
VAR_SEQ 630 630 Missing (in isoform 1).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:3104326}.
/FTId=VSP_006748.
VARIANT 651 651 H -> R (in allele ENPP1b).
{ECO:0000269|PubMed:12121276}.
VARIANT 680 680 R -> S (in allele ENPP1b).
{ECO:0000269|PubMed:12121276}.
MUTAGEN 28 28 A->G: No effect on basolateral sorting in
epithelial cells.
{ECO:0000269|PubMed:11598187}.
MUTAGEN 30 30 S->A,D: Little change in baolateral
sorting in epithelial cells.
{ECO:0000269|PubMed:11598187}.
MUTAGEN 31 31 L->A: 60% of ENPP1 redirected to apical
surface in epithelial cells. 75% of ENPP1
redirected to apical surface in
epithelial cells; abrogation of increased
NPP activity in oestoblastic matrix
vesicles; when associated with A-32.
{ECO:0000269|PubMed:11598187,
ECO:0000269|PubMed:15075217}.
MUTAGEN 32 32 L->A: 70% of ENPP1 redirected to apical
surface in epithelial cells; abrogation
of increased NPP activity in oestoblastic
matrix vesicles. 75% of ENPP1 redirected
to apical surface in epithelial cells;
abrogation of increased NPP activity in
oestoblastic matrix vesicles; when
associated with A-31.
{ECO:0000269|PubMed:11598187,
ECO:0000269|PubMed:15075217}.
MUTAGEN 42 42 L->A: No change in increased NPP activity
in oestoblastic matrix vesicles.
{ECO:0000269|PubMed:15075217}.
MUTAGEN 57 57 Y->G: No change in increased NPP activity
in oestoblastic matrix vesicles.
{ECO:0000269|PubMed:15075217}.
MUTAGEN 200 200 D->N: Decreases phosphodiesterase
activity by 95%. Abolishes formation of
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 237 237 K->A: Decreases phosphodiesterase
activity by 40%. Decreased formation of
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 238 238 T->A: Abolishes all phosphodiesterase
activity. Abolishes formation of
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 238 238 T->S: Decreases phosphodiesterase
activity by 95%. Accumulates
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 239 239 F->A: Decreases phosphodiesterase
activity by 50%. Decreased formation of
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689,
ECO:0000269|PubMed:23027977}.
MUTAGEN 242 242 H->L: Strongly decreased
phosphodiesterase activity.
{ECO:0000269|PubMed:23027977}.
MUTAGEN 304 323 Missing: Nearly abolishes activity with
nucleotide phosphates. Confers very low
activity with lysophospholipids.
{ECO:0000269|PubMed:23027977}.
MUTAGEN 308 308 D->A: Decreased phosphodiesterase
activity. {ECO:0000269|PubMed:23027977}.
MUTAGEN 322 322 Y->A: Strongly decreased
phosphodiesterase activity.
{ECO:0000269|PubMed:23027977}.
MUTAGEN 358 358 D->Q: Decreases phosphodiesterase
activity by 90%. Accumulates
nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 362 362 H->Q: Decreases phosphodiesterase
activity by 95%. 65% activity can be
restored by addition of Zn(2+) ions.
Accumulates nucleotidylated intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 405 405 D->N: Abolishes all phosphodiesterase
activity. 10% activity can be restored by
addition of Zn(2+) ions. Abolishes
formation of nucleotidylated
intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 406 406 H->Q: Abolishes all phosphodiesterase
activity. 15% activity can be restored by
addition of Zn(2+) ions. Abolishes
formation of nucleotidylated
intermediate.
{ECO:0000269|PubMed:11027689}.
MUTAGEN 517 517 H->Q: Abolishes all phosphodiesterase
activity. 60% activity can be restored by
addition of Zn(2+) ions. Abolishes
formation of nucleotidylated
intermediate.
{ECO:0000269|PubMed:11027689}.
TURN 94 96 {ECO:0000244|PDB:4B56}.
STRAND 100 103 {ECO:0000244|PDB:4B56}.
HELIX 108 111 {ECO:0000244|PDB:4B56}.
HELIX 118 122 {ECO:0000244|PDB:4B56}.
HELIX 124 126 {ECO:0000244|PDB:4B56}.
TURN 133 137 {ECO:0000244|PDB:4B56}.
STRAND 145 147 {ECO:0000244|PDB:4B56}.
HELIX 152 155 {ECO:0000244|PDB:4B56}.
HELIX 162 167 {ECO:0000244|PDB:4B56}.
TURN 172 174 {ECO:0000244|PDB:4GTW}.
STRAND 194 199 {ECO:0000244|PDB:4GTW}.
HELIX 204 209 {ECO:0000244|PDB:4GTW}.
HELIX 211 213 {ECO:0000244|PDB:4GTW}.
HELIX 215 222 {ECO:0000244|PDB:4GTW}.
STRAND 224 228 {ECO:0000244|PDB:4GTW}.
HELIX 238 247 {ECO:0000244|PDB:4GTW}.
HELIX 251 254 {ECO:0000244|PDB:4GTW}.
STRAND 259 263 {ECO:0000244|PDB:4GTW}.
TURN 264 267 {ECO:0000244|PDB:4GTW}.
STRAND 268 270 {ECO:0000244|PDB:4GTW}.
STRAND 272 274 {ECO:0000244|PDB:4GTW}.
HELIX 275 278 {ECO:0000244|PDB:4GTW}.
TURN 280 282 {ECO:0000244|PDB:4GTW}.
HELIX 288 294 {ECO:0000244|PDB:4GTW}.
STRAND 299 303 {ECO:0000244|PDB:4B56}.
STRAND 307 309 {ECO:0000244|PDB:4GTW}.
STRAND 311 313 {ECO:0000244|PDB:4B56}.
STRAND 317 319 {ECO:0000244|PDB:4B56}.
HELIX 328 338 {ECO:0000244|PDB:4GTW}.
TURN 343 345 {ECO:0000244|PDB:4GTW}.
STRAND 348 354 {ECO:0000244|PDB:4GTW}.
HELIX 358 364 {ECO:0000244|PDB:4GTW}.
STRAND 366 368 {ECO:0000244|PDB:4B56}.
HELIX 369 391 {ECO:0000244|PDB:4GTW}.
STRAND 399 403 {ECO:0000244|PDB:4GTW}.
STRAND 413 418 {ECO:0000244|PDB:4GTW}.
HELIX 420 423 {ECO:0000244|PDB:4GTW}.
STRAND 428 432 {ECO:0000244|PDB:4GTW}.
STRAND 434 436 {ECO:0000244|PDB:4GTW}.
STRAND 438 443 {ECO:0000244|PDB:4GTW}.
TURN 444 446 {ECO:0000244|PDB:4GTW}.
TURN 448 450 {ECO:0000244|PDB:4GTW}.
HELIX 453 460 {ECO:0000244|PDB:4GTW}.
STRAND 468 473 {ECO:0000244|PDB:4GTW}.
HELIX 474 476 {ECO:0000244|PDB:4GTW}.
HELIX 479 481 {ECO:0000244|PDB:4GTW}.
STRAND 487 489 {ECO:0000244|PDB:4GTW}.
STRAND 491 496 {ECO:0000244|PDB:4GTW}.
STRAND 501 505 {ECO:0000244|PDB:4GTW}.
TURN 506 508 {ECO:0000244|PDB:4B56}.
STRAND 513 516 {ECO:0000244|PDB:4GTW}.
HELIX 524 526 {ECO:0000244|PDB:4GTW}.
STRAND 530 534 {ECO:0000244|PDB:4GTW}.
STRAND 539 543 {ECO:0000244|PDB:4GTW}.
HELIX 548 550 {ECO:0000244|PDB:4GTW}.
HELIX 551 559 {ECO:0000244|PDB:4GTW}.
TURN 570 573 {ECO:0000244|PDB:4GTW}.
HELIX 574 576 {ECO:0000244|PDB:4GTW}.
STRAND 577 579 {ECO:0000244|PDB:4GTW}.
STRAND 591 594 {ECO:0000244|PDB:4GTY}.
STRAND 611 613 {ECO:0000244|PDB:4B56}.
HELIX 617 624 {ECO:0000244|PDB:4B56}.
TURN 630 632 {ECO:0000244|PDB:4B56}.
HELIX 633 637 {ECO:0000244|PDB:4B56}.
STRAND 652 656 {ECO:0000244|PDB:4B56}.
STRAND 658 665 {ECO:0000244|PDB:4B56}.
TURN 666 669 {ECO:0000244|PDB:4B56}.
STRAND 670 678 {ECO:0000244|PDB:4B56}.
HELIX 703 705 {ECO:0000244|PDB:4B56}.
HELIX 707 710 {ECO:0000244|PDB:4B56}.
STRAND 717 722 {ECO:0000244|PDB:4B56}.
TURN 728 731 {ECO:0000244|PDB:4B56}.
HELIX 735 738 {ECO:0000244|PDB:4B56}.
HELIX 740 742 {ECO:0000244|PDB:4B56}.
STRAND 743 746 {ECO:0000244|PDB:4B56}.
HELIX 748 759 {ECO:0000244|PDB:4B56}.
HELIX 761 768 {ECO:0000244|PDB:4B56}.
STRAND 771 779 {ECO:0000244|PDB:4B56}.
STRAND 785 787 {ECO:0000244|PDB:4B56}.
HELIX 791 797 {ECO:0000244|PDB:4B56}.
STRAND 799 806 {ECO:0000244|PDB:4B56}.
STRAND 810 821 {ECO:0000244|PDB:4B56}.
HELIX 826 828 {ECO:0000244|PDB:4B56}.
STRAND 830 840 {ECO:0000244|PDB:4B56}.
HELIX 846 848 {ECO:0000244|PDB:4B56}.
TURN 851 853 {ECO:0000244|PDB:4GTX}.
HELIX 855 865 {ECO:0000244|PDB:4B56}.
HELIX 870 877 {ECO:0000244|PDB:4GTW}.
HELIX 889 896 {ECO:0000244|PDB:4GTW}.
SEQUENCE 906 AA; 103176 MW; 068D45B0ED0F224D CRC64;
MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP AKDPNTYKVL
SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE
TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKTHNDCCI NYSSVCQDKK SWVEETCESI
DTPECPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP
NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY TLYLEEPDSS
GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN
KYLGDVNNVK VVYGPAARLR PTDVPETYYS FNYEALAKNL SCREPNQHFR PYLKPFLPKR
LHFAKSDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG
AEVDSFENIE VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS
TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH HVCLLQQQQF
LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP LSPVHKCSYY KSNSKLSYGF
LTPPRLNRVS NHIYSEALLT SNIVPMYQSF QVIWHYLHDT LLQRYAHERN GINVVSGPVF
DFDYDGRYDS LEILKQNSRV IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP
HRPDNIESCT HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP
IFSQED


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