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Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2) (EC 3.1.4.39) (Autotaxin) (Extracellular lysophospholipase D) (LysoPLD)

 ENPP2_MOUSE             Reviewed;         862 AA.
Q9R1E6; A8UH85; A8UH93; B2ZP54; Q6PDE0; Q99LG9;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
05-DEC-2018, entry version 167.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2;
Short=E-NPP 2;
EC=3.1.4.39 {ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339, ECO:0000269|PubMed:27780639};
AltName: Full=Autotaxin {ECO:0000303|PubMed:18175805};
AltName: Full=Extracellular lysophospholipase D;
Short=LysoPLD;
Flags: Precursor;
Name=Enpp2; Synonyms=Npps2, Pdnp2 {ECO:0000303|PubMed:10702660};
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).
STRAIN=C57BL/6J;
PubMed=10702660;
Piao J.-H., Matsuda Y., Nakamura H., Sano K.;
"Assignment of Pdnp2, the gene encoding phosphodiesterase I/nucleotide
pyrophosphatase 2, to mouse chromosome 15D2.";
Cytogenet. Cell Genet. 87:172-174(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CATALYTIC ACTIVITY,
FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
TISSUE SPECIFICITY.
TISSUE=Adipocyte, and Skeletal muscle;
PubMed=18175805; DOI=10.1074/jbc.M708705200;
Giganti A., Rodriguez M., Fould B., Moulharat N., Coge F.,
Chomarat P., Galizzi J.-P., Valet P., Saulnier-Blache J.-S.,
Boutin J.A., Ferry G.;
"Murine and human autotaxin alpha, beta, and gamma isoforms: gene
organization, tissue distribution, and biochemical characterization.";
J. Biol. Chem. 283:7776-7789(2008).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MRL/MpJ;
Burgess-Herbert S.L., Shockley K., Sheehan S., Bickerstaff L.,
Harwood B.I.V., Shen Y., Li R., Churchill G.A., Paigen B.;
"Comparative genomics, experimental biology, and bioinformatics merge
to narrow a QTL for HDL cholesterol on mouse chromosome 15 and human
chromosome 8.";
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Skin;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Retina;
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).
[7]
INDUCTION, AND POSSIBLE FUNCTION IN OBESITY.
PubMed=15700135; DOI=10.1007/s00125-004-1660-8;
Boucher J., Quilliot D., Pradere J.P., Simon M.F., Gres S., Guigne C.,
Prevot D., Ferry G., Boutin J.A., Carpene C., Valet P.,
Saulnier-Blache J.S.;
"Potential involvement of adipocyte insulin resistance in obesity-
associated up-regulation of adipocyte lysophospholipase D/autotaxin
expression.";
Diabetologia 48:569-577(2005).
[8]
PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
ACTIVITY, GLYCOSYLATION, AND MUTAGENESIS OF 12-VAL--VAL-22;
12-VAL--GLY-27; 23-ASN--GLY-27; CYS-25; GLY-27; 27-GLY--ALA-30;
27-GLY--ARG-35; 30-ALA--ILE-33; 30-ALA--GLY-41; 32-ARG--ARG-35;
36-ALA--GLU-40; ASN-53 AND ASN-410.
PubMed=17208043; DOI=10.1016/j.bbalip.2006.11.010;
Pradere J.P., Tarnus E., Gres S., Valet P., Saulnier-Blache J.S.;
"Secretion and lysophospholipase D activity of autotaxin by adipocytes
are controlled by N-glycosylation and signal peptidase.";
Biochim. Biophys. Acta 1771:93-102(2007).
[9]
SUBCELLULAR LOCATION, INTERDOMAIN DISULFIDE BOND, AND MUTAGENESIS OF
851-LEU--THR-853; LEU-851; LYS-852 AND THR-853.
PubMed=19329427; DOI=10.1074/jbc.M900790200;
Jansen S., Andries M., Derua R., Waelkens E., Bollen M.;
"Domain interplay mediated by an essential disulfide linkage is
critical for the activity and secretion of the metastasis-promoting
enzyme autotaxin.";
J. Biol. Chem. 284:14296-14302(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
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).
[11]
FUNCTION.
PubMed=28414242; DOI=10.1021/acs.jmedchem.7b00032;
Desroy N., Housseman C., Bock X., Joncour A., Bienvenu N., Cherel L.,
Labeguere V., Rondet E., Peixoto C., Grassot J.M., Picolet O.,
Annoot D., Triballeau N., Monjardet A., Wakselman E., Roncoroni V.,
Le Tallec S., Blanque R., Cottereaux C., Vandervoort N.,
Christophe T., Mollat P., Lamers M., Auberval M., Hrvacic B.,
Ralic J., Oste L., van der Aar E., Brys R., Heckmann B.;
"Discovery of 2-[[2-Ethyl-6-[4-[2-(3-hydroxyazetidin-1-yl)-2-
oxoethyl]piperazin-1-yl]-8-methylimidazo[1,2-a]pyridin-3-
yl]methylamino]-4-(4-fluorophenyl)thiazole-5-carbonitrile (GLPG1690),
a First-in-Class Autotaxin Inhibitor Undergoing Clinical Evaluation
for the Treatment of Idiopathic Pulmonary Fibrosis.";
J. Med. Chem. 60:3580-3590(2017).
[12] {ECO:0000244|PDB:3NKM, ECO:0000244|PDB:3NKN, ECO:0000244|PDB:3NKO, ECO:0000244|PDB:3NKP, ECO:0000244|PDB:3NKQ, ECO:0000244|PDB:3NKR}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 36-862 IN COMPLEXES WITH
LYSOPHOSPHATIDIC ACID; ZINC AND CALCIUM IONS, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-410
AND ASN-524, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-210;
LEU-213; ASN-230; LEU-243; GLU-247 AND PHE-249.
PubMed=21240269; DOI=10.1038/nsmb.1998;
Nishimasu H., Okudaira S., Hama K., Mihara E., Dohmae N., Inoue A.,
Ishitani R., Takagi J., Aoki J., Nureki O.;
"Crystal structure of autotaxin and insight into GPCR activation by
lipid mediators.";
Nat. Struct. Mol. Biol. 18:205-212(2011).
[13] {ECO:0000244|PDB:4GTW, ECO:0000244|PDB:4GTX, ECO:0000244|PDB:4GTY, ECO:0000244|PDB:4GTZ}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 51-58.
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).
[14] {ECO:0000244|PDB:3WAV, ECO:0000244|PDB:3WAW, ECO:0000244|PDB:3WAX, ECO:0000244|PDB:3WAY}
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 36-862 IN COMPLEXES WITH
INHIBITORS; CALCIUM AND ZINC, GLYCOSYLATION AT ASN-53; ASN-410 AND
ASN-524, CATALYTIC ACTIVITY, COFACTOR, AND DISULFIDE BOND.
PubMed=23688339; DOI=10.1021/cb400150c;
Kawaguchi M., Okabe T., Okudaira S., Nishimasu H., Ishitani R.,
Kojima H., Nureki O., Aoki J., Nagano T.;
"Screening and X-ray crystal structure-based optimization of autotaxin
(ENPP2) inhibitors, using a newly developed fluorescence probe.";
ACS Chem. Biol. 8:1713-1721(2013).
[15] {ECO:0000244|PDB:5LIA}
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 36-862 IN COMPLEX WITH
SYNTHETIC INHIBITOR; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, GLYCOSYLATION AT ASN-410 AND ASN-524, AND DISULFIDE BONDS.
PubMed=27780639; DOI=10.1016/j.bmcl.2016.10.036;
Shah P., Cheasty A., Foxton C., Raynham T., Farooq M., Gutierrez I.F.,
Lejeune A., Pritchard M., Turnbull A., Pang L., Owen P., Boyd S.,
Stowell A., Jordan A., Hamilton N.M., Hitchin J.R., Stockley M.,
MacDonald E., Quesada M.J., Trivier E., Skeete J., Ovaa H.,
Moolenaar W.H., Ryder H.;
"Discovery of potent inhibitors of the lysophospholipase autotaxin.";
Bioorg. Med. Chem. Lett. 26:5403-5410(2016).
[16] {ECO:0000244|PDB:5OHI, ECO:0000244|PDB:5OLB}
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 36-862 IN COMPLEX WITH
SYNTHETIC INHIBITOR; CALCIUM AND ZINC, GLYCOSYLATION AT ASN-53;
ASN-410 AND ASN-524, AND DISULFIDE BONDS.
PubMed=29259743; DOI=10.1021/acsmedchemlett.7b00312;
Kuttruff C.A., Ferrara M., Bretschneider T., Hoerer S., Handschuh S.,
Nosse B., Romig H., Nicklin P., Roth G.J.;
"Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly
Reduces LPA Levels in Vivo.";
ACS Med. Chem. Lett. 8:1252-1257(2017).
-!- FUNCTION: Hydrolyzes lysophospholipids to produce the signaling
molecule lysophosphatidic acid (LPA) in extracellular fluids
(PubMed:17208043, PubMed:28414242, PubMed:27780639). Major
substrate is lysophosphatidylcholine (PubMed:17208043,
PubMed:27780639). Also can act on sphingosylphosphorylcholine
producing sphingosine-1-phosphate, a modulator of cell motility.
Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and
barely ATP (PubMed:18175805). Involved in several motility-related
processes such as angiogenesis and neurite outgrowth. Acts as an
angiogenic factor by stimulating migration of smooth muscle cells
and microtubule formation. Stimulates migration of melanoma cells,
probably via a pertussis toxin-sensitive G protein. May have a
role in induction of parturition (By similarity). Possible
involvement in cell proliferation and adipose tissue development
(Probable). Tumor cell motility-stimulating factor.
{ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:17208043,
ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:27780639, ECO:0000269|PubMed:28414242,
ECO:0000305|PubMed:15700135}.
-!- CATALYTIC ACTIVITY:
Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-
alkyl-sn-glycero-3-phosphate + ethanolamine + H(+);
Xref=Rhea:RHEA:15965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57603, ChEBI:CHEBI:58014, ChEBI:CHEBI:76168;
EC=3.1.4.39; Evidence={ECO:0000269|PubMed:17208043,
ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339, ECO:0000269|PubMed:27780639};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339, ECO:0000269|PubMed:27780639};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339, ECO:0000269|PubMed:27780639};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339, ECO:0000269|PubMed:27780639};
-!- ACTIVITY REGULATION: Inhibited by lysophosphatidic acid (LPA) and
sphingosine-1-phosphate (S1P) (By similarity). Inhibited by EDTA
and EGTA. {ECO:0000250, ECO:0000269|PubMed:18175805}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.9 mM for pNppp (isoform 1) {ECO:0000269|PubMed:18175805};
KM=4.4 mM for pNppp (isoform 2) {ECO:0000269|PubMed:18175805};
KM=11.8 mM for pNppp (isoform 3) {ECO:0000269|PubMed:18175805};
Vmax=1.9 nmol/min/ug enzyme with pNppp as substrate (isoform 1)
{ECO:0000269|PubMed:18175805};
Vmax=0.35 nmol/min/ug enzyme with pNppp as substrate (isoform 2)
{ECO:0000269|PubMed:18175805};
Vmax=1.8 nmol/min/ug enzyme with pNppp as substrate (isoform 3)
{ECO:0000269|PubMed:18175805};
pH dependence:
Optimum pH is 8.0 for isoforms 1, 2 and 3.
{ECO:0000269|PubMed:18175805};
Temperature dependence:
Isoforms 1 and 3 have maximum activity from 45 to 55 degrees
Celsius. {ECO:0000269|PubMed:18175805};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17208043,
ECO:0000269|PubMed:19329427, ECO:0000269|PubMed:21240269}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Beta;
IsoId=Q9R1E6-1; Sequence=Displayed;
Name=2; Synonyms=Alpha;
IsoId=Q9R1E6-2; Sequence=VSP_036396;
Name=3; Synonyms=Gamma;
IsoId=Q9R1E6-3; Sequence=VSP_036397;
-!- TISSUE SPECIFICITY: Expressed in brain and adipose tissue.
{ECO:0000269|PubMed:18175805}.
-!- INDUCTION: Up-regulated in adipocytes of obese-diabetic db/db
mice. {ECO:0000269|PubMed:15700135}.
-!- PTM: N-glycosylation, but not furin-cleavage, plays a critical
role on secretion and on lysoPLD activity. Secretion requires
simultaneous glycosylation on Asn-53 and Asn-410, while probable
glycosylation of Asn-410 has a preferential role on lysoPLD
activity. Not O-glycosylated. {ECO:0000269|PubMed:17208043,
ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339}.
-!- PTM: The interdomain disulfide bond between Cys-413 and Cys-805 is
essential for catalytic activity. {ECO:0000269|PubMed:19329427}.
-!- DISEASE: Note=May contribute to obesity (PubMed:15700135).
{ECO:0000269|PubMed:15700135}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
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EMBL; AF123542; AAD46480.1; -; mRNA.
EMBL; EU131009; ABW38314.1; -; mRNA.
EMBL; EU131010; ABW38315.1; -; mRNA.
EMBL; EU677474; ACD12865.1; -; Genomic_DNA.
EMBL; EU677475; ACD12866.1; -; Genomic_DNA.
EMBL; AK161144; BAE36214.1; -; mRNA.
EMBL; CH466545; EDL29265.1; -; Genomic_DNA.
EMBL; BC003264; AAH03264.1; -; mRNA.
EMBL; BC058759; AAH58759.1; -; mRNA.
CCDS; CCDS27472.1; -. [Q9R1E6-1]
CCDS; CCDS49607.1; -. [Q9R1E6-2]
CCDS; CCDS70628.1; -. [Q9R1E6-3]
RefSeq; NP_001129549.1; NM_001136077.3. [Q9R1E6-2]
RefSeq; NP_001272923.1; NM_001285994.2. [Q9R1E6-3]
RefSeq; NP_001272924.1; NM_001285995.2.
RefSeq; NP_056559.2; NM_015744.4. [Q9R1E6-1]
UniGene; Mm.250256; -.
PDB; 3NKM; X-ray; 2.00 A; A=36-862.
PDB; 3NKN; X-ray; 1.80 A; A=36-862.
PDB; 3NKO; X-ray; 1.75 A; A=36-862.
PDB; 3NKP; X-ray; 1.75 A; A=36-862.
PDB; 3NKQ; X-ray; 1.70 A; A=36-862.
PDB; 3NKR; X-ray; 1.70 A; A=36-862.
PDB; 3WAV; X-ray; 1.80 A; A=36-862.
PDB; 3WAW; X-ray; 1.95 A; A=36-862.
PDB; 3WAX; X-ray; 1.90 A; A=36-862.
PDB; 3WAY; X-ray; 1.75 A; A=36-862.
PDB; 4GTW; X-ray; 2.70 A; A/B=51-58.
PDB; 4GTX; X-ray; 3.20 A; A/B=51-58.
PDB; 4GTY; X-ray; 3.19 A; A/B=51-58.
PDB; 4GTZ; X-ray; 3.19 A; A/B=51-58.
PDB; 5HRT; X-ray; 2.00 A; A=36-862.
PDB; 5INH; X-ray; 1.84 A; A=36-862.
PDB; 5JVG; X-ray; 3.43 A; U=1-81.
PDB; 5LIA; X-ray; 1.92 A; A=36-862.
PDB; 5OHI; X-ray; 1.66 A; A=36-862.
PDB; 5OLB; X-ray; 1.82 A; A=36-862.
PDBsum; 3NKM; -.
PDBsum; 3NKN; -.
PDBsum; 3NKO; -.
PDBsum; 3NKP; -.
PDBsum; 3NKQ; -.
PDBsum; 3NKR; -.
PDBsum; 3WAV; -.
PDBsum; 3WAW; -.
PDBsum; 3WAX; -.
PDBsum; 3WAY; -.
PDBsum; 4GTW; -.
PDBsum; 4GTX; -.
PDBsum; 4GTY; -.
PDBsum; 4GTZ; -.
PDBsum; 5HRT; -.
PDBsum; 5INH; -.
PDBsum; 5JVG; -.
PDBsum; 5LIA; -.
PDBsum; 5OHI; -.
PDBsum; 5OLB; -.
ProteinModelPortal; Q9R1E6; -.
SMR; Q9R1E6; -.
BindingDB; Q9R1E6; -.
ChEMBL; CHEMBL3826871; -.
GuidetoPHARMACOLOGY; 2901; -.
iPTMnet; Q9R1E6; -.
PhosphoSitePlus; Q9R1E6; -.
PeptideAtlas; Q9R1E6; -.
PRIDE; Q9R1E6; -.
Ensembl; ENSMUST00000041591; ENSMUSP00000036180; ENSMUSG00000022425. [Q9R1E6-1]
Ensembl; ENSMUST00000167541; ENSMUSP00000132640; ENSMUSG00000022425. [Q9R1E6-3]
Ensembl; ENSMUST00000171545; ENSMUSP00000128941; ENSMUSG00000022425. [Q9R1E6-2]
GeneID; 18606; -.
KEGG; mmu:18606; -.
UCSC; uc007vro.3; mouse. [Q9R1E6-1]
UCSC; uc007vrq.3; mouse. [Q9R1E6-3]
UCSC; uc011zsx.2; mouse. [Q9R1E6-2]
CTD; 5168; -.
MGI; MGI:1321390; Enpp2.
GeneTree; ENSGT00940000155778; -.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; Q9R1E6; -.
KO; K01122; -.
OMA; DGLHDTQ; -.
OrthoDB; EOG091G017X; -.
PhylomeDB; Q9R1E6; -.
TreeFam; TF330032; -.
BRENDA; 3.1.4.39; 3474.
SABIO-RK; Q9R1E6; -.
ChiTaRS; Enpp2; mouse.
EvolutionaryTrace; Q9R1E6; -.
PRO; PR:Q9R1E6; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022425; Expressed in 405 organ(s), highest expression level in choroid plexus epithelium.
ExpressionAtlas; Q9R1E6; baseline and differential.
Genevisible; Q9R1E6; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004551; F:nucleotide diphosphatase activity; ISS:MGI.
GO; GO:0004528; F:phosphodiesterase I activity; ISS:MGI.
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:0060326; P:cell chemotaxis; ISO:MGI.
GO; GO:0044849; P:estrous cycle; IBA:GO_Central.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
GO; GO:0009395; P:phospholipid catabolic process; ISO:MGI.
GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:MGI.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0045765; P:regulation of angiogenesis; IEA:InterPro.
GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
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; IPR029881; ENPP2.
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.
PANTHER; PTHR10151:SF21; PTHR10151:SF21; 1.
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; Calcium; Chemotaxis;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Obesity; Reference proteome; Repeat; Secreted; Signal;
Zinc.
SIGNAL 1 27 {ECO:0000250}.
PROPEP 28 35 Removed by furin.
/FTId=PRO_0000281650.
CHAIN 36 862 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 2.
/FTId=PRO_0000188568.
DOMAIN 54 97 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 98 142 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 144 501 Phosphodiesterase.
REGION 210 213 Substrate binding. {ECO:0000244|PDB:3NKR,
ECO:0000269|PubMed:21240269}.
REGION 243 254 Substrate binding.
{ECO:0000305|PubMed:21240269}.
REGION 597 862 Nuclease.
REGION 829 850 Required for secretion.
MOTIF 126 128 Cell attachment site. {ECO:0000255}.
ACT_SITE 209 209 Nucleophile.
{ECO:0000305|PubMed:21240269}.
METAL 171 171 Zinc 1; catalytic. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 209 209 Zinc 1; catalytic. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 311 311 Zinc 2; catalytic. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 315 315 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 358 358 Zinc 1; catalytic. {ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 359 359 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 474 474 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
METAL 739 739 Calcium. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
METAL 741 741 Calcium. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
METAL 743 743 Calcium. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
METAL 745 745 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
METAL 747 747 Calcium. {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
BINDING 230 230 Substrate. {ECO:0000244|PDB:3NKR,
ECO:0000269|PubMed:21240269}.
BINDING 306 306 Substrate. {ECO:0000244|PDB:3NKR,
ECO:0000269|PubMed:21240269}.
SITE 852 852 Essential for catalytic activity.
{ECO:0000269|PubMed:19329427}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5INH,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639}.
CARBOHYD 806 806 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 75 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 62 93 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 73 86 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 79 85 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 102 119 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 107 137 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 117 130 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 123 129 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 148 194 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 156 350 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:29259743}.
DISULFID 366 468 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:29259743}.
DISULFID 413 805 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 566 666 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 568 651 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
DISULFID 774 784 {ECO:0000244|PDB:3NKM,
ECO:0000244|PDB:3NKN,
ECO:0000244|PDB:3NKO,
ECO:0000244|PDB:3NKP,
ECO:0000244|PDB:3NKQ,
ECO:0000244|PDB:3NKR,
ECO:0000244|PDB:3WAV,
ECO:0000244|PDB:3WAW,
ECO:0000244|PDB:3WAX,
ECO:0000244|PDB:3WAY,
ECO:0000244|PDB:5HRT,
ECO:0000244|PDB:5INH,
ECO:0000244|PDB:5LIA,
ECO:0000244|PDB:5OHI,
ECO:0000244|PDB:5OLB,
ECO:0000269|PubMed:21240269,
ECO:0000269|PubMed:23688339,
ECO:0000269|PubMed:27780639,
ECO:0000269|PubMed:29259743}.
VAR_SEQ 323 323 E -> EESSYGSPLTPAKRPKRKVAPKRRQERPVAPPKKRR
RKLHRMDHYTAETRQDK (in isoform 2).
{ECO:0000303|PubMed:18175805}.
/FTId=VSP_036396.
VAR_SEQ 592 592 E -> EAETGKFRGSKHENKKSLNGNVEPRK (in
isoform 3).
{ECO:0000303|PubMed:18175805}.
/FTId=VSP_036397.
MUTAGEN 12 27 Missing: Complete inhibition of
secretion. {ECO:0000269|PubMed:17208043}.
MUTAGEN 12 22 Missing: Complete inhibition of
secretion. {ECO:0000269|PubMed:17208043}.
MUTAGEN 23 27 Missing: No effect on secretion.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 23 23 Missing: No effect on secretion.
MUTAGEN 25 25 Missing: No effect on secretion.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 27 35 Missing: No effect on secretion nor
lysophospholipase activity.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 27 30 Missing: No effect on secretion.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 27 27 Missing: No effect on secretion.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 30 41 Missing: No effect on secretion nor
lysophospholipase activity.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 30 33 Missing: No effect on secretion nor
lysophospholipase activity.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 32 35 Missing: No effect on secretion nor
lysophospholipase activity.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 36 40 Missing: No effect on secretion nor
lysophospholipase activity.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 53 53 Missing: No effect on secretion; slightly
decreases lysophospholipase activity.
Almost complete loss of lysophospholipase
activity; when associated with N-410 del.
{ECO:0000269|PubMed:17208043}.
MUTAGEN 210 210 F->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 213 213 L->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 230 230 N->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 243 243 L->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 247 247 E->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 249 249 F->A: Reduced lysophospholipase activity.
{ECO:0000269|PubMed:21240269}.
MUTAGEN 410 410 Missing: No effect on secretion; greatly
inhibits lysoPLD activity. Inhibits
secretion. Almost complete loss of
lysoPLD activity; when associated with N-
53 del. {ECO:0000269|PubMed:17208043}.
MUTAGEN 512 512 M->A: Reduced lysophospholipase activity.
MUTAGEN 851 853 LKT->AAA,RRR,SSS: No catalytic activity.
{ECO:0000269|PubMed:19329427}.
MUTAGEN 851 851 L->A: No effect.
{ECO:0000269|PubMed:19329427}.
MUTAGEN 852 852 K->A,R: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:19329427}.
MUTAGEN 853 853 T->A: No effect.
{ECO:0000269|PubMed:19329427}.
CONFLICT 103 103 T -> I (in Ref. 3; ACD12866).
{ECO:0000305}.
CONFLICT 517 517 G -> S (in Ref. 1; AAD46480).
{ECO:0000305}.
CONFLICT 550 550 P -> T (in Ref. 1; AAD46480).
{ECO:0000305}.
CONFLICT 573 573 E -> K (in Ref. 1; AAD46480).
{ECO:0000305}.
CONFLICT 743 743 N -> D (in Ref. 3; ACD12866 and 6;
AAH03264). {ECO:0000305}.
TURN 59 63 {ECO:0000244|PDB:5OHI}.
HELIX 77 79 {ECO:0000244|PDB:5OHI}.
TURN 80 83 {ECO:0000244|PDB:5OHI}.
HELIX 89 93 {ECO:0000244|PDB:5OHI}.
TURN 98 100 {ECO:0000244|PDB:5HRT}.
HELIX 104 106 {ECO:0000244|PDB:5OHI}.
STRAND 115 118 {ECO:0000244|PDB:5OHI}.
HELIX 123 126 {ECO:0000244|PDB:5OHI}.
HELIX 133 138 {ECO:0000244|PDB:5OHI}.
HELIX 143 145 {ECO:0000244|PDB:5OHI}.
STRAND 165 171 {ECO:0000244|PDB:5OHI}.
HELIX 175 183 {ECO:0000244|PDB:5OHI}.
HELIX 186 194 {ECO:0000244|PDB:5OHI}.
STRAND 195 197 {ECO:0000244|PDB:5OHI}.
HELIX 209 218 {ECO:0000244|PDB:5OHI}.
HELIX 222 225 {ECO:0000244|PDB:5OHI}.
STRAND 229 234 {ECO:0000244|PDB:5OHI}.
TURN 235 238 {ECO:0000244|PDB:5OHI}.
STRAND 239 241 {ECO:0000244|PDB:5OHI}.
STRAND 243 246 {ECO:0000244|PDB:3NKQ}.
HELIX 247 249 {ECO:0000244|PDB:5OHI}.
HELIX 251 253 {ECO:0000244|PDB:5OHI}.
HELIX 259 265 {ECO:0000244|PDB:5OHI}.
HELIX 281 292 {ECO:0000244|PDB:5OHI}.
TURN 296 298 {ECO:0000244|PDB:5OHI}.
STRAND 301 310 {ECO:0000244|PDB:5OHI}.
HELIX 311 317 {ECO:0000244|PDB:5OHI}.
HELIX 322 324 {ECO:0000244|PDB:5OHI}.
HELIX 325 344 {ECO:0000244|PDB:5OHI}.
TURN 348 350 {ECO:0000244|PDB:5OHI}.
STRAND 352 358 {ECO:0000244|PDB:5OHI}.
STRAND 368 371 {ECO:0000244|PDB:5OHI}.
HELIX 372 374 {ECO:0000244|PDB:5OHI}.
HELIX 379 381 {ECO:0000244|PDB:3NKQ}.
STRAND 382 385 {ECO:0000244|PDB:5OHI}.
STRAND 387 396 {ECO:0000244|PDB:5OHI}.
HELIX 404 411 {ECO:0000244|PDB:5OHI}.
STRAND 419 424 {ECO:0000244|PDB:5OHI}.
HELIX 425 427 {ECO:0000244|PDB:5OHI}.
HELIX 430 432 {ECO:0000244|PDB:5OHI}.
STRAND 442 447 {ECO:0000244|PDB:5OHI}.
STRAND 452 456 {ECO:0000244|PDB:5OHI}.
HELIX 457 459 {ECO:0000244|PDB:3WAV}.
STRAND 471 473 {ECO:0000244|PDB:3WAY}.
HELIX 481 483 {ECO:0000244|PDB:5OHI}.
STRAND 487 494 {ECO:0000244|PDB:5OHI}.
STRAND 496 499 {ECO:0000244|PDB:5OHI}.
HELIX 505 507 {ECO:0000244|PDB:5OHI}.
HELIX 508 515 {ECO:0000244|PDB:5OHI}.
TURN 527 530 {ECO:0000244|PDB:5OHI}.
HELIX 531 533 {ECO:0000244|PDB:5OHI}.
STRAND 534 536 {ECO:0000244|PDB:5OHI}.
HELIX 559 561 {ECO:0000244|PDB:5OHI}.
HELIX 579 581 {ECO:0000244|PDB:5LIA}.
TURN 583 586 {ECO:0000244|PDB:3WAV}.
TURN 593 595 {ECO:0000244|PDB:5OHI}.
STRAND 609 613 {ECO:0000244|PDB:5OHI}.
STRAND 618 622 {ECO:0000244|PDB:5OHI}.
TURN 623 626 {ECO:0000244|PDB:5OHI}.
STRAND 627 635 {ECO:0000244|PDB:5OHI}.
HELIX 646 648 {ECO:0000244|PDB:5OHI}.
HELIX 660 662 {ECO:0000244|PDB:5OHI}.
HELIX 666 671 {ECO:0000244|PDB:5OHI}.
STRAND 676 681 {ECO:0000244|PDB:5OHI}.
HELIX 683 685 {ECO:0000244|PDB:5OHI}.
HELIX 689 695 {ECO:0000244|PDB:5OHI}.
HELIX 698 700 {ECO:0000244|PDB:5OHI}.
STRAND 701 704 {ECO:0000244|PDB:5OHI}.
HELIX 706 717 {ECO:0000244|PDB:5OHI}.
HELIX 719 727 {ECO:0000244|PDB:5OHI}.
STRAND 729 737 {ECO:0000244|PDB:5OHI}.
STRAND 743 745 {ECO:0000244|PDB:5OHI}.
HELIX 749 751 {ECO:0000244|PDB:5OHI}.
STRAND 765 776 {ECO:0000244|PDB:5OHI}.
HELIX 781 783 {ECO:0000244|PDB:5OHI}.
STRAND 788 796 {ECO:0000244|PDB:5OHI}.
TURN 805 808 {ECO:0000244|PDB:5OHI}.
HELIX 811 813 {ECO:0000244|PDB:5OHI}.
HELIX 815 821 {ECO:0000244|PDB:5OHI}.
HELIX 826 833 {ECO:0000244|PDB:5OHI}.
STRAND 834 836 {ECO:0000244|PDB:5OHI}.
HELIX 845 853 {ECO:0000244|PDB:5OHI}.
SEQUENCE 862 AA; 98885 MW; 343D44DEAA8FA352 CRC64;
MARQGCFGSY QVISLFTFAI GVNLCLGFTA SRIKRAEWDE GPPTVLSDSP WTNTSGSCKG
RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW ECTKDRCGEV RNEENACHCS
EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE IRVPECPAGF VRPPLIIFSV DGFRASYMKK
GSKVMPNIEK LRSCGTHAPY MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAT
FHLRGREKFN HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLKLHRC VNVIFVGDHG
MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRPKIPNNL KYDPKAIIAN LTCKKPDQHF
KPYMKQHLPK RLHYANNRRI EDLHLLVERR WHVARKPLDV YKKPSGKCFF QGDHGFDNKV
NSMQTVFVGY GPTFKYRTKV PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR
PTLPEEVSRP NYPGIMYLQS DFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEERHLLYGR
PAVLYRTSYD ILYHTDFESG YSEIFLMPLW TSYTISKQAE VSSIPEHLTN CVRPDVRVSP
GFSQNCLAYK NDKQMSYGFL FPPYLSSSPE AKYDAFLVTN MVPMYPAFKR VWTYFQRVLV
KKYASERNGV NVISGPIFDY NYNGLRDIED EIKQYVEGSS IPVPTHYYSI ITSCLDFTQP
ADKCDGPLSV SSFILPHRPD NDESCNSSED ESKWVEELMK MHTARVRDIE HLTGLDFYRK
TSRSYSEILT LKTYLHTYES EI


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