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Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)]

 PA24A_HUMAN             Reviewed;         749 AA.
P47712; B1AKG4; Q29R80;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
05-DEC-2018, entry version 195.
RecName: Full=Cytosolic phospholipase A2;
Short=cPLA2;
AltName: Full=Phospholipase A2 group IVA;
Includes:
RecName: Full=Phospholipase A2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Includes:
RecName: Full=Lysophospholipase;
EC=3.1.1.5;
Name=PLA2G4A; Synonyms=CPLA2, PLA2G4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
LYS-651.
PubMed=1904318; DOI=10.1016/0092-8674(91)90556-E;
Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A.,
Lin A.Y., Milona N., Knopf J.L.;
"A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-
dependent translocation domain with homology to PKC and GAP.";
Cell 65:1043-1051(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-651.
PubMed=1869522;
Sharp J., White D., Chiou G., Goodson T., Gamboa G., McClure D.,
Burgett S., Hoskins J., Skatrud P., Sportsman J., Becker G., Kang L.,
Roberts E., Kramer R.;
"Molecular cloning and expression of human Ca(2+)-sensitive cytosolic
phospholipase A2.";
J. Biol. Chem. 266:14850-14853(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-224 AND LYS-651.
NIEHS SNPs program;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-651.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
MUTAGENESIS OF SER-505, AND PHOSPHORYLATION AT SER-505.
PubMed=8381049; DOI=10.1016/0092-8674(93)90666-E;
Lin L.-L., Wartmann M., Lin A.Y., Knopf J.L., Seth A., Davis R.J.;
"cPLA2 is phosphorylated and activated by MAP kinase.";
Cell 72:269-278(1993).
[7]
ACTIVE SITE, MUTAGENESIS OF CYS-139; CYS-141; CYS-151; SER-195;
SER-215; CYS-220; SER-228; CYS-324; CYS-331; SER-577; CYS-620; CYS-634
AND CYS-726, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8083230;
Sharp J.D., Pickard R.T., Chiou X.G., Manetta J.V., Kovacevic S.,
Miller J.R., Varshavsky A.D., Roberts E.F., Strifler B.A., Brems D.N.,
Kramer R.M.;
"Serine 228 is essential for catalytic activities of 85-kDa cytosolic
phospholipase A2.";
J. Biol. Chem. 269:23250-23254(1994).
[8]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, AND MUTAGENESIS
OF SER-228.
PubMed=8619991; DOI=10.1021/bi952541k;
Huang Z., Payette P., Abdullah K., Cromlish W.A., Kennedy B.P.;
"Functional identification of the active-site nucleophile of the human
85-kDa cytosolic phospholipase A2.";
Biochemistry 35:3712-3721(1996).
[9]
ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-200; SER-228
AND ASP-549.
PubMed=8702602; DOI=10.1074/jbc.271.32.19225;
Pickard R.T., Chiou X.G., Strifler B.A., DeFelippis M.R., Hyslop P.A.,
Tebbe A.L., Yee Y.K., Reynolds L.J., Dennis E.A., Kramer R.M.,
Sharp J.D.;
"Identification of essential residues for the catalytic function of
85-kDa cytosolic phospholipase A2. Probing the role of histidine,
aspartic acid, cysteine, and arginine.";
J. Biol. Chem. 271:19225-19231(1996).
[10]
PHOSPHORYLATION AT SER-505 AND SER-727.
PubMed=9468497; DOI=10.1074/jbc.273.8.4449;
Boersch-Haubold A.G., Bartoli F., Asselin J., Dudler T., Kramer R.M.,
Apitz-Castro R., Watson S.P., Gelb M.H.;
"Identification of the phosphorylation sites of cytosolic
phospholipase A2 in agonist-stimulated human platelets and HeLa
cells.";
J. Biol. Chem. 273:4449-4458(1998).
[11]
INTERACTION WITH KAT5.
PubMed=11416127; DOI=10.1128/MCB.21.14.4470-4481.2001;
Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G.,
Taheri M.R., Bonventre J.V.;
"PLIP, a novel splice variant of Tip60, interacts with group IV
cytosolic phospholipase A(2), induces apoptosis, and potentiates
prostaglandin production.";
Mol. Cell. Biol. 21:4470-4481(2001).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
INVOLVEMENT IN PHOSPHOLIPASE A2 DEFICIENCY, AND VARIANTS PRO-111;
HIS-485 AND LYS-651.
PubMed=18451993; DOI=10.1172/JCI30473;
Adler D.H., Cogan J.D., Phillips J.A., Schnetz-Boutaud N., Milne G.L.,
Iverson T., Stein J.A., Brenner D.A., Morrow J.D., Boutaud O.,
Oates J.A.;
"Inherited human cPLA(2alpha) deficiency is associated with impaired
eicosanoid biosynthesis, small intestinal ulceration, and platelet
dysfunction.";
J. Clin. Invest. 118:2121-2131(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437; SER-727
AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437 AND
SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-268; SER-435;
SER-437; SER-727 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-541 AND LYS-606, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-141 IN COMPLEX WITH
CALCIUM IONS, AND DOMAIN.
PubMed=9430701; DOI=10.1074/jbc.273.3.1596;
Perisic O., Fong S., Lynch D.E., Bycroft M., Williams R.L.;
"Crystal structure of a calcium-phospholipid binding domain from
cytosolic phospholipase A2.";
J. Biol. Chem. 273:1596-1604(1998).
[23]
STRUCTURE BY NMR OF 1-138 IN COMPLEX WITH CALCIUM IONS, DOMAIN, AND
SUBCELLULAR LOCATION.
PubMed=9665851; DOI=10.1006/jmbi.1998.1874;
Xu G.-Y., McDonagh T., Yu H.-A., Nalefski E.A., Clark J.D.,
Cumming D.A.;
"Solution structure and membrane interactions of the C2 domain of
cytosolic phospholipase A2.";
J. Mol. Biol. 280:485-500(1998).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
AND ACTIVE SITE.
PubMed=10319815; DOI=10.1016/S0092-8674(00)80744-8;
Dessen A., Tang J., Schmidt H., Stahl M., Clark J.D., Seehra J.,
Somers W.S.;
"Crystal structure of human cytosolic phospholipase A2 reveals a novel
topology and catalytic mechanism.";
Cell 97:349-360(1999).
[25]
VARIANT [LARGE SCALE ANALYSIS] GLN-442.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the
sn-2 position releasing arachidonic acid. Together with its
lysophospholipid activity, it is implicated in the initiation of
the inflammatory response.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-
acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168;
EC=3.1.1.4;
-!- CATALYTIC ACTIVITY:
Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid
+ H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
-!- ACTIVITY REGULATION: Stimulated by agonists such as ATP, EGF,
thrombin and bradykinin as well as by cytosolic Ca(2+).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=2.7 umol/min/mg enzyme for the phospholipase A2 reaction
{ECO:0000269|PubMed:8083230};
Vmax=4.6 umol/min/mg enzyme for the lysophosphatase reaction
{ECO:0000269|PubMed:8083230};
-!- SUBUNIT: Interacts with KAT5. {ECO:0000269|PubMed:10319815,
ECO:0000269|PubMed:11416127, ECO:0000269|PubMed:9430701,
ECO:0000269|PubMed:9665851}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
Note=Translocates to membrane vesicles in a calcium-dependent
fashion.
-!- TISSUE SPECIFICITY: Expressed in various tissues such as
macrophages, platelets, neutrophils, fibroblasts and lung
endothelium.
-!- DOMAIN: The N-terminal C2 domain associates with lipid membranes
upon calcium binding. It modulates enzyme activity by presenting
the active site to its substrate in response to elevations of
cytosolic Ca(2+). {ECO:0000269|PubMed:9430701,
ECO:0000269|PubMed:9665851}.
-!- PTM: Activated by phosphorylation at both Ser-505 and Ser-727.
{ECO:0000269|PubMed:8381049, ECO:0000269|PubMed:9468497}.
-!- DISEASE: Note=PLA2G4A mutations resulting in phospholipase A2
deficiency have been found in a patient affected by recurrent
episodes of multiple complicated ulcers of the small intestine,
not due to cyclooxygenase inhibitors use. Disease features also
include platelet dysfunction, and globally decreased eicosanoid
synthesis (PubMed:18451993). {ECO:0000269|PubMed:18451993}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pla2g4a/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PLA2G4AID41733ch1q31.html";
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EMBL; M72393; AAB00789.1; -; mRNA.
EMBL; M68874; AAA60105.1; -; mRNA.
EMBL; AY552098; AAS45712.1; -; Genomic_DNA.
EMBL; AL022147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC114340; AAI14341.1; -; mRNA.
CCDS; CCDS1372.1; -.
PIR; A39329; A39329.
RefSeq; NP_001298122.1; NM_001311193.1.
RefSeq; NP_077734.1; NM_024420.2.
RefSeq; XP_011507944.1; XM_011509642.2.
UniGene; Hs.497200; -.
PDB; 1BCI; NMR; -; A=1-138.
PDB; 1CJY; X-ray; 2.50 A; A/B=1-749.
PDB; 1RLW; X-ray; 2.40 A; A=17-141.
PDBsum; 1BCI; -.
PDBsum; 1CJY; -.
PDBsum; 1RLW; -.
ProteinModelPortal; P47712; -.
SMR; P47712; -.
BioGrid; 111338; 34.
DIP; DIP-40991N; -.
IntAct; P47712; 9.
MINT; P47712; -.
STRING; 9606.ENSP00000356436; -.
BindingDB; P47712; -.
ChEMBL; CHEMBL3816; -.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00411; Carbachol.
DrugBank; DB00578; Carbenicillin.
DrugBank; DB05029; Duramycin.
DrugBank; DB00445; Epirubicin.
DrugBank; DB04827; Ethyl carbamate.
DrugBank; DB00591; Fluocinolone Acetonide.
DrugBank; DB00588; Fluticasone Propionate.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB01083; Orlistat.
DrugBank; DB01103; Quinacrine.
DrugBank; DB00086; Streptokinase.
DrugBank; DB04786; Suramin.
GuidetoPHARMACOLOGY; 1424; -.
SwissLipids; SLP:000000565; -.
iPTMnet; P47712; -.
PhosphoSitePlus; P47712; -.
BioMuta; PLA2G4A; -.
DMDM; 317373312; -.
EPD; P47712; -.
MaxQB; P47712; -.
PaxDb; P47712; -.
PeptideAtlas; P47712; -.
PRIDE; P47712; -.
ProteomicsDB; 55788; -.
Ensembl; ENST00000367466; ENSP00000356436; ENSG00000116711.
GeneID; 5321; -.
KEGG; hsa:5321; -.
UCSC; uc001gsc.4; human.
CTD; 5321; -.
DisGeNET; 5321; -.
EuPathDB; HostDB:ENSG00000116711.9; -.
GeneCards; PLA2G4A; -.
HGNC; HGNC:9035; PLA2G4A.
HPA; CAB010050; -.
HPA; HPA050062; -.
HPA; HPA054206; -.
MalaCards; PLA2G4A; -.
MIM; 600522; gene.
neXtProt; NX_P47712; -.
OpenTargets; ENSG00000116711; -.
Orphanet; 468635; Cryptogenic multifocal ulcerous stenosing enteritis.
Orphanet; 477787; Cytosolic phospholipase-A2 alpha deficiency associated bleeding disorder.
PharmGKB; PA271; -.
eggNOG; KOG1012; Eukaryota.
eggNOG; KOG1325; Eukaryota.
eggNOG; ENOG410XR72; LUCA.
GeneTree; ENSGT00940000153184; -.
HOGENOM; HOG000115420; -.
HOVERGEN; HBG053479; -.
InParanoid; P47712; -.
KO; K16342; -.
OMA; WVQRMLM; -.
OrthoDB; EOG091G0276; -.
PhylomeDB; P47712; -.
TreeFam; TF325228; -.
BioCyc; MetaCyc:HS04039-MONOMER; -.
BRENDA; 3.1.1.4; 2681.
Reactome; R-HSA-111995; phospho-PLA2 pathway.
Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
Reactome; R-HSA-1482798; Acyl chain remodeling of CL.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
Reactome; R-HSA-1483115; Hydrolysis of LPC.
Reactome; R-HSA-1483166; Synthesis of PA.
Reactome; R-HSA-2142753; Arachidonic acid metabolism.
Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
SIGNOR; P47712; -.
ChiTaRS; PLA2G4A; human.
EvolutionaryTrace; P47712; -.
GeneWiki; PLA2G4A; -.
GenomeRNAi; 5321; -.
PMAP-CutDB; P47712; -.
PRO; PR:P47712; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116711; Expressed in 190 organ(s), highest expression level in seminal vesicle.
CleanEx; HS_PLA2G4A; -.
Genevisible; P47712; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0005811; C:lipid droplet; IDA:HPA.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; EXP:Reactome.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0004622; F:lysophospholipase activity; TAS:Reactome.
GO; GO:0008970; F:phospholipase A1 activity; TAS:Reactome.
GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
GO; GO:0035965; P:cardiolipin acyl-chain remodeling; TAS:Reactome.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
GO; GO:0046456; P:icosanoid biosynthetic process; IEA:Ensembl.
GO; GO:0006690; P:icosanoid metabolic process; NAS:UniProtKB.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome.
GO; GO:0006663; P:platelet activating factor biosynthetic process; NAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR002642; LysoPLipase_cat_dom.
Pfam; PF00168; C2; 1.
Pfam; PF01735; PLA2_B; 1.
SMART; SM00239; C2; 1.
SMART; SM00022; PLAc; 1.
SUPFAM; SSF52151; SSF52151; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS51210; PLA2C; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Disease mutation;
Hydrolase; Isopeptide bond; Lipid degradation; Lipid metabolism;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Ubl conjugation.
CHAIN 1 749 Cytosolic phospholipase A2.
/FTId=PRO_0000187262.
DOMAIN 5 106 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 140 740 PLA2c. {ECO:0000255|PROSITE-
ProRule:PRU00555}.
REGION 1 178 Phospholipid binding. {ECO:0000305}.
ACT_SITE 228 228 Nucleophile.
{ECO:0000269|PubMed:10319815,
ECO:0000269|PubMed:8083230,
ECO:0000269|PubMed:8619991,
ECO:0000269|PubMed:8702602}.
ACT_SITE 549 549 Proton acceptor.
{ECO:0000269|PubMed:10319815,
ECO:0000269|PubMed:8702602}.
METAL 40 40 Calcium 1.
METAL 40 40 Calcium 2.
METAL 41 41 Calcium 1; via carbonyl oxygen.
METAL 43 43 Calcium 1.
METAL 43 43 Calcium 2.
METAL 65 65 Calcium 1.
METAL 93 93 Calcium 2.
METAL 94 94 Calcium 2; via carbonyl oxygen.
METAL 95 95 Calcium 2.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 268 268 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P50393}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 505 505 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:8381049,
ECO:0000269|PubMed:9468497}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:P50393}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:9468497}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 541 541 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 606 606 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 103 103 G -> R (in dbSNP:rs28395828).
/FTId=VAR_029276.
VARIANT 111 111 S -> P (probable disease-associated
mutation found in a compound heterozygote
affected by phospholipase A2 deficiency
also carrying H-485; dbSNP:rs121434634).
{ECO:0000269|PubMed:18451993}.
/FTId=VAR_070778.
VARIANT 224 224 V -> I (in dbSNP:rs12720588).
{ECO:0000269|Ref.3}.
/FTId=VAR_018760.
VARIANT 442 442 H -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035826.
VARIANT 485 485 R -> H (probable disease-associated
mutation found in a compound heterozygote
affected by phospholipase A2 deficiency
also carrying P-111; dbSNP:rs121434635).
{ECO:0000269|PubMed:18451993}.
/FTId=VAR_070779.
VARIANT 637 637 I -> V (in dbSNP:rs28395831).
/FTId=VAR_062128.
VARIANT 651 651 R -> K (in dbSNP:rs2307198).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18451993,
ECO:0000269|PubMed:1869522,
ECO:0000269|PubMed:1904318,
ECO:0000269|Ref.3}.
/FTId=VAR_018424.
MUTAGEN 139 139 C->A: No effect on phospholipase
activity; when associated with A-141 and
A-151. {ECO:0000269|PubMed:8083230}.
MUTAGEN 141 141 C->A: No effect on phospholipase
activity; when associated with A-139 and
A-151. {ECO:0000269|PubMed:8083230}.
MUTAGEN 151 151 C->A: No effect on phospholipase
activity; when associated with A-139 and
A-141. {ECO:0000269|PubMed:8083230}.
MUTAGEN 195 195 S->A: 5-fold reduced phospholipase and
lysophosphatase activities. 100-fold
reduced phospholipase and lysophosphatase
activities; when associated with A-577.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 200 200 R->A,H: Abolishes phospholipase activity.
{ECO:0000269|PubMed:8702602}.
MUTAGEN 200 200 R->K: Reduces phospholipase activity 200-
fold. {ECO:0000269|PubMed:8702602}.
MUTAGEN 215 215 S->A: No effect on phospholipase or
lysophosphatase activity.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 220 220 C->A: No effect on phospholipase
activity. {ECO:0000269|PubMed:8083230}.
MUTAGEN 228 228 S->A,C,T: Abolishes both phospholipase
and lysophosphatase activities.
{ECO:0000269|PubMed:8083230,
ECO:0000269|PubMed:8619991,
ECO:0000269|PubMed:8702602}.
MUTAGEN 324 324 C->A: No effect on phospholipase
activity; when associated with A-331.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 331 331 C->A: No effect on phospholipase
activity; when associated with A-324.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 505 505 S->A: Decreases agonist-stimulated
release of arachidonic acid.
{ECO:0000269|PubMed:8381049}.
MUTAGEN 549 549 D->A: Abolishes phospholipiase activity.
{ECO:0000269|PubMed:8702602}.
MUTAGEN 549 549 D->E: Reduces phospholipiase activity
2000-fold. {ECO:0000269|PubMed:8702602}.
MUTAGEN 549 549 D->N: Reduces phospholipiase activity
300-fold. {ECO:0000269|PubMed:8702602}.
MUTAGEN 577 577 S->A: 7-fold reduced phospholipase and
lysophosphatase activities. 100-fold
reduced phospholipase and lysophosphatase
activities; when associated with A-195.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 620 620 C->A: No effect on phospholipase
activity; when associated with A-634.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 634 634 C->A: No effect on phospholipase
activity; when associated with A-620.
{ECO:0000269|PubMed:8083230}.
MUTAGEN 726 726 C->A: No effect on phospholipase
activity. {ECO:0000269|PubMed:8083230}.
STRAND 18 29 {ECO:0000244|PDB:1RLW}.
HELIX 34 39 {ECO:0000244|PDB:1RLW}.
STRAND 44 49 {ECO:0000244|PDB:1RLW}.
STRAND 51 54 {ECO:0000244|PDB:1BCI}.
STRAND 57 60 {ECO:0000244|PDB:1BCI}.
STRAND 70 79 {ECO:0000244|PDB:1RLW}.
STRAND 86 93 {ECO:0000244|PDB:1RLW}.
STRAND 96 98 {ECO:0000244|PDB:1CJY}.
STRAND 100 108 {ECO:0000244|PDB:1RLW}.
HELIX 109 111 {ECO:0000244|PDB:1RLW}.
STRAND 117 124 {ECO:0000244|PDB:1RLW}.
TURN 125 127 {ECO:0000244|PDB:1RLW}.
STRAND 128 137 {ECO:0000244|PDB:1RLW}.
STRAND 143 146 {ECO:0000244|PDB:1CJY}.
HELIX 152 177 {ECO:0000244|PDB:1CJY}.
HELIX 179 181 {ECO:0000244|PDB:1CJY}.
STRAND 190 194 {ECO:0000244|PDB:1CJY}.
HELIX 198 214 {ECO:0000244|PDB:1CJY}.
HELIX 218 220 {ECO:0000244|PDB:1CJY}.
STRAND 221 226 {ECO:0000244|PDB:1CJY}.
HELIX 228 239 {ECO:0000244|PDB:1CJY}.
TURN 241 245 {ECO:0000244|PDB:1CJY}.
HELIX 248 260 {ECO:0000244|PDB:1CJY}.
HELIX 263 266 {ECO:0000244|PDB:1CJY}.
HELIX 269 284 {ECO:0000244|PDB:1CJY}.
HELIX 291 304 {ECO:0000244|PDB:1CJY}.
HELIX 305 307 {ECO:0000244|PDB:1CJY}.
HELIX 313 318 {ECO:0000244|PDB:1CJY}.
TURN 319 321 {ECO:0000244|PDB:1CJY}.
STRAND 326 333 {ECO:0000244|PDB:1CJY}.
HELIX 341 343 {ECO:0000244|PDB:1CJY}.
STRAND 344 349 {ECO:0000244|PDB:1CJY}.
STRAND 354 356 {ECO:0000244|PDB:1CJY}.
TURN 357 360 {ECO:0000244|PDB:1CJY}.
STRAND 361 363 {ECO:0000244|PDB:1CJY}.
HELIX 365 367 {ECO:0000244|PDB:1CJY}.
STRAND 370 373 {ECO:0000244|PDB:1CJY}.
STRAND 376 379 {ECO:0000244|PDB:1CJY}.
HELIX 386 393 {ECO:0000244|PDB:1CJY}.
HELIX 396 399 {ECO:0000244|PDB:1CJY}.
HELIX 401 404 {ECO:0000244|PDB:1CJY}.
HELIX 417 423 {ECO:0000244|PDB:1CJY}.
HELIX 426 429 {ECO:0000244|PDB:1CJY}.
HELIX 463 476 {ECO:0000244|PDB:1CJY}.
STRAND 488 490 {ECO:0000244|PDB:1CJY}.
TURN 492 495 {ECO:0000244|PDB:1CJY}.
STRAND 543 548 {ECO:0000244|PDB:1CJY}.
HELIX 550 552 {ECO:0000244|PDB:1CJY}.
HELIX 558 561 {ECO:0000244|PDB:1CJY}.
HELIX 564 566 {ECO:0000244|PDB:1CJY}.
STRAND 570 575 {ECO:0000244|PDB:1CJY}.
HELIX 588 599 {ECO:0000244|PDB:1CJY}.
HELIX 611 615 {ECO:0000244|PDB:1CJY}.
STRAND 619 623 {ECO:0000244|PDB:1CJY}.
STRAND 636 641 {ECO:0000244|PDB:1CJY}.
HELIX 646 648 {ECO:0000244|PDB:1CJY}.
STRAND 650 652 {ECO:0000244|PDB:1CJY}.
HELIX 660 666 {ECO:0000244|PDB:1CJY}.
STRAND 670 672 {ECO:0000244|PDB:1CJY}.
HELIX 687 702 {ECO:0000244|PDB:1CJY}.
HELIX 705 718 {ECO:0000244|PDB:1CJY}.
SEQUENCE 749 AA; 85239 MW; EE71CA0EBE617856 CRC64;
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT
RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFTVS SMKVGEKKEV
PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG
LHSARDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH
PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSRGSTMEEE
LENITTKHIV SNDSSDSDDE SHEPKGTENE DAGSDYQSDN QASWIHRMIM ALVSDSALFN
TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV
KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN
KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY RAPGVPRETE
EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN TLNNIDVIKE AMVESIEYRR
QNPSRCSVSL SNVEARRFFN KEFLSKPKA


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