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Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Calcium-independent phospholipase A2) (Desnutrin) (IPLA2-zeta) (Pigment epithelium-derived factor) (TTS2.2) (Transport-secretion protein 2) (TTS2)

 PLPL2_HUMAN             Reviewed;         504 AA.
Q96AD5; O60643; Q5EFF5; Q6XYE5; Q96ET6; Q9NQ61; Q9NQ62;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 131.
RecName: Full=Patatin-like phospholipase domain-containing protein 2;
EC=3.1.1.3;
AltName: Full=Adipose triglyceride lipase;
AltName: Full=Calcium-independent phospholipase A2;
AltName: Full=Desnutrin;
AltName: Full=IPLA2-zeta;
AltName: Full=Pigment epithelium-derived factor;
AltName: Full=TTS2.2;
AltName: Full=Transport-secretion protein 2;
Short=TTS2;
Name=PNPLA2; Synonyms=ATGL; ORFNames=FP17548;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=15550674; DOI=10.1126/science.1100747;
Zimmermann R., Strauss J.G., Haemmerle G., Schoiswohl G.,
Birner-Gruenberger R., Riederer M., Lass A., Neuberger G.,
Eisenhaber F., Hermetter A., Zechner R.;
"Fat mobilization in adipose tissue is promoted by adipose
triglyceride lipase.";
Science 306:1383-1386(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-481.
Strahl T., Shingler W.H., Lammiman M., Gregory C.D., Leach L.,
Matthias P., Nielsen P.J., Shaw P.E.;
"TTS-2, a novel protein implicated in vesicular transport of the cell
surface receptor ICAM-3.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-481.
TISSUE=Brain, and Eye;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-504 (ISOFORM 1).
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND ENZYME REGULATION.
PubMed=15364929; DOI=10.1074/jbc.M407841200;
Jenkins C.M., Mancuso D.J., Yan W., Sims H.F., Gibson B., Gross R.W.;
"Identification, cloning, expression, and purification of three novel
human calcium-independent phospholipase A2 family members possessing
triacylglycerol lipase and acylglycerol transacylase activities.";
J. Biol. Chem. 279:48968-48975(2004).
[7]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=16249444; DOI=10.2337/diabetes.54.11.3190;
Langin D., Dicker A., Tavernier G., Hoffstedt J., Mairal A., Ryden M.,
Arner E., Sicard A., Jenkins C.M., Viguerie N., van Harmelen V.,
Gross R.W., Holm C., Arner P.;
"Adipocyte lipases and defect of lipolysis in human obesity.";
Diabetes 54:3190-3197(2005).
[8]
TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-47.
PubMed=16150821; DOI=10.1194/jlr.M500290-JLR200;
Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T.,
Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.;
"Expression, regulation, and triglyceride hydrolase activity of
Adiponutrin family members.";
J. Lipid Res. 46:2477-2487(2005).
[9]
DEVELOPMENTAL STAGE.
PubMed=16705060; DOI=10.1152/ajpendo.00317.2005;
Kim J.Y., Tillison K., Lee J.-H., Rearick D.A., Smas C.M.;
"The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated
by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for
transactivation by PPARgamma.";
Am. J. Physiol. 291:E115-E127(2006).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-47.
PubMed=16239926; DOI=10.1038/sj.embor.7400559;
Smirnova E., Goldberg E.B., Makarova K.S., Lin L., Brown W.J.,
Jackson C.L.;
"ATGL has a key role in lipid droplet/adiposome degradation in
mammalian cells.";
EMBO Rep. 7:106-113(2006).
[11]
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH
SERPINF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=17032652; DOI=10.1074/jbc.M600353200;
Notari L., Baladron V., Aroca-Aguilar J.D., Balko N., Heredia R.,
Meyer C., Notario P.M., Saravanamuthu S., Nueda M.-L.,
Sanchez-Sanchez F., Escribano J., Laborda J., Becerra S.P.;
"Identification of a lipase-linked cell membrane receptor for pigment
epithelium-derived factor.";
J. Biol. Chem. 281:38022-38037(2006).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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).
[14]
PHOSPHORYLATION AT SER-404.
PubMed=22733971; DOI=10.1210/en.2012-1127;
Pagnon J., Matzaris M., Stark R., Meex R.C., Macaulay S.L., Brown W.,
O'Brien P.E., Tiganis T., Watt M.J.;
"Identification and functional characterization of protein kinase A
phosphorylation sites in the major lipolytic protein, adipose
triglyceride lipase.";
Endocrinology 153:4278-4289(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND SER-428, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[16]
INTERACTION WITH FAF2.
PubMed=23297223; DOI=10.1073/pnas.1213738110;
Olzmann J.A., Richter C.M., Kopito R.R.;
"Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid
droplet turnover.";
Proc. Natl. Acad. Sci. U.S.A. 110:1345-1350(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
PHOSPHORYLATION AT SER-404.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[19]
VARIANTS PHE-219; LYS-252 AND PRO-481, POLYMORPHISM, AND ASSOCIATION
WITH DIABETES MELLITUS TYPE 2.
PubMed=16644682; DOI=10.2337/db05-1498;
Schoenborn V., Heid I.M., Vollmert C., Lingenhel A., Adams T.D.,
Hopkins P.N., Illig T., Zimmermann R., Zechner R., Hunt S.C.,
Kronenberg F.;
"The ATGL gene is associated with free fatty acids, triglycerides, and
type 2 diabetes.";
Diabetes 55:1270-1275(2006).
[20]
VARIANT NLSDM LEU-195.
PubMed=17187067; DOI=10.1038/ng1951;
Fischer J., Lefevre C., Morava E., Mussini J.-M., Laforet P.,
Negre-Salvayre A., Lathrop M., Salvayre R.;
"The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in
neutral lipid storage disease with myopathy.";
Nat. Genet. 39:28-30(2007).
-!- FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in
adipocyte and non-adipocyte lipid droplets (PubMed:15550674). Also
has acylglycerol transacylase activity. May act coordinately with
LIPE/HLS within the lipolytic cascade. Regulates adiposome size
and may be involved in the degradation of adiposomes
(PubMed:16239926). May play an important role in energy
homeostasis. May play a role in the response of the organism to
starvation, enhancing hydrolysis of triglycerides and providing
free fatty acids to other tissues to be oxidized in situations of
energy depletion. {ECO:0000269|PubMed:15364929,
ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16239926}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate.
-!- ENZYME REGULATION: Inhibited by BEL ((E)-6-(bromomethylene)-3-(1-
naphthalenyl)-2H-tetrahydropyran-2-one), a suicide substrate
inhibitor. No differences in enzymatic activity that uses (1,2-
dilinoleoyl)-phosphatidylcholine as substrate was detected in the
presence or absence of ATP. Activated by ABHD5 and SERPINF1.
{ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:17032652}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.5 with (1,2-dilinoleoyl)-phosphatidylcholine as
substrate. {ECO:0000269|PubMed:17032652};
-!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
-!- SUBUNIT: Interacts with ABHD5; this association stimulates PNPLA2
triglyceride hydrolase activity (By similarity). Interacts with
SERPINF1; interacts at one site of interaction. Despite a
colocalization in lipid droplets, it probably does not interact
with PLIN (By similarity). Interacts with PLIN5; prevents
interaction with ABHD5 (By similarity). Interacts with FAF2
(PubMed:23297223). {ECO:0000250|UniProtKB:Q8BJ56,
ECO:0000269|PubMed:23297223}.
-!- SUBCELLULAR LOCATION: Lipid droplet. Cell membrane; Single-pass
type II membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96AD5-1; Sequence=Displayed;
Name=2;
IsoId=Q96AD5-2; Sequence=VSP_026421;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Also
detected in heart, skeletal muscle, and portions of the
gastrointestinal tract. Detected in normal retina and
retinoblastoma cells. Detected in retinal pigment epithelium and,
at lower intensity, in the inner segments of photoreceptors and in
the ganglion cell layer of the neural retina (at protein level).
{ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821,
ECO:0000269|PubMed:16249444, ECO:0000269|PubMed:17032652}.
-!- DEVELOPMENTAL STAGE: Induced during differentiation of primary
preadipocytes to adipocytes. Expression increased from fetal to
adult in retinal pigment epithelium. {ECO:0000269|PubMed:16249444,
ECO:0000269|PubMed:16705060, ECO:0000269|PubMed:17032652}.
-!- PTM: Phosphorylation at Ser-404 by PKA is increased during fasting
and moderate intensity exercise, and moderately increases
lipolytic activity (By similarity). Phosphorylation at Ser-404 is
increased upon beta-adrenergic stimulation. {ECO:0000250,
ECO:0000269|PubMed:22733971}.
-!- POLYMORPHISM: Genetic variations in PNPLA2 may influence plasma
free fatty acids and triglycerides levels, and fasting glucose
concentrations. {ECO:0000269|PubMed:16644682}.
-!- DISEASE: Note=Genetic variations in PNPLA2 may be associated with
risk of diabetes mellitus type 2. {ECO:0000269|PubMed:16644682}.
-!- DISEASE: Neutral lipid storage disease with myopathy (NLSDM)
[MIM:610717]: Neutral lipid storage disorder (NLSD) with myopathy
but without ichthyosis. NLSDs are characterized by the presence of
triglyceride-containing cytoplasmic droplets in leukocytes and in
other tissues, including bone marrow, skin, and muscle.
Individuals with NLSDM did not show obesity, in spite of a defect
in triglyceride degradation in fibroblasts and in marked
triglyceride storage in liver, muscles, and other visceral cells.
{ECO:0000269|PubMed:17187067}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAP34448.1; Type=Frameshift; Positions=501; Evidence={ECO:0000305};
Sequence=CAC01131.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAC01132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY894804; AAW81962.1; -; mRNA.
EMBL; AJ278475; CAC01131.1; ALT_INIT; mRNA.
EMBL; AJ278476; CAC01132.1; ALT_INIT; mRNA.
EMBL; AY203925; AAP34448.1; ALT_FRAME; mRNA.
EMBL; BC011958; AAH11958.1; -; mRNA.
EMBL; BC017280; AAH17280.1; -; mRNA.
EMBL; AF055000; AAC09354.1; -; mRNA.
CCDS; CCDS7718.1; -. [Q96AD5-1]
RefSeq; NP_065109.1; NM_020376.3. [Q96AD5-1]
RefSeq; XP_016873517.1; XM_017018028.1. [Q96AD5-1]
UniGene; Hs.654697; -.
ProteinModelPortal; Q96AD5; -.
BioGrid; 121370; 19.
IntAct; Q96AD5; 7.
MINT; Q96AD5; -.
STRING; 9606.ENSP00000337701; -.
ChEMBL; CHEMBL3822353; -.
SwissLipids; SLP:000000311; -.
iPTMnet; Q96AD5; -.
PhosphoSitePlus; Q96AD5; -.
BioMuta; PNPLA2; -.
DMDM; 74731110; -.
EPD; Q96AD5; -.
MaxQB; Q96AD5; -.
PaxDb; Q96AD5; -.
PeptideAtlas; Q96AD5; -.
PRIDE; Q96AD5; -.
ProteomicsDB; 75955; -.
ProteomicsDB; 75956; -. [Q96AD5-2]
DNASU; 57104; -.
Ensembl; ENST00000336615; ENSP00000337701; ENSG00000177666. [Q96AD5-1]
GeneID; 57104; -.
KEGG; hsa:57104; -.
UCSC; uc001lrt.4; human. [Q96AD5-1]
CTD; 57104; -.
DisGeNET; 57104; -.
EuPathDB; HostDB:ENSG00000177666.15; -.
GeneCards; PNPLA2; -.
HGNC; HGNC:30802; PNPLA2.
HPA; HPA055173; -.
HPA; HPA062602; -.
MalaCards; PNPLA2; -.
MIM; 609059; gene.
MIM; 610717; phenotype.
neXtProt; NX_Q96AD5; -.
OpenTargets; ENSG00000177666; -.
Orphanet; 98908; Neutral lipid storage myopathy.
PharmGKB; PA134903083; -.
eggNOG; KOG3773; Eukaryota.
eggNOG; ENOG410XSQS; LUCA.
GeneTree; ENSGT00390000005295; -.
HOVERGEN; HBG007046; -.
InParanoid; Q96AD5; -.
KO; K16816; -.
OMA; TGVCLGE; -.
OrthoDB; EOG091G05MG; -.
PhylomeDB; Q96AD5; -.
TreeFam; TF314272; -.
Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
UniPathway; UPA00256; -.
ChiTaRS; PNPLA2; human.
GeneWiki; PNPLA2; -.
GenomeRNAi; 57104; -.
PRO; PR:Q96AD5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000177666; -.
CleanEx; HS_PNPLA2; -.
Genevisible; Q96AD5; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016411; F:acylglycerol O-acyltransferase activity; TAS:Reactome.
GO; GO:0004465; F:lipoprotein lipase activity; TAS:Reactome.
GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
GO; GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
GO; GO:0034389; P:lipid particle organization; IEA:Ensembl.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway.
CDD; cd07220; Pat_PNPLA2; 1.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR033562; PLPL.
InterPro; IPR033903; PNPLA2.
InterPro; IPR002641; PNPLA_dom.
PANTHER; PTHR12406; PTHR12406; 1.
Pfam; PF01734; Patatin; 1.
SUPFAM; SSF52151; SSF52151; 1.
PROSITE; PS51635; PNPLA; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Glycoprotein; Hydrolase; Lipid degradation;
Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 504 Patatin-like phospholipase domain-
containing protein 2.
/FTId=PRO_0000292527.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 504 Lumenal. {ECO:0000255}.
DOMAIN 10 179 PNPLA. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOTIF 14 19 GXGXXG. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOTIF 45 49 GXSXG. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOTIF 166 168 DGA/G. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
ACT_SITE 47 47 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOD_RES 372 372 Phosphoserine; in vitro.
{ECO:0000250|UniProtKB:Q8BJ56}.
MOD_RES 404 404 Phosphoserine; by PKA and FAM20C.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22733971,
ECO:0000269|PubMed:26091039}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 324 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_026421.
VARIANT 195 195 P -> L (in NLSDM; dbSNP:rs121918259).
{ECO:0000269|PubMed:17187067}.
/FTId=VAR_032995.
VARIANT 219 219 L -> F (in dbSNP:rs140612115).
{ECO:0000269|PubMed:16644682}.
/FTId=VAR_032996.
VARIANT 252 252 N -> K (in dbSNP:rs140201358).
{ECO:0000269|PubMed:16644682}.
/FTId=VAR_032997.
VARIANT 481 481 L -> P (in dbSNP:rs1138693).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16644682,
ECO:0000269|Ref.2}.
/FTId=VAR_032998.
MUTAGEN 47 47 S->A: Reduces rate of lipid hydrolysis;
does not affect the localization around
the rim of the adiposomes.
{ECO:0000269|PubMed:16150821,
ECO:0000269|PubMed:16239926}.
CONFLICT 163 163 R -> G (in Ref. 5; AAC09354).
{ECO:0000305}.
CONFLICT 296 296 I -> V (in Ref. 1; AAW81962).
{ECO:0000305}.
CONFLICT 333 333 A -> G (in Ref. 3; AAP34448).
{ECO:0000305}.
CONFLICT 351 351 R -> C (in Ref. 1; AAW81962).
{ECO:0000305}.
CONFLICT 402 402 V -> L (in Ref. 2; CAC01131/CAC01132).
{ECO:0000305}.
CONFLICT 419 419 L -> P (in Ref. 1; AAW81962).
{ECO:0000305}.
SEQUENCE 504 AA; 55316 MW; D9C16F942AB0B3C7 CRC64;
MFPREKTWNI SFAGCGFLGV YYVGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGV
CLGEAGAKFI EVSKEARKRF LGPLHPSFNL VKIIRSFLLK VLPADSHEHA SGRLGISLTR
VSDGENVIIS HFNSKDELIQ ANVCSGFIPV YCGLIPPSLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PLVLREMCKQ
GYRDGLRFLQ RNGLLNRPNP LLALPPARPH GPEDKDQAVE SAQAEDYSQL PGEDHILEHL
PARLNEALLE ACVEPTDLLT TLSNMLPVRL ATAMMVPYTL PLESALSFTI RLLEWLPDVP
EDIRWMKEQT GSICQYLVMR AKRKLGRHLP SRLPEQVELR RVQSLPSVPL SCAAYREALP
GWMRNNLSLG DALAKWEECQ RQLLLGLFCT NVAFPPEALR MRAPADPAPA PADPASPQHQ
LAGPAPLLST PAPEARPVIG ALGL


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EIAAB31564 Adipose triglyceride lipase,ATGL,Calcium-independent phospholipase A2,Desnutrin,FP17548,Homo sapiens,Human,IPLA2-zeta,Patatin-like phospholipase domain-containing protein 2,Pigment epithelium-derived
EIAAB31565 Adipose triglyceride lipase,Atgl,Desnutrin,Mouse,Mus musculus,Patatin-like phospholipase domain-containing protein 2,Pnpla2
EIAAB31576 Calcium-independent phospholipase A2-gamma,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,Ipla22,Ipla2g,iPLA2-gamma,Mouse,Mus musculus,Patatin-like phospholipase domain-c
EIAAB31566 Acylglycerol O-acyltransferase,Adiponutrin,Adpn,Calcium-independent phospholipase A2-epsilon,iPLA2-epsilon,Mouse,Mus musculus,Patatin-like phospholipase domain-containing protein 3,Pnpla3
EIAAB31567 Acylglycerol O-acyltransferase,Adiponutrin,ADPN,C22orf20,Calcium-independent phospholipase A2-epsilon,Homo sapiens,Human,iPLA2-epsilon,Patatin-like phospholipase domain-containing protein 3,PNPLA3
EIAAB31575 BM-043,Calcium-independent phospholipase A2-gamma,Homo sapiens,Human,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,IPLA22,iPLA2-2,IPLA2G,iPLA2-gamma,Patatin-like phospho
EIAAB31562 Adipose triglyceride lipase,Atgl,Patatin-like phospholipase domain-containing protein 2,Pnpla2,Rat,Rattus norvegicus
EIAAB31563 Adipose triglyceride lipase,ATGL,Bos taurus,Bovine,Patatin-like phospholipase domain-containing protein 2,PNPLA2
EIAAB31574 Calcium-independent phospholipase A2-gamma,Group VIB calcium-independent phospholipase A2,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,iPLA2-gamma,Oryctolagus cuniculus
U0411h CLIA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,Homo sapiens,Human,iPLA2,IPLA2,PLA2G6 96T
E0411h ELISA kit 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,Homo sapiens,Human,iPLA2,IPLA2,PLA2G6 96T
E0411h ELISA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,Homo sapiens,Human,iPLA2,IPLA2,PLA2G6 96T
DL-iPLA2-Hu Human Phospholipase A2,Calcium Independent (iPLA2) ELISA Kit 96T
DL-iPLA2-Mu Mouse Phospholipase A2, Calcium Independent (iPLA2) ELISA Kit 96T
DL-iPLA2-Ra Rat Phospholipase A2, Calcium Independent (iPLA2) ELISA Kit 96T
U0411m CLIA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Mouse,Mus musculus,Pla2g6 96T
E0411m ELISA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Mouse,Mus musculus,Pla2g6 96T
U0411r CLIA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Pla2g6,Rat,Rattus norvegicus 96T
E0411m ELISA kit 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Mouse,Mus musculus,Pla2g6 96T
E0411r ELISA kit 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Pla2g6,Rat,Rattus norvegicus 96T
E0411r ELISA 85 kDa calcium-independent phospholipase A2,CaI-PLA2,Group VI phospholipase A2,GVI PLA2,iPLA2,Pla2g6,Rat,Rattus norvegicus 96T
E90411Ra ELISA Kit for Rat Phospholipase A2,Calcium Independent(iPLA2) 96T
UB-E10544 Rat Phospholipase A2(Calcium Independent(iPLA2)ELISA kit 96T
201-11-1101 Rat Phospholipase A2, Calcium Independent (iPLA2)ELISA kit 96T
E90411Hu ELISA Kit for Phospholipase A2, Calcium Independent (iPLA2) 96T/Kit


 

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