Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Desnutrin)

 PLPL2_MOUSE             Reviewed;         486 AA.
Q8BJ56; O89080; Q05BJ0; Q3UD97; Q643S0; Q6P234; Q9D1Q9; Q9DCF6;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 120.
RecName: Full=Patatin-like phospholipase domain-containing protein 2;
EC=3.1.1.3;
AltName: Full=Adipose triglyceride lipase;
AltName: Full=Desnutrin;
Name=Pnpla2; Synonyms=Atgl;
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), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=C57BL/6J; TISSUE=White adipose tissue;
PubMed=15337759; DOI=10.1074/jbc.M403855200;
Villena J.A., Roy S., Sarkadi-Nagy E., Kim K.-H., Sul H.S.;
"Desnutrin, an adipocyte gene encoding a novel patatin domain-
containing protein, is induced by fasting and glucocorticoids: ectopic
expression of desnutrin increases triglyceride hydrolysis.";
J. Biol. Chem. 279:47066-47075(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
PHOSPHORYLATION.
STRAIN=C57BL/6J;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=C57BL/6J;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Testis;
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 MRNA] (ISOFORMS 1 AND 3).
STRAIN=FVB/N; TISSUE=Trophoblast stem cell;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-473.
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
Chu C.C., Paul W.E.;
"Expressed genes in interleukin-4 treated B cells identified by cDNA
representational difference analysis.";
Mol. Immunol. 35:487-502(1998).
[7]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
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).
[8]
INDUCTION.
PubMed=16009485; DOI=10.1016/j.mce.2005.06.002;
Kralisch S., Klein J., Lossner U., Bluher M., Paschke R., Stumvoll M.,
Fasshauer M.;
"Isoproterenol, TNFalpha, and insulin downregulate adipose
triglyceride lipase in 3T3-L1 adipocytes.";
Mol. Cell. Endocrinol. 240:43-49(2005).
[9]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABHD5, AND MUTAGENESIS
OF SER-47.
PubMed=16679289; DOI=10.1016/j.cmet.2006.03.005;
Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G.,
Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G.,
Zechner R.;
"Adipose triglyceride lipase-mediated lipolysis of cellular fat stores
is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.";
Cell Metab. 3:309-319(2006).
[10]
INDUCTION.
PubMed=16380488; DOI=10.2337/diabetes.55.01.06.db05-0982;
Kershaw E.E., Hamm J.K., Verhagen L.A.W., Peroni O., Katic M.,
Flier J.S.;
"Adipose triglyceride lipase: function, regulation by insulin, and
comparison with adiponutrin.";
Diabetes 55:148-157(2006).
[11]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=17074755; DOI=10.1074/jbc.M608048200;
Schweiger M., Schreiber R., Haemmerle G., Lass A., Fledelius C.,
Jacobsen P., Tornqvist H., Zechner R., Zimmermann R.;
"Adipose triglyceride lipase and hormone-sensitive lipase are the
major enzymes in adipose tissue triacylglycerol catabolism.";
J. Biol. Chem. 281:40236-40241(2006).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16675698; DOI=10.1126/science.1123965;
Haemmerle G., Lass A., Zimmermann R., Gorkiewicz G., Meyer C.,
Rozman J., Heldmaier G., Maier R., Theussl C., Eder S., Kratky D.,
Wagner E.F., Klingenspor M., Hoefler G., Zechner R.;
"Defective lipolysis and altered energy metabolism in mice lacking
adipose triglyceride lipase.";
Science 312:734-737(2006).
[13]
ACTIVITY REGULATION.
PubMed=17114792; DOI=10.1074/jbc.M605770200;
Miyoshi H., Perfield J.W. II, Souza S.C., Shen W.-J., Zhang H.-H.,
Stancheva Z.S., Kraemer F.B., Obin M.S., Greenberg A.S.;
"Control of adipose triglyceride lipase action by serine 517 of
perilipin A globally regulates protein kinase A-stimulated lipolysis
in adipocytes.";
J. Biol. Chem. 282:996-1002(2007).
[14]
INTERACTION WITH ABHD5, AND LACK OF INTERACTION WITH PLIN.
PubMed=17189257; DOI=10.1074/jbc.M610580200;
Granneman J.G., Moore H.-P.H., Granneman R.L., Greenberg A.S.,
Obin M.S., Zhu Z.;
"Analysis of lipolytic protein trafficking and interactions in
adipocytes.";
J. Biol. Chem. 282:5726-5735(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-430, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
INTERACTION WITH PLIN5, AND EXCLUSION OF INTERACTION WITH ABHD5.
PubMed=21148142; DOI=10.1074/jbc.M110.180711;
Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.;
"Interactions of perilipin-5 (Plin5) with adipose triglyceride
lipase.";
J. Biol. Chem. 286:5126-5135(2011).
[17]
INTERACTION WITH PLIN5.
PubMed=21393244; DOI=10.1074/jbc.M110.207779;
Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J.,
Dalen K., Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D.,
Brasaemle D., Sztalryd C.;
"Unique regulation of adipose triglyceride lipase (ATGL) by perilipin
5, a lipid droplet-associated protein.";
J. Biol. Chem. 286:15707-15715(2011).
[18]
PHOSPHORYLATION AT SER-374; SER-396; SER-406; SER-430 AND SER-468, AND
MUTAGENESIS OF SER-396 AND SER-406.
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).
-!- 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. 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:15337759, ECO:0000269|PubMed:15550674,
ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698,
ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:16679289}.
-!- ACTIVITY REGULATION: Stimulated by PKA-dependent PLIN
phosphorylation. {ECO:0000269|PubMed:15550674,
ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:17114792}.
-!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
-!- SUBUNIT: Interacts with ABHD5; this association stimulates PNPLA2
triglyceride hydrolase activity (PubMed:16679289,
PubMed:17189257). Interacts with SERPINF1; interacts at one site
of interaction (By similarity). Despite a colocalization in lipid
droplets, it probably does not interact with PLIN. Interacts with
PLIN5; prevents interaction with ABHD5 (PubMed:21148142,
PubMed:21393244). Interacts with FAF2 (By similarity).
{ECO:0000250|UniProtKB:Q96AD5, ECO:0000269|PubMed:16679289,
ECO:0000269|PubMed:17189257, ECO:0000269|PubMed:21148142,
ECO:0000269|PubMed:21393244}.
-!- SUBCELLULAR LOCATION: Lipid droplet. Cell membrane; Single-pass
type II membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8BJ56-1; Sequence=Displayed;
Name=2;
IsoId=Q8BJ56-2; Sequence=VSP_026424;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8BJ56-3; Sequence=VSP_026422, VSP_026423;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in white and brown
adipose tissue, and to a lesser degree in testis and cardiac
muscle. Barely detected in liver, spleen, thymus, kidney, skeletal
muscle, and brain. Among the white adipose depots, gonadal fat
showed the highest level of expression compared with inguinal and
renal white adipose tissues. {ECO:0000269|PubMed:15337759,
ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821,
ECO:0000269|PubMed:16705060}.
-!- DEVELOPMENTAL STAGE: Increased expression when preadipocytes are
induced to differentiate to adipocytes. Not detected in
proliferating or confluent preadipocytes.
{ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674,
ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16705060}.
-!- INDUCTION: Transiently induced during fasting. cAMP and glucagon
may not be involved in the induction during fasting. Induced by
dexamethasone. Down-regulated by insulin, isoprotenerol and TNF-
alfa. Expression is not affected by glucose and by growth hormone.
Expression is reduced in fasted leptin deficient mouse (ob/ob), an
obese mouse model. Expression is not affected in fed ob/ob mouse.
{ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:16009485,
ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16380488,
ECO:0000269|PubMed:16705060}.
-!- PTM: Phosphorylation at Ser-406 by PKA is increased during fasting
and moderate intensity exercise, and moderately increases
lipolytic activity. {ECO:0000269|PubMed:15550674,
ECO:0000269|PubMed:22733971}.
-!- DISRUPTION PHENOTYPE: Mice show increased adipose mass and
triacylglycerol deposition in multiple tissues. They accumulate
large amounts of lipid in the heart, causing cardiac dysfunction
and premature death. {ECO:0000269|PubMed:16675698}.
-!- SEQUENCE CAUTION:
Sequence=BAB22643.1; Type=Frameshift; Positions=301, 317, 460; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY731699; AAU33824.1; -; mRNA.
EMBL; AY894805; AAW81963.1; -; mRNA.
EMBL; AY510273; AAS48458.1; -; mRNA.
EMBL; AK002826; BAB22387.1; -; mRNA.
EMBL; AK003207; BAB22643.1; ALT_FRAME; mRNA.
EMBL; AK031609; BAC27476.1; -; mRNA.
EMBL; AK150184; BAE29364.1; -; mRNA.
EMBL; BC019188; AAH19188.1; -; mRNA.
EMBL; BC044781; AAH44781.1; -; mRNA.
EMBL; BC064747; AAH64747.1; -; mRNA.
EMBL; U89431; AAC36536.1; -; mRNA.
CCDS; CCDS22015.1; -. [Q8BJ56-2]
CCDS; CCDS52445.1; -. [Q8BJ56-1]
RefSeq; NP_001157161.1; NM_001163689.1. [Q8BJ56-1]
RefSeq; NP_080078.2; NM_025802.3. [Q8BJ56-2]
UniGene; Mm.29998; -.
ProteinModelPortal; Q8BJ56; -.
BioGrid; 211763; 5.
DIP; DIP-61641N; -.
IntAct; Q8BJ56; 2.
STRING; 10090.ENSMUSP00000127149; -.
BindingDB; Q8BJ56; -.
ChEMBL; CHEMBL3425391; -.
SwissLipids; SLP:000000317; -.
iPTMnet; Q8BJ56; -.
PhosphoSitePlus; Q8BJ56; -.
SwissPalm; Q8BJ56; -.
PaxDb; Q8BJ56; -.
PeptideAtlas; Q8BJ56; -.
PRIDE; Q8BJ56; -.
Ensembl; ENSMUST00000064151; ENSMUSP00000065116; ENSMUSG00000025509. [Q8BJ56-2]
Ensembl; ENSMUST00000164016; ENSMUSP00000127149; ENSMUSG00000025509. [Q8BJ56-1]
GeneID; 66853; -.
KEGG; mmu:66853; -.
UCSC; uc009klg.2; mouse. [Q8BJ56-2]
UCSC; uc009klh.2; mouse. [Q8BJ56-3]
UCSC; uc009kli.2; mouse. [Q8BJ56-1]
CTD; 57104; -.
MGI; MGI:1914103; Pnpla2.
eggNOG; KOG3773; Eukaryota.
eggNOG; ENOG410XSQS; LUCA.
GeneTree; ENSGT00390000005295; -.
HOVERGEN; HBG007046; -.
InParanoid; Q8BJ56; -.
KO; K16816; -.
OMA; TGVCLGE; -.
OrthoDB; EOG091G05MG; -.
PhylomeDB; Q8BJ56; -.
TreeFam; TF314272; -.
BRENDA; 3.1.1.3; 3474.
Reactome; R-MMU-1482883; Acyl chain remodeling of DAG and TAG.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
UniPathway; UPA00256; -.
ChiTaRS; Pnpla2; mouse.
PRO; PR:Q8BJ56; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025509; Expressed in 277 organ(s), highest expression level in brown adipose tissue.
CleanEx; MM_PNPLA2; -.
ExpressionAtlas; Q8BJ56; baseline and differential.
Genevisible; Q8BJ56; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
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; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
GO; GO:0044242; P:cellular lipid catabolic process; IMP:MGI.
GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
GO; GO:0034389; P:lipid particle organization; IMP:MGI.
GO; GO:0019915; P:lipid storage; IMP:UniProtKB.
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:0019433; P:triglyceride catabolic process; IMP:MGI.
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; Glycoprotein;
Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism;
Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 486 Patatin-like phospholipase domain-
containing protein 2.
/FTId=PRO_0000292528.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 486 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 374 374 Phosphoserine; in vitro.
{ECO:0000269|PubMed:22733971}.
MOD_RES 396 396 Phosphoserine; by PKA.
{ECO:0000269|PubMed:22733971}.
MOD_RES 406 406 Phosphoserine; by PKA.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:22733971}.
MOD_RES 430 430 Phosphoserine; in vitro.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:22733971}.
MOD_RES 468 468 Phosphoserine; in vitro.
{ECO:0000269|PubMed:22733971}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 56 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026422.
VAR_SEQ 57 62 VTGACL -> MSHACQ (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026423.
VAR_SEQ 253 308 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_026424.
MUTAGEN 47 47 S->A: Loss of triacylglycerol hydrolysis
activity. {ECO:0000269|PubMed:16679289}.
MUTAGEN 396 396 S->A: Slightly reduced TG hydrolase
activity. {ECO:0000269|PubMed:22733971}.
MUTAGEN 406 406 S->A: Reduced TG hydrolase activity.
{ECO:0000269|PubMed:22733971}.
CONFLICT 3 3 P -> T (in Ref. 4; BAB22387).
{ECO:0000305}.
CONFLICT 30 30 R -> H (in Ref. 1; AAU33824).
{ECO:0000305}.
CONFLICT 193 193 I -> V (in Ref. 4; BAE29364).
{ECO:0000305}.
CONFLICT 319 320 DL -> VG (in Ref. 4; BAB22643).
{ECO:0000305}.
CONFLICT 362 362 P -> T (in Ref. 4; BAE29364).
{ECO:0000305}.
CONFLICT 385 385 R -> G (in Ref. 6; AAC36536).
{ECO:0000305}.
CONFLICT 389 389 D -> G (in Ref. 5; AAH64747).
{ECO:0000305}.
CONFLICT 412 412 L -> P (in Ref. 6; AAC36536).
{ECO:0000305}.
SEQUENCE 486 AA; 53657 MW; 512FE1931B72FC9C CRC64;
MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGA
CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK TLPADCHERA NGRLGISLTR
VSDGENVIIS HFSSKDELIQ ANVCSTFIPV YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ
GYRDGLRFLR RNGLLNQPNP LLALPPVVPQ EEDAEEAAVV EERAGEEDQL QPYRKDRILE
HLPARLNEAL LEACVEPKDL MTTLSNMLPV RLATAMMVPY TLPLESAVSF TIRLLEWLPD
VPEDIRWMKE QTGSICQYLV MRAKRKLGDH LPSRLSEQVE LRRAQSLPSV PLSCATYSEA
LPNWVRNNLS LGDALAKWEE CQRQLLLGLF CTNVAFPPDA LRMRAPASPT AADPATPQDP
PGLPPC


Related products :

Catalog number Product name Quantity
EIAAB31565 Adipose triglyceride lipase,Atgl,Desnutrin,Mouse,Mus musculus,Patatin-like phospholipase domain-containing protein 2,Pnpla2
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
EIAAB31563 Adipose triglyceride lipase,ATGL,Bos taurus,Bovine,Patatin-like phospholipase domain-containing protein 2,PNPLA2
EIAAB31562 Adipose triglyceride lipase,Atgl,Patatin-like phospholipase domain-containing protein 2,Pnpla2,Rat,Rattus norvegicus
YF-PA20119 anti-Adipose Triglyceride Lipase 50 ug
E02A0057 Rat Adipose Triglyceride Lipase ELISA 96T/kit
ER750 Adipose Triglyceride Lipase Elisa Kit 96T
E01A0893 Human Adipose Triglyceride Lipase 96 Tests/kit
YF-MA19023 anti-Adipose Triglyceride Lipase (2H1) 100 ug
E01A0893 Human Anti-Adipose Triglyceride Lipase 96 Tests/kit
E05A0057 Guinea Pig Adipose Triglyceride Lipase ELISA 96T/kit
E02A0893 Rat Adipose Triglyceride Lipase ELISA , ATGL
NBL1-14554 Adipose Triglyceride Lipase Lysate 0.1 mg
KN0928Ra Rat Adipose Triglyceride Lipase(ATGL)ELISA Kit 96 WELLS
E09A0057 Monkey Adipose Triglyceride Lipase ELISA 96T/kit
E12A0057 Chicken Adipose Triglyceride Lipase ELISA 96T/kit
E02A0893 Rat Adipose Triglyceride Lipase ELISA , ATGL 96 Tests/kit
E01A0057 Human Adipose Triglyceride Lipase ELISA 96T/kit
E14A0057 Sheep Adipose Triglyceride Lipase ELISA 96T/kit
CSB-E14127r Rat Adipose Triglyceride Lipase,ATGL ELISA Kit 96T
E04A0057 Rabbit Adipose Triglyceride Lipase ELISA 96T/kit
E11A0057 Bovine Adipose Triglyceride Lipase ELISA 96T/kit
Y050500 Anti_ATGL(adipose triglyceride lipase)_(C_terminal) 100ug
E-EL-R0387 Rat ATGL (Adipose Triglyceride Lipase) ELISA Kit 96T
E06A0057 Goat Adipose Triglyceride Lipase ELISA 96T/kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur