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

 PLPL2_RAT               Reviewed;         478 AA.
P0C548;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 1.
20-JUN-2018, entry version 84.
RecName: Full=Patatin-like phospholipase domain-containing protein 2;
EC=3.1.1.3;
AltName: Full=Adipose triglyceride lipase;
Name=Pnpla2; Synonyms=Atgl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
INDUCTION.
PubMed=16906479; DOI=10.1007/s00125-006-0336-y;
Festuccia W.T., Laplante M., Berthiaume M., Gelinas Y., Deshaies Y.;
"PPARgamma agonism increases rat adipose tissue lipolysis, expression
of glyceride lipases, and the response of lipolysis to hormonal
control.";
Diabetologia 49:2427-2436(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[4]
INTERACTION WITH PLIN5.
PubMed=23408028; DOI=10.1152/ajpregu.00418.2012;
MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.;
"Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest
and following stimulated contraction.";
Am. J. Physiol. 304:R644-R650(2013).
[5]
INTERACTION WITH PLIN5.
PubMed=24303154; DOI=10.1002/phy2.84;
Macpherson R.E., Vandenboom R., Roy B.D., Peters S.J.;
"Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and
following lipolysis during adrenergic or contractile stimulation.";
Physiol. Rep. 1:E00084-E00084(2013).
-!- FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in
adipocyte and non-adipocyte lipid droplets. 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:0000250|UniProtKB:Q96AD5}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate.
-!- 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 (By similarity).
Despite a colocalization in lipid droplets, it probably does not
interact with PLIN (By similarity). Interacts with PLIN5; prevents
interaction with ABHD5 (PubMed:23408028, PubMed:24303154).
Interacts with FAF2 (By similarity).
{ECO:0000250|UniProtKB:P0C548, ECO:0000269|PubMed:23408028,
ECO:0000269|PubMed:24303154}.
-!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Cell membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
-!- INDUCTION: Increased by rosiglitazone in subcutaneous and visceral
white adipose tissue. {ECO:0000269|PubMed:16906479}.
-!- PTM: May be phosphorylated. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-398 by PKA is increased during fasting
and moderate intensity exercise, and moderately increases
lipolytic activity. {ECO:0000250}.
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EMBL; AC109542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001101979.2; NM_001108509.2.
RefSeq; XP_003749062.1; XM_003749014.3.
RefSeq; XP_017459687.1; XM_017604198.1.
UniGene; Rn.19196; -.
ProteinModelPortal; P0C548; -.
SMR; P0C548; -.
BioGrid; 262869; 1.
STRING; 10116.ENSRNOP00000025826; -.
iPTMnet; P0C548; -.
PhosphoSitePlus; P0C548; -.
PaxDb; P0C548; -.
PRIDE; P0C548; -.
Ensembl; ENSRNOT00000025319; ENSRNOP00000025319; ENSRNOG00000018736.
Ensembl; ENSRNOT00000025826; ENSRNOP00000025826; ENSRNOG00000047551.
GeneID; 100911615; -.
GeneID; 361676; -.
KEGG; rno:100911615; -.
KEGG; rno:361676; -.
CTD; 57104; -.
RGD; 1309044; Pnpla2.
eggNOG; KOG3773; Eukaryota.
eggNOG; ENOG410XSQS; LUCA.
GeneTree; ENSGT00390000005295; -.
HOGENOM; HOG000007467; -.
HOVERGEN; HBG007046; -.
InParanoid; P0C548; -.
KO; K16816; -.
OMA; TGVCLGE; -.
OrthoDB; EOG091G05MG; -.
PhylomeDB; P0C548; -.
TreeFam; TF314272; -.
Reactome; R-RNO-1482883; Acyl chain remodeling of DAG and TAG.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
UniPathway; UPA00256; -.
PRO; PR:P0C548; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018736; -.
Genevisible; P0C548; RN.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISS:UniProtKB.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
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;
Cell membrane; Complete proteome; Glycoprotein; Hydrolase;
Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 478 Patatin-like phospholipase domain-
containing protein 2.
/FTId=PRO_0000292529.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 478 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 366 366 Phosphoserine; in vitro.
{ECO:0000250|UniProtKB:Q8BJ56}.
MOD_RES 388 388 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q8BJ56}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 460 460 Phosphoserine; in vitro.
{ECO:0000250|UniProtKB:Q8BJ56}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 478 AA; 52567 MW; E6B8294E47631410 CRC64;
MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGA
CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK TLPADCHTRA SGRLGISLTR
VSDGENVIIS HFSSKDELIQ ANVCSTFIPV YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRITNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ
GYRDGLRFLR RNGLLNQPNP LLALPPVVPQ EEDAEEAAVT EERTGGEDRI LEHLPARLNE
ALLEACVEPK DLMTTLSNML PVRLATAMMV PYTLPLESAV SFTIRLLEWL PDVPEDIRWM
KEQTGSICQY LVMRAKRKLG DHLPSRLSEQ VELRRAQSLP SVPLSCATYS EALPNWVRNN
LSLGDALAKW EECQRQLLLG LFCTNVAFPP DALRMRAPAS PTATDPATPQ DPSGLPPC


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