ID A5JT15_PIG Unreviewed; 486 AA.
AC A5JT15;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Adipose triglyceride lipase {ECO:0000313|EMBL:ABS58651.1};
DE SubName: Full=Patatin-like phospholipase domain-containing 2 {ECO:0000313|EMBL:ABQ50607.1, ECO:0000313|EMBL:ABV45507.1};
DE SubName: Full=Patatin-like phospholipase domain-containing protein 2 isoform X1 {ECO:0000313|EMBL:HDA48348.1};
DE SubName: Full=Patatin-like phospholipase domain-containing protein 2 isoform X3 {ECO:0000313|EMBL:HDA66573.1};
GN Name=PNPLA2 {ECO:0000313|EMBL:ABQ50607.1,
GN ECO:0000313|Ensembl:ENSSSCP00000013651.3,
GN ECO:0000313|VGNC:VGNC:91607};
GN Synonyms=ATGL {ECO:0000313|EMBL:ABS58651.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ABQ50607.1};
RN [1] {ECO:0000313|EMBL:ABQ50607.1}
RP NUCLEOTIDE SEQUENCE.
RA Dai L.H., Chen J.F., Xiong Y.Z., Deng C.Y., Zuo B., Xu D.Q., Lei M.G.,
RA Zheng R., Li F.E., Jiang S.W.;
RT "Cloning, characterization and expression of porcine adiposome triglyceride
RT lipase (ATGL) gene.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV45507.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Subcutaneous adipose {ECO:0000313|EMBL:ABV45507.1};
RA Yang Y., Zhao C.-J., Wu C.-X., Rui X., Ma C.-W.;
RT "cDNA cloning and expression profile of PNPLA2 from Chinese mini-pig.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABS58651.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18407985;
RA Shan T., Wang Y., Wu T., Guo J., Liu J., Feng J., Xu Z.;
RT "Porcine adipose triglyceride lipase complementary deoxyribonucleic acid
RT clone, expression pattern, and regulation by resveratrol.";
RL J. Anim. Sci. 86:1781-1788(2008).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000013651.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013651.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HDA48348.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [6] {ECO:0000313|Ensembl:ENSSSCP00000013651.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; EF567019; ABQ50607.1; -; Genomic_DNA.
DR EMBL; EF583921; ABS58651.1; -; mRNA.
DR EMBL; EU009401; ABV45507.1; -; mRNA.
DR EMBL; DQIR01092872; HDA48348.1; -; Transcribed_RNA.
DR EMBL; DQIR01111097; HDA66573.1; -; Transcribed_RNA.
DR EMBL; DQIR01126085; HDA81561.1; -; Transcribed_RNA.
DR EMBL; DQIR01126086; HDA81562.1; -; Transcribed_RNA.
DR STRING; 9823.ENSSSCP00000013651; -.
DR PaxDb; 9823-ENSSSCP00000013651; -.
DR Ensembl; ENSSSCT00000014036.5; ENSSSCP00000013651.3; ENSSSCG00000012841.5.
DR VGNC; VGNC:91607; PNPLA2.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000160155; -.
DR OMA; TKWEEYQ; -.
DR TreeFam; TF314272; -.
DR Reactome; R-SSC-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000012841; Expressed in subcutaneous adipose tissue and 43 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0051265; F:diolein transacylation activity; IEA:Ensembl.
DR GO; GO:0051264; F:mono-olein transacylation activity; IEA:Ensembl.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IEA:Ensembl.
DR GO; GO:1905691; P:lipid droplet disassembly; IEA:Ensembl.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR CDD; cd07220; Pat_PNPLA2; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR033903; PNPLA2.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2 IPLA2 -RELATED; 1.
DR PANTHER; PTHR12406:SF29; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 10..179
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 53166 MW; 7D865864CA9F69BA CRC64;
MFPKETTWNI SFAGCGFLGV YHVGVASCLR EHAPFLVANA KHIYGASAGA LVATALVTGV
CLGDTGASII EVSKEARKRF LGPLHPSFNL VKTIRGCLVK ILPADSHERA SGRLGISLTR
VSDGENVIIT RFAAREELIQ ANVCSTFIPV YCGLIPPALQ GERYVDGGIS DNLPLYELKS
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFSLRNLY RLSKALFPPE PLVLREMCKQ
GYRDGLRFLR RNGLLNRPNP LLALPPACPR APEEEDAPKA EVAEERAGAK EPLQLPTSDS
ILEHLPSRLN DALLEACMEP TDLLSTLSNL LPVRLATAMM VPYTLPLESA VSFTVRLLEW
LPDVPEDIRW IKEQTGSICQ YLVMRAKRKL GRHLPSRLTE QVELRRSQSL PSVPLSCAAY
GGVLPSWMRN SLSLGDVLAK WEERQRQLLL GLFCTNTAFP PDALRMLAPA GPAPAPSQHP
PGSPPC
//
