Tag | Content |
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CPLM ID | CPLM-016484 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Patatin-like phospholipase domain-containing protein 2 |
Protein Synonyms/Alias | Adipose triglyceride lipase; Desnutrin |
Gene Name | Pnpla2 |
Gene Synonyms/Alias | Atgl |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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224 | RNLYRLSKALFPPEP | ubiquitination | [1] | 295 | DQLQPYRKDRILEHL | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 10 179 Patatin. MOTIF 45 49 GXSXG. ACT_SITE 47 47 MOD_RES 374 374 Phosphoserine; in vitro. MOD_RES 396 396 Phosphoserine; by PKA. MOD_RES 406 406 Phosphoserine; by PKA. MOD_RES 430 430 Phosphoserine; in vitro. MOD_RES 468 468 Phosphoserine; in vitro. CARBOHYD 39 39 N-linked (GlcNAc...) (Potential). |
Keyword | Alternative splicing; Cell membrane; Complete proteome; Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 486 AA |
Protein Sequence | MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGA 60 CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK TLPADCHERA NGRLGISLTR 120 VSDGENVIIS HFSSKDELIQ ANVCSTFIPV YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN 180 TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ 240 GYRDGLRFLR RNGLLNQPNP LLALPPVVPQ EEDAEEAAVV EERAGEEDQL QPYRKDRILE 300 HLPARLNEAL LEACVEPKDL MTTLSNMLPV RLATAMMVPY TLPLESAVSF TIRLLEWLPD 360 VPEDIRWMKE QTGSICQYLV MRAKRKLGDH LPSRLSEQVE LRRAQSLPSV PLSCATYSEA 420 LPNWVRNNLS LGDALAKWEE CQRQLLLGLF CTNVAFPPDA LRMRAPASPT AADPATPQDP 480 PGLPPC 486 |
Gene Ontology | GO:0005829; C:cytosol; IDA:MGI. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC. GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB. GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB. GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB. GO:0019433; P:triglyceride catabolic process; IMP:MGI. |
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