CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
224RNLYRLSKALFPPEPubiquitination[1]
295DQLQPYRKDRILEHLubiquitination[1]
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. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002641; Patatin/PLipase_A2-rel. 
Pfam
 PF01734; Patatin 
SMART
  
PROSITE
  
PRINTS