CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021945
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calcium-independent phospholipase A2-gamma 
Protein Synonyms/Alias
 Intracellular membrane-associated calcium-independent phospholipase A2 gamma; iPLA2-gamma; PNPLA-gamma; Patatin-like phospholipase domain-containing protein 8; iPLA2-2 
Gene Name
 PNPLA8 
Gene Synonyms/Alias
 IPLA22; IPLA2G; BM-043 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
438IGYVDPVKGRGIRILubiquitination[1]
726LDESRNEKLDQLQLEubiquitination[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids. 
Sequence Annotation
 DOMAIN 445 640 Patatin.
 MOTIF 481 485 GXSXG.
 CARBOHYD 4 4 N-linked (GlcNAc...) (Potential).
 CARBOHYD 361 361 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 782 AA 
Protein Sequence
MSINLTVDIY IYLLSNARSV CGKQRSKQLY FLFSPKHYWR ISHISLQRGF HTNIIRCKWT 60
KSEAHSCSKH CYSPSNHGLH IGILKLSTSA PKGLTKVNIC MSRIKSTLNS VSKAVFGNQN 120
EMISRLAQFK PSSQILRKVS DSGWLKQKNI KQAIKSLKKY SDKSAEKSPF PEEKSHIIDK 180
EEDIGKRSLF HYTSSITTKF GDSFYFLSNH INSYFKRKEK MSQQKENEHF RDKSELEDKK 240
VEEGKLRSPD PGILAYKPGS ESVHTVDKPT SPSAIPDVLQ VSTKQSIANF LSRPTEGVQA 300
LVGGYIGGLV PKLKYDSKSQ SEEQEEPAKT DQAVSKDRNA EEKKRLSLQR EKIIARVSID 360
NRTRALVQAL RRTTDPKLCI TRVEELTFHL LEFPEGKGVA VKERIIPYLL RLRQIKDETL 420
QAAVREILAL IGYVDPVKGR GIRILSIDGG GTRGVVALQT LRKLVELTQK PVHQLFDYIC 480
GVSTGAILAF MLGLFHMPLD ECEELYRKLG SDVFSQNVIV GTVKMSWSHA FYDSQTWENI 540
LKDRMGSALM IETARNPTCP KVAAVSTIVN RGITPKAFVF RNYGHFPGIN SHYLGGCQYK 600
MWQAIRASSA APGYFAEYAL GNDLHQDGGL LLNNPSALAM HECKCLWPDV PLECIVSLGT 660
GRYESDVRNT VTYTSLKTKL SNVINSATDT EEVHIMLDGL LPPDTYFRFN PVMCENIPLD 720
ESRNEKLDQL QLEGLKYIER NEQKMKKVAK ILSQEKTTLQ KINDWIKLKT DMYEGLPFFS 780
KL 782 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
 GO:0004622; F:lysophospholipase activity; IEA:EC.
 GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
 GO:0050482; P:arachidonic acid secretion; IDA:UniProtKB.
 GO:0008219; P:cell death; IDA:UniProtKB.
 GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
 GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
 GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
 GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
 GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
 GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
 GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002641; Patatin/PLipase_A2-rel. 
Pfam
 PF01734; Patatin 
SMART
  
PROSITE
  
PRINTS