Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00202
Entry Name
UniProt Accession
Theoretical PI
6.46
Molecular Weight
60938.66
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Cytosolic phospholipase A2 gamma
Protein Synonyms/Alias
cPLA2-gamma; 3.1.1.4; Phospholipase A2 group IVC;
Gene Name
PLA2G4C
Gene Synonyms/Alias
Created Date
10-MAY-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
538
Canonical
PKDSARSCCLA****
[1]
S-Palmitoylation
538
Canonical
PKDSARSCCLA****
[2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Tucker DE, Stewart A, Nallan L, Bendale P, Ghomashchi F, Gelb MH, Leslie CC.Group IVC cytosolic phospholipase A2gamma is farnesylated and palmitoylated inmammalian cells. J Lipid Res. 2005 Oct;46(10):2122-33. Epub 2005 Aug 1. PubMedPMID: 16061942; PubMed Central PMCID: PMC2405939.[PMID:16061942]
[2] Jenkins CM, Han X, Yang J, Mancuso DJ, Sims HF, Muslin AJ, Gross RW.Purification of recombinant human cPLA2 gamma and identification of C-terminalfarnesylation, proteolytic processing, and carboxymethylation by MALDI-TOF-TOFanalysis. Biochemistry. 2003 Oct 14;42(40):11798-807.[PMID:14529291]
Functional Description
Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid.
Sequence Annotation
Domain: 1 541 PLA2c.
Active site: 82 82 Nucleophile.
Active site: 385 385 Proton acceptor.
Modified residue: 538 538 Cysteine methyl ester.
Protein Length
541 AA.
Protein Sequence
(Canonical)
MGSSEVSIIP GLQKEEKAAV ERRRLHVLKA LKKLRIEADE APVVAVLGSG GGLRAHIACL  60
GVLSEMKEQG LLDAVTYLAG VSGSTWAISS LYTNDGDMEA LEADLKHRFT RQEWDLAKSL  120
QKTIQAARSE NYSLTDFWAY MVISKQTREL PESHLSNMKK PVEEGTLPYP IFAAIDNDLQ  180
PSWQEARAPE TWFEFTPHHA GFSALGAFVS ITHFGSKFKK GRLVRTHPER DLTFLRGLWG  240
SALGNTEVIR EYIFDQLRNL TLKGLWRRAV ANAKSIGHLI FARLLRLQES SQGEHPPPED  300
EGGEPEHTWL TEMLENWTRT SLEKQEQPHE DPERKGSLSN LMDFVKKTGI CASKWEWGTT  360
HNFLYKHGGI RDKIMSSRKH LHLVDAGLAI NTPFPLVLPP TREVHLILSF DFSAGDPFET  420
IRATTDYCRR HKIPFPQVEE AELDLWSKAP ASCYILKGET GPVVMHFPLF NIDACGGDIE  480
AWSDTYDTFK LADTYTLDVV VLLLALAKKN VRENKKKILR ELMNVAGLYY PKDSARSCCL  540
A                                                                  541
MGSSEVSIIP GLQKEEKAAV ERRRLHVLKA LKKLRIEADE APVVAVLGSG GGLRAHIACL  60
GVLSEMKEQG LLDAVTYLAG VSGSTWAISS LYTNDGDMEA LEADLKHRFT RQEWDLAKSL  120
QKTIQAARSE NYSLTDFWAY MVISKQTREL PESHLSNMKK PVEEGTLPYP IFAAIDNDLQ  180
PSWQEARAPE TWFEFTPHHA GFSALGAFVS ITHFGSKFKK GRLVRTHPER DLTFLRGLWG  240
SALGNTEVIR EYIFDQLRNL TLKGLWRRAV ANAKSIGHLI FARLLRLQES SQGEHPPPED  300
EGGEPEHTWL TEMLENWTRT SLEKQEQPHE DPERKGSLSN LMDFVKKTGI CASKWEWGTT  360
HNFLYKHGGI RDKIMSSRKH LHLVDAGLAI NTPFPLVLPP TREVHLILSF DFSAGDPFET  420
IRATTDYCRR HKIPFPQVEE AELDLWSKAP ASCYILKGET GPVVMHFPLF NIDACGGDIE  480
AWSDTYDTFK LADTYTLDVV VLLLALAKKN VRENKKKILR ELMNVAGLYY PKDSARSCCL  540
A                                                                  541
FASTA
(Canonical)
>LipidDB-9606-00202|Q9UP65
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
Gene Ontology
GO:0005938; C:cell cortex; IEA:Ensembl
GO:0005829; C:cytosol; TAS:UniProtKB
GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome
GO:0016020; C:membrane; TAS:UniProtKB
GO:0005635; C:nuclear envelope; IEA:Ensembl
GO:0005654; C:nucleoplasm; IEA:Ensembl
GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB
GO:0005543; F:phospholipid binding; NAS:UniProtKB
GO:0019369; P:arachidonic acid metabolic process; NAS:UniProtKB
GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome
GO:0046475; P:glycerophospholipid catabolic process; IDA:UniProtKB
GO:0006954; P:inflammatory response; NAS:UniProtKB
GO:0035556; P:intracellular signal transduction; NAS:UniProtKB
GO:0007567; P:parturition; NAS:UniProtKB
GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome
GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome
GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome
GO:0006644; P:phospholipid metabolic process; TAS:UniProtKB
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR016035; Acyl_Trfase/lysoPLipase
InterPro; IPR002642; LysoPLipase_cat_dom
Pfam
Pfam; PF01735; PLA2_B;
SMART
SMART; SM00022; PLAc;
PROSITE
PROSITE; PS51210; PLA2C;
PRINTS