PLA2G4C
entrez
8605
canonical
uniprot
Q9UP65
canonical
ensembl
ENSG00000105499
resolver
ensp
ENSP00000346228
resolver
ensp
ENSP00000469473
resolver
ensp
ENSP00000472546
resolver
ensp
ENSP00000557148
resolver
ensp
ENSP00000690060
resolver
ensp
ENSP00000749245
resolver
genesymbol
PLA2G4C
resolver
hgnc
HGNC:9037
resolver
uniprot
B2RB71
resolver
uniprot
B4DI40
resolver
uniprot
O75457
resolver
uniprot
Q6IBI8
resolver
uniprot
Q9UG68
resolver
uniprot_entry
PA24C_HUMAN
resolver
uniprot_sec
B2RB71
resolver
uniprot_sec
B4DI40
resolver
uniprot_sec
O75457
resolver
uniprot_sec
Q6IBI8
resolver
uniprot_sec
Q9UG68
resolver
activity_regulation
ACTIVITY REGULATION: Not regulated by calcium, coenzyme A or ATP (PubMed:10085124, PubMed:15944408, PubMed:9705332). Lysophospholipase activity is inhibited by palmitoyl-CoA (PubMed:14529291). Lysophospholipase and O-acyltransferase activities are inhibited by methylarachidonoylfluorophosphonate (PubMed:19501189). Lysophospholipase activity is inhibited by phosphatidate or lysophosphatidate (PubMed:19501189). O-acyltransferase activity is up-regulated at low concentration (10-20 uM) of phosphatidate or lysophosphatidate, but inhibited at higher concentrations (PubMed:19501189). {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:19501189, ECO:0000269|PubMed:9705332}.
uniprot
proteins
amino_acid_sequence
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPEDEGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTTHNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIEAWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCLA
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
FUNCTION: Calcium-independent phospholipase, lysophospholipase and O-acyltransferase involved in phospholipid remodeling with implications in endoplasmic reticulum membrane homeostasis and lipid droplet biogenesis (PubMed:10085124, PubMed:10358058, PubMed:19501189, PubMed:28336330, PubMed:9705332). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids with choline and ethanolamine head groups, producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:10085124, PubMed:10358058, PubMed:19501189, PubMed:28336330, PubMed:9705332). Transfers the sn-1 fatty acyl from one lysophospholipid molecule to the sn-2 position of another lysophospholipid to form diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl ether bonds at sn-1 position of lysophospholipids (PubMed:15944408, PubMed:19501189). Catalyzes sn-2 fatty acyl transfer from phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with lower efficiency (PubMed:15944408, PubMed:19501189). In response to dietary fatty acids, may play a role in the formation of nascent lipid droplets from the endoplasmic reticulum likely by regulating the phospholipid composition of these organelles (PubMed:28336330). {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189, ECO:0000269|PubMed:28336330, ECO:0000269|PubMed:9705332}.; FUNCTION: (Microbial infection) May play a role in replication and assembly of human hepatitis C virus (HCV) (PubMed:23015700, PubMed:28336330). In response to HCV infection, promotes remodeling of host endoplasmic reticulum membranes to form organelle-like structures called membranous web, where HCV replication occur (PubMed:23015700). Can further mediate translocation of replication complexes to lipid droplets to enable virion assembly (PubMed:23015700, PubMed:28336330). {ECO:0000269|PubMed:23015700, ECO:0000269|PubMed:28336330}.; FUNCTION: (Microbial infection) May facilitate human T-lymphotropic virus type 1 (HTLV-1) infection by promoting leukotriene B4 (LTB4) biosynthesis. LTB4 acts as a chemoattractant for HTLV-1-infected CD4-positive T cells and favors cell to cell viral transmission. {ECO:0000269|PubMed:28639618}.
uniprot
proteins
mass_dalton
60939
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="R->A: Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-82; A-385 and A-402."; /evidence="ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:28336330"; MUTAGEN 82; /note="S->A: Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-385 and A-402."; /evidence="ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:28336330"; MUTAGEN 385; /note="D->A: Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-82 and A-402."; /evidence="ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:28336330"; MUTAGEN 402; /note="R->A: Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-82 and A-385."; /evidence="ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:28336330"; MUTAGEN 538..539; /note="CC->SS: Loss of prenylation."; /evidence="ECO:0000269|PubMed:9705332"; MUTAGEN 538; /note="C->S: Has no effect on membrane localization. Decreases the affinity for 1-O-hexadecyl-sn-glycero-3-phosphocholine acyl acceptor in transacylation reaction."; /evidence="ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189
uniprot
proteins
pubmed
10085124
uniprot
proteins
pubmed
10358058
uniprot
proteins
pubmed
14529291
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15944408
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
19501189
uniprot
proteins
pubmed
23015700
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28336330
uniprot
proteins
pubmed
28639618
uniprot
proteins
pubmed
9705332
uniprot
proteins
sequence_length
541
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332}; Lipid-anchor {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189, ECO:0000269|PubMed:28336330}; Lipid-anchor. Mitochondrion membrane {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189}; Lipid-anchor. Lipid droplet {ECO:0000269|PubMed:28336330}. Note=Translocates from endoplasmic reticulum to lipid droplets in response to oleate. {ECO:0000269|PubMed:28336330}.
uniprot
proteins