PA24C_HUMAN
ID PA24C_HUMAN Reviewed; 541 AA.
AC Q9UP65; B2RB71; B4DI40; O75457; Q6IBI8; Q9UG68;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytosolic phospholipase A2 gamma;
DE Short=cPLA2-gamma;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332};
DE AltName: Full=Cytosolic lysophospholipase;
DE EC=3.1.1.5 {ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189};
DE AltName: Full=Cytosolic lysophospholipid O-acyltransferase;
DE EC=2.3.1.- {ECO:0000269|PubMed:19501189};
DE AltName: Full=Phospholipase A2 group IVC;
DE Flags: Precursor;
GN Name=PLA2G4C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP ISOPRENYLATION AT CYS-538, AND MUTAGENESIS OF 538-CYS-CYS-539.
RC TISSUE=Skeletal muscle;
RX PubMed=9705332; DOI=10.1074/jbc.273.34.21926;
RA Underwood K.W., Song C., Kriz R.W., Chang X.J., Knopf J.L., Lin L.L.;
RT "A novel calcium-independent phospholipase A2, cPLA2-gamma, that is
RT prenylated and contains homology to cPLA2.";
RL J. Biol. Chem. 273:21926-21932(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MUTAGENESIS OF ARG-54; SER-82; ASP-385 AND ARG-402, AND
RP VARIANT PRO-203.
RX PubMed=10085124; DOI=10.1074/jbc.274.13.8823;
RA Pickard R.T., Strifler B.A., Kramer R.M., Sharp J.D.;
RT "Molecular cloning of two new human paralogs of 85-kDa cytosolic
RT phospholipase A2.";
RL J. Biol. Chem. 274:8823-8831(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-21; PRO-38; VAL-127;
RP PHE-142; VAL-143; GLY-148; LEU-151; PRO-203; SER-226; PRO-360 AND ASN-411.
RG NIEHS SNPs program;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP VAL-143 AND PRO-203.
RC TISSUE=Corpus callosum, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-203.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 420-476, AND VARIANT CYS-430.
RA Koyama K.S., Kimura T., Imai T.;
RT "SNP search of PLA2G4C gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-541 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10358058; DOI=10.1074/jbc.274.24.17063;
RA Song C., Chang X.J., Bean K.M., Proia M.S., Knopf J.L., Kriz R.W.;
RT "Molecular characterization of cytosolic phospholipase A2-beta.";
RL J. Biol. Chem. 274:17063-17067(1999).
RN [12]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP ISOPRENYLATION AT CYS-538, AND METHYLATION AT CYS-538.
RX PubMed=14529291; DOI=10.1021/bi034611q;
RA Jenkins C.M., Han X., Yang J., Mancuso D.J., Sims H.F., Muslin A.J.,
RA Gross R.W.;
RT "Purification of recombinant human cPLA2 gamma and identification of C-
RT terminal farnesylation, proteolytic processing, and carboxymethylation by
RT MALDI-TOF-TOF analysis.";
RL Biochemistry 42:11798-11807(2003).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-538.
RX PubMed=15944408; DOI=10.1093/jb/mvi067;
RA Yamashita A., Kamata R., Kawagishi N., Nakanishi H., Suzuki H., Sugiura T.,
RA Waku K.;
RT "Roles of C-terminal processing, and involvement in transacylation reaction
RT of human group IVC phospholipase A2 (cPLA2gamma).";
RL J. Biochem. 137:557-567(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-538.
RX PubMed=19501189; DOI=10.1016/j.bbalip.2009.05.008;
RA Yamashita A., Tanaka K., Kamata R., Kumazawa T., Suzuki N., Koga H.,
RA Waku K., Sugiura T.;
RT "Subcellular localization and lysophospholipase/transacylation activities
RT of human group IVC phospholipase A2 (cPLA2gamma).";
RL Biochim. Biophys. Acta 1791:1011-1022(2009).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION), AND
RP SUBUNIT (MICROBIAL INFECTION).
RX PubMed=23015700; DOI=10.1128/jvi.01785-12;
RA Xu S., Pei R., Guo M., Han Q., Lai J., Wang Y., Wu C., Zhou Y., Lu M.,
RA Chen X.;
RT "Cytosolic phospholipase A2 gamma is involved in hepatitis C virus
RT replication and assembly.";
RL J. Virol. 86:13025-13037(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, REGION, AND
RP MUTAGENESIS OF ARG-54; SER-82; ASP-385 AND ARG-402.
RX PubMed=28336330; DOI=10.1016/j.bbalip.2017.03.007;
RA Su X., Liu S., Zhang X., Lam S.M., Hu X., Zhou Y., Chen J., Wang Y., Wu C.,
RA Shui G., Lu M., Pei R., Chen X.;
RT "Requirement of cytosolic phospholipase A2 gamma in lipid droplet
RT formation.";
RL Biochim. Biophys. Acta 1862:692-705(2017).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), AND INDUCTION (MICROBIAL INFECTION).
RX PubMed=28639618; DOI=10.1038/ncomms15890;
RA Percher F., Curis C., Peres E., Artesi M., Rosewick N., Jeannin P.,
RA Gessain A., Gout O., Mahieux R., Ceccaldi P.E., Van den Broeke A.,
RA Duc Dodon M., Afonso P.V.;
RT "HTLV-1-induced leukotriene B4 secretion by T cells promotes T cell
RT recruitment and virus propagation.";
RL Nat. Commun. 8:15890-15890(2017).
CC -!- FUNCTION: Calcium-independent phospholipase, lysophospholipase and O-
CC acyltransferase involved in phospholipid remodeling with implications
CC in endoplasmic reticulum membrane homeostasis and lipid droplet
CC biogenesis (PubMed:19501189, PubMed:9705332, PubMed:10085124,
CC PubMed:10358058, PubMed:28336330). Preferentially hydrolyzes the ester
CC bond of the fatty acyl group attached at the sn-2 position of
CC phospholipids with choline and ethanolamine head groups, producing
CC lysophospholipids that are used in deacylation-reacylation cycles
CC (PubMed:19501189, PubMed:9705332, PubMed:10085124, PubMed:10358058,
CC PubMed:28336330). Transfers the sn-1 fatty acyl from one
CC lysophospholipid molecule to the sn-2 position of another
CC lysophospholipid to form diacyl, alkylacyl and alkenylacyl
CC glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl
CC ether bonds at sn-1 position of lysophospholipids (PubMed:19501189,
CC PubMed:15944408). Catalyzes sn-2 fatty acyl transfer from phospholipids
CC to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with
CC lower efficiency (PubMed:19501189, PubMed:15944408). In response to
CC dietary fatty acids, may play a role in the formation of nascent lipid
CC droplets from the endoplasmic reticulum likely by regulating the
CC phospholipid composition of these organelles (PubMed:28336330).
CC {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189,
CC ECO:0000269|PubMed:28336330, ECO:0000269|PubMed:9705332}.
CC -!- FUNCTION: (Microbial infection) May play a role in replication and
CC assembly of human hepatitis C virus (HCV) (PubMed:23015700,
CC PubMed:28336330). In response to HCV infection, promotes remodeling of
CC host endoplasmic reticulum membranes to form organelle-like structures
CC called membranous web, where HCV replication occur (PubMed:23015700).
CC Can further mediate translocation of replication complexes to lipid
CC droplets to enable virion assembly (PubMed:23015700, PubMed:28336330).
CC {ECO:0000269|PubMed:23015700, ECO:0000269|PubMed:28336330}.
CC -!- FUNCTION: (Microbial infection) May facilitate human T-lymphotropic
CC virus type 1 (HTLV-1) infection by promoting leukotriene B4 (LTB4)
CC biosynthesis. LTB4 acts as a chemoattractant for HTLV-1-infected CD4-
CC positive T cells and favors cell to cell viral transmission.
CC {ECO:0000269|PubMed:28639618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:10085124, ECO:0000305|PubMed:10358058,
CC ECO:0000305|PubMed:14529291, ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:10085124, ECO:0000305|PubMed:10358058,
CC ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-
CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:55430, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:9705332};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:9705332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:15944408,
CC ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:14529291, ECO:0000305|PubMed:15944408,
CC ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:15944408,
CC ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:14529291, ECO:0000305|PubMed:15944408,
CC ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC Evidence={ECO:0000305|PubMed:15944408, ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-
CC sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40899, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73005;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-
CC sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-
CC phosphocholine + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63764, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63765;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphoethanolamine + sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:63768, ChEBI:CHEBI:73004,
CC ChEBI:CHEBI:73005, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63769;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-O-hexadecyl-sn-
CC glycero-3-phosphocholine = 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:63656,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:64496, ChEBI:CHEBI:72744,
CC ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63657;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-O-(1Z-alkenyl)-
CC sn-glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-hexadecanoyl-
CC sn-glycero-3-phosphoethanolamine + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:63772, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77303;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63773;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + 1-O-
CC hexadecyl-sn-glycero-3-phosphocholine = 1-O-hexadecyl-2-hexadecanoyl-
CC sn-glycero-3-phosphocholine + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63760, ChEBI:CHEBI:64496, ChEBI:CHEBI:72744,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63761;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine =
CC 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphocholine + 1-octadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63788, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003,
CC ChEBI:CHEBI:75036, ChEBI:CHEBI:78268;
CC Evidence={ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63789;
CC Evidence={ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine =
CC 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphocholine + 1-octadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63776, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496,
CC ChEBI:CHEBI:75036, ChEBI:CHEBI:78268;
CC Evidence={ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63777;
CC Evidence={ECO:0000305|PubMed:15944408, ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-O-(1Z-alkenyl)-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63784, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:149549;
CC Evidence={ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63785;
CC Evidence={ECO:0000305|PubMed:15944408, ECO:0000305|PubMed:19501189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine
CC = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-O-(1Z)-alkenyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63780, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77295;
CC Evidence={ECO:0000269|PubMed:15944408};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63781;
CC Evidence={ECO:0000305|PubMed:15944408};
CC -!- ACTIVITY REGULATION: Not regulated by calcium, coenzyme A or ATP
CC (PubMed:9705332, PubMed:10085124, PubMed:15944408). Lysophospholipase
CC activity is inhibited by palmitoyl-CoA (PubMed:14529291).
CC Lysophospholipase and O-acyltransferase activities are inhibited by
CC methylarachidonoylfluorophosphonate (PubMed:19501189).
CC Lysophospholipase activity is inhibited by phosphatidate or
CC lysophosphatidate (PubMed:19501189). O-acyltransferase activity is up-
CC regulated at low concentration (10-20 uM) of phosphatidate or
CC lysophosphatidate, but inhibited at higher concentrations
CC (PubMed:19501189). {ECO:0000269|PubMed:10085124,
CC ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:19501189,
CC ECO:0000269|PubMed:9705332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for 1-O-hexadecyl-sn-glycero-3-phosphocholine (O-
CC acyltransferase activity) {ECO:0000269|PubMed:15944408};
CC Vmax=218 pmol/min/mg enzyme {ECO:0000269|PubMed:10085124};
CC pH dependence:
CC Optimum pH is 6.5 for lysophospholipase activity, and 8-9 for O-
CC acyltransferase activity. {ECO:0000269|PubMed:19501189};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for lysophospholipase
CC activity, and 50 degrees Celsius for O-acyltransferase activity.
CC Lysophospholipase activity is present even at 0 degrees Celsius and
CC its rate increases with temperature up to 40 degrees Celsius. O-
CC acyltransferase activity is low below 25 degrees Celsius, but
CC increases sharply between 30 and 40 degrees Celsius and peaked near
CC 50 degrees Celsius. {ECO:0000269|PubMed:19501189};
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV non-structural
CC protein 4B/NS4B; this interaction likely initiates the recruitment of
CC replication complexes to lipid droplets. {ECO:0000269|PubMed:23015700}.
CC -!- INTERACTION:
CC Q9UP65; P42858: HTT; NbExp=12; IntAct=EBI-25848809, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10085124,
CC ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332}; Lipid-anchor
CC {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291,
CC ECO:0000269|PubMed:9705332}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189,
CC ECO:0000269|PubMed:28336330}; Lipid-anchor. Mitochondrion membrane
CC {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189}; Lipid-
CC anchor. Lipid droplet {ECO:0000269|PubMed:28336330}. Note=Translocates
CC from endoplasmic reticulum to lipid droplets in response to oleate.
CC {ECO:0000269|PubMed:28336330}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UP65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UP65-2; Sequence=VSP_045850;
CC Name=3;
CC IsoId=Q9UP65-3; Sequence=VSP_045849;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.
CC {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:9705332}.
CC -!- INDUCTION: (Microbial infection) Up-regulated by HCV.
CC {ECO:0000269|PubMed:23015700}.
CC -!- INDUCTION: (Microbial infection) Transcriptionally up-regulated by
CC HTLV-1 Tax. {ECO:0000269|PubMed:28639618}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pla2g4c/";
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DR EMBL; AF058921; AAC32823.1; -; mRNA.
DR EMBL; AF065214; AAC78835.1; -; mRNA.
DR EMBL; AY485310; AAR25453.1; -; Genomic_DNA.
DR EMBL; AK295400; BAG58352.1; -; mRNA.
DR EMBL; AK314524; BAG37118.1; -; mRNA.
DR EMBL; CR456816; CAG33097.1; -; mRNA.
DR EMBL; AC010458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52314.1; -; Genomic_DNA.
DR EMBL; BC063416; AAH63416.1; -; mRNA.
DR EMBL; AB105807; BAC87745.1; -; Genomic_DNA.
DR EMBL; AL050193; CAB43312.3; -; mRNA.
DR CCDS; CCDS12710.1; -. [Q9UP65-1]
DR CCDS; CCDS54286.1; -. [Q9UP65-2]
DR CCDS; CCDS59403.1; -. [Q9UP65-3]
DR PIR; T13162; T13162.
DR RefSeq; NP_001152794.1; NM_001159322.1. [Q9UP65-3]
DR RefSeq; NP_001152795.1; NM_001159323.1. [Q9UP65-2]
DR RefSeq; NP_003697.2; NM_003706.2. [Q9UP65-1]
DR AlphaFoldDB; Q9UP65; -.
DR SMR; Q9UP65; -.
DR BioGRID; 114165; 12.
DR IntAct; Q9UP65; 1.
DR STRING; 9606.ENSP00000472546; -.
DR BindingDB; Q9UP65; -.
DR ChEMBL; CHEMBL4834; -.
DR SwissLipids; SLP:000000888; -.
DR SwissLipids; SLP:000001081; -. [Q9UP65-1]
DR iPTMnet; Q9UP65; -.
DR PhosphoSitePlus; Q9UP65; -.
DR SwissPalm; Q9UP65; -.
DR BioMuta; PLA2G4C; -.
DR DMDM; 322510066; -.
DR jPOST; Q9UP65; -.
DR MassIVE; Q9UP65; -.
DR PaxDb; Q9UP65; -.
DR PeptideAtlas; Q9UP65; -.
DR PRIDE; Q9UP65; -.
DR ProteomicsDB; 85355; -. [Q9UP65-1]
DR Antibodypedia; 31649; 118 antibodies from 28 providers.
DR DNASU; 8605; -.
DR Ensembl; ENST00000354276.7; ENSP00000346228.2; ENSG00000105499.14. [Q9UP65-2]
DR Ensembl; ENST00000599111.5; ENSP00000472546.1; ENSG00000105499.14. [Q9UP65-3]
DR Ensembl; ENST00000599921.6; ENSP00000469473.1; ENSG00000105499.14. [Q9UP65-1]
DR GeneID; 8605; -.
DR KEGG; hsa:8605; -.
DR MANE-Select; ENST00000599921.6; ENSP00000469473.1; NM_003706.3; NP_003697.2.
DR UCSC; uc002phx.4; human. [Q9UP65-1]
DR CTD; 8605; -.
DR DisGeNET; 8605; -.
DR GeneCards; PLA2G4C; -.
DR HGNC; HGNC:9037; PLA2G4C.
DR HPA; ENSG00000105499; Tissue enhanced (retina, skeletal muscle).
DR MIM; 603602; gene.
DR neXtProt; NX_Q9UP65; -.
DR OpenTargets; ENSG00000105499; -.
DR PharmGKB; PA33365; -.
DR VEuPathDB; HostDB:ENSG00000105499; -.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_2_0_1; -.
DR InParanoid; Q9UP65; -.
DR OMA; TTRNFLY; -.
DR OrthoDB; 302848at2759; -.
DR PhylomeDB; Q9UP65; -.
DR TreeFam; TF325228; -.
DR PathwayCommons; Q9UP65; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR Reactome; R-HSA-1483152; Hydrolysis of LPE.
DR SignaLink; Q9UP65; -.
DR BioGRID-ORCS; 8605; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; PLA2G4C; human.
DR GeneWiki; PLA2G4C; -.
DR GenomeRNAi; 8605; -.
DR Pharos; Q9UP65; Tchem.
DR PRO; PR:Q9UP65; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UP65; protein.
DR Bgee; ENSG00000105499; Expressed in gluteal muscle and 176 other tissues.
DR ExpressionAtlas; Q9UP65; baseline and differential.
DR Genevisible; Q9UP65; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; TAS:Reactome.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; NAS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; NAS:UniProtKB.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0007567; P:parturition; NAS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:UniProtKB.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Host-virus interaction; Hydrolase; Lipid droplet; Lipid metabolism;
KW Lipoprotein; Membrane; Methylation; Mitochondrion; Phospholipid metabolism;
KW Phosphoprotein; Prenylation; Reference proteome; Transferase.
FT CHAIN 1..538
FT /note="Cytosolic phospholipase A2 gamma"
FT /id="PRO_0000022995"
FT PROPEP 539..541
FT /note="Removed in mature form"
FT /id="PRO_0000022996"
FT DOMAIN 1..541
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 260..292
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000269|PubMed:28336330"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10085124"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10085124"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 538
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:14529291,
FT ECO:0000305|PubMed:9705332"
FT LIPID 538
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:14529291,
FT ECO:0000305|PubMed:9705332"
FT VAR_SEQ 1..13
FT /note="MGSSEVSIIPGLQ -> MRTRPRPRLRRTENFLTAVHHGK (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045849"
FT VAR_SEQ 528..541
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045850"
FT VARIANT 21
FT /note="E -> K (in dbSNP:rs11564522)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018761"
FT VARIANT 38
FT /note="A -> P (in dbSNP:rs2307279)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018420"
FT VARIANT 127
FT /note="A -> V (in dbSNP:rs11564532)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018762"
FT VARIANT 142
FT /note="V -> F (in dbSNP:rs11564534)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018763"
FT VARIANT 143
FT /note="I -> V (in dbSNP:rs2303744)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_018421"
FT VARIANT 148
FT /note="R -> G (in dbSNP:rs2307282)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018764"
FT VARIANT 151
FT /note="P -> L (in dbSNP:rs11564538)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018765"
FT VARIANT 203
FT /note="S -> P (in dbSNP:rs156631)"
FT /evidence="ECO:0000269|PubMed:10085124,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_018422"
FT VARIANT 226
FT /note="T -> S (in dbSNP:rs11564541)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018766"
FT VARIANT 360
FT /note="T -> P (in dbSNP:rs11564620)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018767"
FT VARIANT 411
FT /note="D -> N (in dbSNP:rs11564638)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018768"
FT VARIANT 430
FT /note="R -> C (in dbSNP:rs191276960)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_018423"
FT MUTAGEN 54
FT /note="R->A: Abolishes enzyme activity. Reduces lipid
FT droplet formation; when associated with A-82; A-385 and A-
FT 402."
FT /evidence="ECO:0000269|PubMed:10085124,
FT ECO:0000269|PubMed:28336330"
FT MUTAGEN 82
FT /note="S->A: Abolishes enzyme activity. Reduces lipid
FT droplet formation; when associated with A-54; A-385 and A-
FT 402."
FT /evidence="ECO:0000269|PubMed:10085124,
FT ECO:0000269|PubMed:28336330"
FT MUTAGEN 385
FT /note="D->A: Abolishes enzyme activity. Reduces lipid
FT droplet formation; when associated with A-54; A-82 and A-
FT 402."
FT /evidence="ECO:0000269|PubMed:10085124,
FT ECO:0000269|PubMed:28336330"
FT MUTAGEN 402
FT /note="R->A: Abolishes enzyme activity. Reduces lipid
FT droplet formation; when associated with A-54; A-82 and A-
FT 385."
FT /evidence="ECO:0000269|PubMed:10085124,
FT ECO:0000269|PubMed:28336330"
FT MUTAGEN 538..539
FT /note="CC->SS: Loss of prenylation."
FT /evidence="ECO:0000269|PubMed:9705332"
FT MUTAGEN 538
FT /note="C->S: Has no effect on membrane localization.
FT Decreases the affinity for 1-O-hexadecyl-sn-glycero-3-
FT phosphocholine acyl acceptor in transacylation reaction."
FT /evidence="ECO:0000269|PubMed:15944408,
FT ECO:0000269|PubMed:19501189"
FT CONFLICT 24
FT /note="R -> G (in Ref. 4; BAG58352)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="M -> I (in Ref. 1; AAC32823)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="E -> G (in Ref. 5; CAG33097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60939 MW; A114B2A614EA4632 CRC64;
MGSSEVSIIP GLQKEEKAAV ERRRLHVLKA LKKLRIEADE APVVAVLGSG GGLRAHIACL
GVLSEMKEQG LLDAVTYLAG VSGSTWAISS LYTNDGDMEA LEADLKHRFT RQEWDLAKSL
QKTIQAARSE NYSLTDFWAY MVISKQTREL PESHLSNMKK PVEEGTLPYP IFAAIDNDLQ
PSWQEARAPE TWFEFTPHHA GFSALGAFVS ITHFGSKFKK GRLVRTHPER DLTFLRGLWG
SALGNTEVIR EYIFDQLRNL TLKGLWRRAV ANAKSIGHLI FARLLRLQES SQGEHPPPED
EGGEPEHTWL TEMLENWTRT SLEKQEQPHE DPERKGSLSN LMDFVKKTGI CASKWEWGTT
HNFLYKHGGI RDKIMSSRKH LHLVDAGLAI NTPFPLVLPP TREVHLILSF DFSAGDPFET
IRATTDYCRR HKIPFPQVEE AELDLWSKAP ASCYILKGET GPVVMHFPLF NIDACGGDIE
AWSDTYDTFK LADTYTLDVV VLLLALAKKN VRENKKKILR ELMNVAGLYY PKDSARSCCL
A
