PA24C_MOUSE
ID PA24C_MOUSE Reviewed; 597 AA.
AC Q64GA5; Q08EC7; Q3UWS1; Q7TN01;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cytosolic phospholipase A2 gamma {ECO:0000303|PubMed:15950603};
DE Short=cPLA2-gamma {ECO:0000303|PubMed:15950603};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU00555};
DE AltName: Full=Cytosolic lysophospholipase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:Q9UP65};
DE AltName: Full=Cytosolic lysophospholipid O-acyltransferase;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9UP65};
DE AltName: Full=Phospholipase A2 group IVC {ECO:0000312|MGI:MGI:1196403};
GN Name=Pla2g4c {ECO:0000312|MGI:MGI:1196403};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAU14177.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAU14177.1};
RX PubMed=15950603; DOI=10.1016/j.ydbio.2005.03.018;
RA Vitale A., Perlin J., Leonelli L., Herr J., Wright P., Digilio L.,
RA Coonrod S.;
RT "Mouse cPLA2gamma, a novel oocyte and early embryo-abundant phospholipase
RT A2 gamma-like protein, is targeted to the nuclear envelope during germinal
RT vesicle breakdown.";
RL Dev. Biol. 282:374-384(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE22819.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAE26375.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI38549.1};
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-independent phospholipase, lysophospholipase and O-
CC acyltransferase involved in phospholipid remodeling. Preferentially
CC hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC position of phospholipids with choline and ethanolamine head groups,
CC producing lysophospholipids that are used in deacylation-reacylation
CC cycles. Transfers the sn-1 fatty acyl from one lysophospholipid
CC molecule to the sn-2 position of another lysophospholipid to form
CC diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester
CC bonds but not alkyl or alkenyl ether bonds at the sn-1 position of
CC lysophospholipids. Catalyzes sn-2 fatty acyl transfer from
CC phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl
CC lysophospholipids with lower efficiency.
CC {ECO:0000250|UniProtKB:Q9UP65}.
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63765;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63769;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63657;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63773;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63761;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63789;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63777;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63785;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
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:0000250|UniProtKB:Q9UP65};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63781;
CC Evidence={ECO:0000250|UniProtKB:Q9UP65};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15950603}. Nucleus envelope
CC {ECO:0000269|PubMed:15950603}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15950603}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15950603}. Note=In germinal vesicle stage oocytes
CC and early embryos, shows mainly uniform nuclear and cortical
CC expression. During germinal vesicle breakdown, found in intensely
CC stained foci which accumulate near the dissolving nuclear envelope.
CC Also localizes to spindle poles at metaphase II.
CC {ECO:0000269|PubMed:15950603}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64GA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64GA5-2; Sequence=VSP_058982;
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary, where it localizes to
CC oocytes in preantral and antral stage follicles (at protein level). Not
CC detected in other tissues tested. {ECO:0000269|PubMed:15950603}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in oocytes at the germinal
CC vesicle stage, and in zygotes (at protein level). Maternal expression
CC persists in embryos at the 2-cell stage but then declines rapidly and
CC is completely lost by the morula stage (at protein level).
CC {ECO:0000269|PubMed:15950603}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY694793; AAU14177.1; -; mRNA.
DR EMBL; AK136098; BAE22819.1; -; mRNA.
DR EMBL; AK136143; BAE22843.1; -; mRNA.
DR EMBL; AK145339; BAE26375.1; -; mRNA.
DR EMBL; AK162196; BAE36785.1; -; mRNA.
DR EMBL; AC161792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054740; AAH54740.1; -; mRNA.
DR EMBL; BC117808; AAI17809.1; -; mRNA.
DR EMBL; BC117809; AAI17810.1; -; mRNA.
DR EMBL; BC129974; AAI29975.1; -; mRNA.
DR EMBL; BC138548; AAI38549.1; -; mRNA.
DR EMBL; BC145767; AAI45768.1; -; mRNA.
DR CCDS; CCDS39771.1; -. [Q64GA5-1]
DR CCDS; CCDS52027.1; -. [Q64GA5-2]
DR RefSeq; NP_001004762.1; NM_001004762.3. [Q64GA5-1]
DR RefSeq; NP_001161976.1; NM_001168504.1. [Q64GA5-2]
DR RefSeq; XP_011248813.1; XM_011250511.2. [Q64GA5-2]
DR RefSeq; XP_017177638.1; XM_017322149.1. [Q64GA5-2]
DR AlphaFoldDB; Q64GA5; -.
DR SMR; Q64GA5; -.
DR STRING; 10090.ENSMUSP00000043672; -.
DR iPTMnet; Q64GA5; -.
DR PhosphoSitePlus; Q64GA5; -.
DR REPRODUCTION-2DPAGE; Q64GA5; -.
DR MaxQB; Q64GA5; -.
DR PRIDE; Q64GA5; -.
DR ProteomicsDB; 294316; -. [Q64GA5-1]
DR ProteomicsDB; 294317; -. [Q64GA5-2]
DR Antibodypedia; 31649; 118 antibodies from 28 providers.
DR DNASU; 232889; -.
DR Ensembl; ENSMUST00000043612; ENSMUSP00000043672; ENSMUSG00000033847. [Q64GA5-1]
DR Ensembl; ENSMUST00000108528; ENSMUSP00000104168; ENSMUSG00000033847. [Q64GA5-2]
DR Ensembl; ENSMUST00000167232; ENSMUSP00000127060; ENSMUSG00000033847. [Q64GA5-2]
DR GeneID; 232889; -.
DR KEGG; mmu:232889; -.
DR UCSC; uc009ffs.2; mouse.
DR UCSC; uc009fft.2; mouse. [Q64GA5-1]
DR CTD; 8605; -.
DR MGI; MGI:1196403; Pla2g4c.
DR VEuPathDB; HostDB:ENSMUSG00000033847; -.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_2_0_1; -.
DR OMA; TTRNFLY; -.
DR OrthoDB; 302848at2759; -.
DR TreeFam; TF325228; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR Reactome; R-MMU-1483152; Hydrolysis of LPE.
DR BioGRID-ORCS; 232889; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pla2g4c; mouse.
DR PRO; PR:Q64GA5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q64GA5; protein.
DR Bgee; ENSMUSG00000033847; Expressed in animal zygote and 121 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005819; C:spindle; 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; ISO:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; ISO:MGI.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:MGI.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; ISS: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; Cytoplasm; Cytoskeleton; Hydrolase; Lipid metabolism;
KW Nucleus; Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..597
FT /note="Cytosolic phospholipase A2 gamma"
FT /id="PRO_0000440671"
FT DOMAIN 1..597
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 576..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT VAR_SEQ 1..3
FT /note="MEL -> MSCAESPKSLHKR (in isoform 2)"
FT /id="VSP_058982"
SQ SEQUENCE 597 AA; 67882 MW; 1566024D000DDFE6 CRC64;
MELSSGVCPA TRLQEAEKAA VHKRSPKVLE ALRKLNIQAD QAPVIAVLGS GGGLRAHIAC
LGVLSELKEL GLLDAVTYLA GVSGSTWALS SLYTKNGNME GIEEELKHRY EKNEWDFHES
LEKAIQASKR ENYSLTDFWA YLIVSRQIRE LQDSNLSSLK KQVEEGVLPY PIFAAIDEDL
LADWRERKTQ NSWFEFTPHH AGYPALGAYV PITEFGSRFE NGKLVKSEPE RDLTFLRGLW
GSAFADIKEI KNYILNYFRN PFGKLKFIEG PVTYSEAPRM NVDAMLLDLV MAYFTDMNDP
SIKDKLCALQ QALGTETDEF GIEMAEIIQN WNETSAEKKE QFLDHLLDRF KKTQEDTTTY
SLMNWNTGLV WDRCVFVNET RKCVSKWQWG TVYNFLYKHG KIADETMCSR ELLHLVDAGF
AINTPYPLVL PPVRETHLIL SFDFSAGDPL ETIRATADYC QRHEIPFPEV SEDQLKEWAK
APASCYVLRG ETGPVVMHFT LFNKDNCGDD IETWRKKYGT VKLSDSYTPD LVRDLLRVSK
ENVKKNKINI LSEMRKVAGN PGNIPRVNKE ACLGDRVKDP QGSQTVEFKK SHNISKD
