ID   PA24F_HUMAN             Reviewed;         849 AA.
AC   Q68DD2; Q6ZMC8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Cytosolic phospholipase A2 zeta;
DE            Short=cPLA2-zeta;
DE            EC=3.1.1.4 {ECO:0000269|PubMed:29158256};
DE   AltName: Full=Phospholipase A2 group IVF;
GN   Name=PLA2G4F;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-849 (ISOFORM 3), AND VARIANT
RP   VAL-740.
RC   TISSUE=Fetal kidney;
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   [4]
RP   PROTEIN SEQUENCE OF 1-13; 191-215; 526-543 AND 553-587, IDENTIFICATION BY
RP   MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Myocardium;
RX   PubMed=29158256; DOI=10.1074/jbc.ra117.000405;
RA   Moon S.H., Liu X., Cedars A.M., Yang K., Kiebish M.A., Joseph S.M.,
RA   Kelley J., Jenkins C.M., Gross R.W.;
RT   "Heart failure-induced activation of phospholipase iPLA2gamma generates
RT   hydroxyeicosatetraenoic acids opening the mitochondrial permeability
RT   transition pore.";
RL   J. Biol. Chem. 293:115-129(2018).
CC   -!- FUNCTION: Has calcium-dependent phospholipase and lysophospholipase
CC       activities with a potential role in membrane lipid remodeling and
CC       biosynthesis of lipid mediators (PubMed:29158256). Preferentially
CC       hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC       position of phospholipids (phospholipase A2 activity)
CC       (PubMed:29158256). Selectively hydrolyzes sn-2 arachidonoyl group from
CC       membrane phospholipids, providing the precursor for eicosanoid
CC       biosynthesis (PubMed:29158256). In myocardial mitochondria, plays a
CC       major role in arachidonate release that is metabolically channeled to
CC       the formation of cardioprotective eicosanoids, epoxyeicosatrienoates
CC       (EETs) (PubMed:29158256). {ECO:0000269|PubMed:29158256}.
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:29158256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:29158256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC         Xref=Rhea:RHEA:36231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:30909, ChEBI:CHEBI:36702; EC=3.1.1.4;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36232;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC         hexadecanoate + H(+); Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC         ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
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:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine +
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:40427,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC         Evidence={ECO:0000269|PubMed:29158256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000305|PubMed:29158256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine + (9Z,12Z)-octadecadienoate + H(+);
CC         Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine + (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+);
CC         Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-
CC         phosphocholine + H2O = 2-O-hexadecyl-sn-glycero-3-phosphocholine +
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:41271,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:77695, ChEBI:CHEBI:77696;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC         phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine +
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + 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:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol
CC         3-phosphocholine + hexadecanoate + H(+); 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:Q50L41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q50L41, ECO:0000255|PROSITE-
CC         ProRule:PRU00041};
CC   -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+).
CC       {ECO:0000250|UniProtKB:Q50L41}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q50L41}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q50L41}; Peripheral membrane protein
CC       {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:29158256}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q68DD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68DD2-2; Sequence=VSP_019888, VSP_019889;
CC       Name=3;
CC         IsoId=Q68DD2-3; Sequence=VSP_019887;
CC   -!- TISSUE SPECIFICITY: Expressed in myocardium (at protein level).
CC       {ECO:0000269|PubMed:29158256}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. It modulates enzyme activity by presenting the active
CC       site to its substrate in response to elevations of cytosolic Ca(2+) (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AK172836; BAD18801.1; -; mRNA.
DR   EMBL; AC036103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR749451; CAH18288.1; -; mRNA.
DR   CCDS; CCDS32204.1; -. [Q68DD2-1]
DR   RefSeq; NP_998765.3; NM_213600.4. [Q68DD2-1]
DR   AlphaFoldDB; Q68DD2; -.
DR   SMR; Q68DD2; -.
DR   BioGRID; 129083; 10.
DR   FunCoup; Q68DD2; 928.
DR   IntAct; Q68DD2; 9.
DR   NDEx; IQUERY-CP-PLA2G4F; 4 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000380442; -.
DR   iPTMnet; Q68DD2; -.
DR   PhosphoSitePlus; Q68DD2; -.
DR   BioMuta; PLA2G4F; -.
DR   DMDM; 317373489; -.
DR   jPOST; Q68DD2; -.
DR   MassIVE; Q68DD2; -.
DR   PaxDb; 9606-ENSP00000380442; -.
DR   PeptideAtlas; Q68DD2; -.
DR   ProteomicsDB; 66075; -. [Q68DD2-1]
DR   ProteomicsDB; 66076; -. [Q68DD2-2]
DR   ProteomicsDB; 66077; -. [Q68DD2-3]
DR   Antibodypedia; 42117; 68 antibodies from 24 providers.
DR   DNASU; 255189; -.
DR   Ensembl; ENST00000397272.7; ENSP00000380442.4; ENSG00000168907.14. [Q68DD2-1]
DR   GeneID; 255189; -.
DR   KEGG; hsa:255189; -.
DR   MANE-Select; ENST00000397272.7; ENSP00000380442.4; NM_213600.4; NP_998765.3.
DR   UCSC; uc001zoz.4; human. [Q68DD2-1]
DR   AGR; HGNC:27396; -.
DR   ClinPGx; PA142671170; -.
DR   CTD; 255189; -.
DR   DisGeNET; 255189; -.
DR   GeneCards; PLA2G4F; -.
DR   HGNC; HGNC:27396; PLA2G4F.
DR   HPA; ENSG00000168907; Tissue enriched (skin).
DR   OpenTargets; ENSG00000168907; -.
DR   VEuPathDB; HostDB:ENSG00000168907; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   GeneTree; ENSGT01030000234606; -.
DR   HOGENOM; CLU_011663_0_0_1; -.
DR   InParanoid; Q68DD2; -.
DR   OMA; PMRLKTR; -.
DR   OrthoDB; 419768at2759; -.
DR   PAN-GO; Q68DD2; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q68DD2; -.
DR   PathwayCommons; Q68DD2; -.
DR   Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR   SignaLink; Q68DD2; -.
DR   Agora; ENSG00000168907; -.
DR   BioGRID-ORCS; 255189; 7 hits in 1144 CRISPR screens.
DR   GenomeRNAi; 255189; -.
DR   Pharos; Q68DD2; Tdark.
DR   PRO; PR:Q68DD2; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q68DD2; protein.
DR   Bgee; ENSG00000168907; Expressed in skin of abdomen and 115 other cell types or tissues.
DR   ExpressionAtlas; Q68DD2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; EXP:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; EXP:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR   GO; GO:0008970; F:glycerophospholipid phospholipase A1 activity; TAS:Reactome.
DR   GO; GO:0004622; F:phosphatidylcholine lysophospholipase A1 activity; IEA:Ensembl.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   CDD; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 1.
DR   FunFam; 2.60.40.150:FF:000030; Phospholipase A2; 1.
DR   FunFam; 3.40.1090.10:FF:000002; Phospholipase A2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF22; CYTOSOLIC PHOSPHOLIPASE A2 ZETA; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Metal-binding; Mitochondrion; Phospholipid degradation;
KW   Phospholipid metabolism; Proteomics identification; Reference proteome.
FT   CHAIN           1..849
FT                   /note="Cytosolic phospholipase A2 zeta"
FT                   /id="PRO_0000247027"
FT   DOMAIN          27..145
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          306..849
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        680
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         118
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         118
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         123
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   VAR_SEQ         352
FT                   /note="G -> GQV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_019887"
FT   VAR_SEQ         433..454
FT                   /note="ALSTERLQYYTQELGVRERSGH -> DVRVSPCQLPRLHSSNLDHSLW (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019888"
FT   VAR_SEQ         455..849
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019889"
FT   VARIANT         30
FT                   /note="G -> V (in dbSNP:rs636604)"
FT                   /id="VAR_053553"
FT   VARIANT         740
FT                   /note="M -> V (in dbSNP:rs1356410)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_027054"
FT   CONFLICT        203
FT                   /note="R -> G (in Ref. 1; BAD18801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="A -> T (in Ref. 1; BAD18801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="G -> E (in Ref. 3; CAH18288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   849 AA;  95082 MW;  B2231EC3A9494598 CRC64;
     MLWALWPRWL ADKMLPLLGA VLLQKREKRG PLWRHWRRET YPYYDLQVKV LRATNIRGTD
     LLSKADCYVQ LWLPTASPSP AQTRIVANCS DPEWNETFHY QIHGAVKNVL ELTLYDKDIL
     GSDQLSLLLF DLRSLKCGQP HKHTFPLNHQ DSQELQVEFV LEKSQVPASE VITNGVLVAH
     PCLRIQGTLR GDGTAPREEY GSRQLQLAVP GAYEKPQLLP LQPPTEPGLP PTFTFHVNPV
     LSSRLHVELM ELLAAVQSGP SAELEAQTSK LGEGGILLSS LPLGQEEQCS VALGEGQEVA
     LSMKVEMSSG DLDLRLGFDL SDGEQEFLDR RKQVVSKALQ QVLGLSEALD SGQVPVVAVL
     GSGGGTRAMS SLYGSLAGLQ ELGLLDTVTY LSGVSGSTWC ISTLYRDPAW SQVALQGPIE
     RAQVHVCSSK MGALSTERLQ YYTQELGVRE RSGHSVSLID LWGLLVEYLL YQEENPAKLS
     DQQEAVRQGQ NPYPIYTSVN VRTNLSGEDF AEWCEFTPYE VGFPKYGAYV PTELFGSELF
     MGRLLQLQPE PRICYLQGMW GSAFATSLDE IFLKTAGSGL SFLEWYRGSV NITDDCQKPQ
     LHNPSRLRTR LLTPQGPFSQ AVLDIFTSRF TSAQSFNFTR GLCLHKDYVA GREFVAWKDT
     HPDAFPNQLT PMRDCLYLVD GGFAINSPFP LALLPQRAVD LILSFDYSLE APFEVLKMTE
     KYCLDRGIPF PSIEVGPEDM EEARECYLFA KAEDPRSPIV LHFPLVNRTF RTHLAPGVER
     QTAEEKAFGD FVINRPDTPY GMMNFTYEPQ DFYRLVALSR YNVLNNVETL KCALQLALDR
     HQARERAGA
//