PA2G3_HUMAN
ID PA2G3_HUMAN Reviewed; 509 AA.
AC Q9NZ20; O95768;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Group 3 secretory phospholipase A2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:12522102, ECO:0000269|PubMed:18801741};
DE AltName: Full=Group III secretory phospholipase A2;
DE Short=GIII sPLA2;
DE Short=sPLA2-III;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 3;
DE Flags: Precursor;
GN Name=PLA2G3 {ECO:0000312|HGNC:HGNC:17934};
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], CHARACTERIZATION, AND VARIANT ALA-70.
RX PubMed=10713052; DOI=10.1074/jbc.275.11.7492;
RA Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.;
RT "Novel human secreted phospholipase A2 with homology to the group III bee
RT venom enzyme.";
RL J. Biol. Chem. 275:7492-7496(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-70.
RC TISSUE=Brain;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF HIS-184.
RX PubMed=12522102; DOI=10.1074/jbc.m211325200;
RA Murakami M., Masuda S., Shimbara S., Bezzine S., Lazdunski M., Lambeau G.,
RA Gelb M.H., Matsukura S., Kokubu F., Adachi M., Kudo I.;
RT "Cellular arachidonate-releasing function of novel classes of secretory
RT phospholipase A2s (groups III and XII).";
RL J. Biol. Chem. 278:10657-10667(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, PTM, TISSUE SPECIFICITY, INDUCTION,
RP GLYCOSYLATION AT ASN-167 AND ASN-280, AND MUTAGENESIS OF ASN-167; HIS-184
RP AND ASN-280.
RX PubMed=15863501; DOI=10.1074/jbc.m502088200;
RA Murakami M., Masuda S., Shimbara S., Ishikawa Y., Ishii T., Kudo I.;
RT "Cellular distribution, post-translational modification, and tumorigenic
RT potential of human group III secreted phospholipase A(2).";
RL J. Biol. Chem. 280:24987-24998(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF HIS-184.
RX PubMed=17868035; DOI=10.1042/bj20070844;
RA Masuda S., Yamamoto K., Hirabayashi T., Ishikawa Y., Ishii T., Kudo I.,
RA Murakami M.;
RT "Human group III secreted phospholipase A2 promotes neuronal outgrowth and
RT survival.";
RL Biochem. J. 409:429-438(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=18801741; DOI=10.1074/jbc.m804628200;
RA Sato H., Kato R., Isogai Y., Saka G., Ohtsuki M., Taketomi Y., Yamamoto K.,
RA Tsutsumi K., Yamada J., Masuda S., Ishikawa Y., Ishii T., Kobayashi T.,
RA Ikeda K., Taguchi R., Hatakeyama S., Hara S., Kudo I., Itabe H.,
RA Murakami M.;
RT "Analyses of group III secreted phospholipase A2 transgenic mice reveal
RT potential participation of this enzyme in plasma lipoprotein modification,
RT macrophage foam cell formation, and atherosclerosis.";
RL J. Biol. Chem. 283:33483-33497(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T.,
RA Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-184.
RX PubMed=23624557; DOI=10.1038/ni.2586;
RA Taketomi Y., Ueno N., Kojima T., Sato H., Murase R., Yamamoto K.,
RA Tanaka S., Sakanaka M., Nakamura M., Nishito Y., Kawana M., Kambe N.,
RA Ikeda K., Taguchi R., Nakamizo S., Kabashima K., Gelb M.H., Arita M.,
RA Yokomizo T., Nakamura M., Watanabe K., Hirai H., Nakamura M., Okayama Y.,
RA Ra C., Aritake K., Urade Y., Morimoto K., Sugimoto Y., Shimizu T.,
RA Narumiya S., Hara S., Murakami M.;
RT "Mast cell maturation is driven via a group III phospholipase A2-
RT prostaglandin D2-DP1 receptor paracrine axis.";
RL Nat. Immunol. 14:554-563(2013).
RN [11]
RP FUNCTION.
RX PubMed=28947740; DOI=10.1038/s41598-017-12434-z;
RA Murase R., Taketomi Y., Miki Y., Nishito Y., Saito M., Fukami K.,
RA Yamamoto K., Murakami M.;
RT "Group III phospholipase A2 promotes colitis and colorectal cancer.";
RL Sci. Rep. 7:12261-12261(2017).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids. Hydrolyzes the ester bond of the
CC fatty acyl group attached at sn-2 position of phospholipids without
CC apparent head group selectivity (PubMed:12522102, PubMed:18801741,
CC PubMed:15863501, PubMed:28947740). Contributes to phospholipid
CC remodeling of low-density lipoprotein (LDL) and high-density
CC lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing
CC unsaturated fatty acids that regulate macrophage differentiation toward
CC foam cells (PubMed:18801741). May act in an autocrine and paracrine
CC manner (PubMed:23624557). Secreted by immature mast cells, acts on
CC nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2
CC (PGD2), which in turn promotes mast cell maturation and degranulation
CC via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on
CC immature sperm cells within the duct, modulating the degree of
CC unsaturation of the fatty acyl components of phosphatidylcholines
CC required for acrosome assembly and sperm cell motility. Facilitates the
CC replacement of fatty acyl chains in phosphatidylcholines in sperm
CC membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty
CC acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6
CC PUFAs to generate oxygenated lipid mediators in the male reproductive
CC tract (By similarity). At pericentrosomal preciliary compartment,
CC negatively regulates ciliogenesis likely by regulating endocytotic
CC recycling of ciliary membrane protein (PubMed:20393563). Coupled to
CC cyclooxygenase pathway provides arachidonate to generate prostaglandin
CC E2 (PGE2), a potent immunomodulatory lipid in inflammation and
CC tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial
CC barrier, preferentially hydrolyzes phospholipids having arachidonate
CC and docosahexaenoate at sn-2 position, contributing to the generation
CC of oxygenated metabolites involved in colonic stem cell homeostasis
CC (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine
CC subclasses from neuron plasma membranes and promotes neurite outgrowth
CC and neuron survival (PubMed:17868035). {ECO:0000250|UniProtKB:Q8BZT7,
CC ECO:0000269|PubMed:12522102, ECO:0000269|PubMed:15863501,
CC ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:18801741,
CC ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:23624557,
CC ECO:0000269|PubMed:28947740}.
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:12522102, ECO:0000269|PubMed:18801741};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:12522102, ECO:0000305|PubMed:18801741};
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:12522102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:12522102};
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:12522102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:12522102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + 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:0000269|PubMed:12522102, ECO:0000269|PubMed:15863501,
CC ECO:0000269|PubMed:18801741, ECO:0000269|PubMed:23624557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:12522102, ECO:0000305|PubMed:15863501,
CC ECO:0000305|PubMed:18801741, ECO:0000305|PubMed:23624557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + 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:0000269|PubMed:12522102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:12522102};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00630};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P00630};
CC -!- ACTIVITY REGULATION: Arachidonic acid release is markedly increased by
CC glypican, a glycosylphosphatidylinositol-anchored heparan sulfate
CC proteoglycan. {ECO:0000269|PubMed:12522102}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12522102}. Cell
CC membrane {ECO:0000269|PubMed:12522102}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:20393563}. Recycling endosome
CC {ECO:0000269|PubMed:20393563}. Note=Localized at pericentrosomal
CC preciliary compartment. {ECO:0000269|PubMed:20393563}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart, liver, and skeletal
CC muscle. Also present in placenta and peripheral blood leukocytes. Not
CC detected in colon, thymus, spleen and small intestine. In lung,
CC expressed in bronchial epithelial cells and alveolar macrophages, but
CC scarcely detected in alveolar epithelium, arterial walls and
CC interstitial fibroblasts (at protein level). In joints of
CC osteoarthritis and rheumatoid arthritis, expressed in endothelial cells
CC (at protein level). In normal heart, detected in some vessels. In
CC myocardial tissues with acute infarction, expressed in vascular
CC endothelial cells adjacent to cardiomyocytes and those in lesions with
CC granulation. Expression in cardiomyocytes is scarce (at protein level).
CC In uterus, breast and colon cancers, detected in tumor cells and
CC neighboring microvascular endothelium, but not in normal glandular
CC tissues (at protein level) (PubMed:15863501). Expressed in dermal
CC resting mast cells (at protein level) and pulmonary mast cells
CC (PubMed:23624557). Expressed in neuronal fibers (at protein level)
CC (PubMed:17868035). Highly expressed in dorsal root ganglia neurons (at
CC protein level) (PubMed:17868035). Expressed in Purkinje cells in
CC cerebellum (at protein level) (PubMed:17868035). In stomach is
CC preferentially expressed in neuronal fibers and in microvascular
CC endothelium (PubMed:17868035). Sparsely expressed in normal aorta (at
CC protein level). Highly expressed in macrophages and smooth muscle cells
CC in aorta with atheroma (PubMed:18801741). {ECO:0000269|PubMed:15863501,
CC ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:18801741,
CC ECO:0000269|PubMed:23624557}.
CC -!- INDUCTION: By IL1B/interleukin-1 beta and TNF in microvascular
CC endothelial cells (at protein level). {ECO:0000269|PubMed:15863501}.
CC -!- DOMAIN: The phospholipase A2-like domain represents the fully processed
CC form after N- and C-termini are cleaved off. It is the secreted mature
CC form found in biological fluids. {ECO:0000269|PubMed:12522102,
CC ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035}.
CC -!- PTM: N-glycosylation does not affect the catalytic activity, but is
CC required for proper secretion. A nonglycosylated form is observed in
CC several cell types. {ECO:0000269|PubMed:15863501}.
CC -!- PTM: In several cell types, the N- and C-termini are cleaved off.
CC {ECO:0000305|PubMed:15863501}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15617.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF220490; AAF44746.1; -; mRNA.
DR EMBL; AC005005; AAD15617.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC025316; AAH25316.1; -; mRNA.
DR CCDS; CCDS13889.1; -.
DR RefSeq; NP_056530.2; NM_015715.4.
DR AlphaFoldDB; Q9NZ20; -.
DR SMR; Q9NZ20; -.
DR BioGRID; 119074; 30.
DR IntAct; Q9NZ20; 2.
DR STRING; 9606.ENSP00000215885; -.
DR BindingDB; Q9NZ20; -.
DR ChEMBL; CHEMBL4667; -.
DR SwissLipids; SLP:000001086; -.
DR GlyGen; Q9NZ20; 5 sites.
DR iPTMnet; Q9NZ20; -.
DR PhosphoSitePlus; Q9NZ20; -.
DR BioMuta; PLA2G3; -.
DR DMDM; 317373314; -.
DR EPD; Q9NZ20; -.
DR MassIVE; Q9NZ20; -.
DR PaxDb; Q9NZ20; -.
DR PeptideAtlas; Q9NZ20; -.
DR PRIDE; Q9NZ20; -.
DR ProteomicsDB; 83316; -.
DR Antibodypedia; 11027; 189 antibodies from 23 providers.
DR DNASU; 50487; -.
DR Ensembl; ENST00000215885.4; ENSP00000215885.3; ENSG00000100078.4.
DR GeneID; 50487; -.
DR KEGG; hsa:50487; -.
DR MANE-Select; ENST00000215885.4; ENSP00000215885.3; NM_015715.5; NP_056530.2.
DR UCSC; uc003aka.4; human.
DR CTD; 50487; -.
DR DisGeNET; 50487; -.
DR GeneCards; PLA2G3; -.
DR HGNC; HGNC:17934; PLA2G3.
DR HPA; ENSG00000100078; Group enriched (esophagus, skin, vagina).
DR MIM; 611651; gene.
DR neXtProt; NX_Q9NZ20; -.
DR OpenTargets; ENSG00000100078; -.
DR PharmGKB; PA38267; -.
DR VEuPathDB; HostDB:ENSG00000100078; -.
DR eggNOG; ENOG502QTYI; Eukaryota.
DR GeneTree; ENSGT00940000161662; -.
DR HOGENOM; CLU_535922_0_0_1; -.
DR InParanoid; Q9NZ20; -.
DR OMA; CPQNISP; -.
DR OrthoDB; 893757at2759; -.
DR PhylomeDB; Q9NZ20; -.
DR TreeFam; TF324679; -.
DR PathwayCommons; Q9NZ20; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR SignaLink; Q9NZ20; -.
DR BioGRID-ORCS; 50487; 5 hits in 1068 CRISPR screens.
DR GenomeRNAi; 50487; -.
DR Pharos; Q9NZ20; Tbio.
DR PRO; PR:Q9NZ20; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NZ20; protein.
DR Bgee; ENSG00000100078; Expressed in gingival epithelium and 90 other tissues.
DR Genevisible; Q9NZ20; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0019372; P:lipoxygenase pathway; IEA:Ensembl.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IDA:UniProtKB.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:UniProtKB.
DR GO; GO:0060376; P:positive regulation of mast cell differentiation; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:Ensembl.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR Gene3D; 1.20.90.10; -; 2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF48619; SSF48619; 2.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Endosome; Glycoprotein; Hydrolase;
KW Lipid metabolism; Mast cell degranulation; Membrane; Metal-binding;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..509
FT /note="Group 3 secretory phospholipase A2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022992"
FT REGION 123..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..291
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000269|PubMed:12522102,
FT ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035"
FT REGION 283..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 214
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15863501"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15863501"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..181
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 180..220
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 187..213
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 211..244
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT VARIANT 70
FT /note="S -> A (in dbSNP:rs2232176)"
FT /evidence="ECO:0000269|PubMed:10713052,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024555"
FT VARIANT 116
FT /note="E -> Q (in dbSNP:rs2074734)"
FT /id="VAR_024556"
FT VARIANT 157
FT /note="L -> V (in dbSNP:rs2074735)"
FT /id="VAR_020288"
FT VARIANT 307
FT /note="H -> Y (in dbSNP:rs2232180)"
FT /id="VAR_056581"
FT VARIANT 322
FT /note="S -> R (in dbSNP:rs2072193)"
FT /id="VAR_024557"
FT VARIANT 378
FT /note="R -> Q (in dbSNP:rs2232183)"
FT /id="VAR_034366"
FT MUTAGEN 167
FT /note="N->S: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:15863501"
FT MUTAGEN 184
FT /note="H->Q: Impairs PGE2 synthesis. Impairs PGD2
FT synthesis. Impairs mast cell degranulation. Impairs neurite
FT outgrowth."
FT /evidence="ECO:0000269|PubMed:12522102,
FT ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035,
FT ECO:0000269|PubMed:23624557"
FT MUTAGEN 280
FT /note="N->S: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:15863501"
SQ SEQUENCE 509 AA; 57167 MW; ED03BED129B0BC9F CRC64;
MGVQAGLFGM LGFLGVALGG SPALRWYRTS CHLTKAVPGN PLGYLSFLAK DAQGLALIHA
RWDAHRRLQS CSWEDEPELT AAYGALCAHE TAWGSFIHTP GPELQRALAT LQSQWEACRA
LEESPAGARK KRAAGQSGVP GGGHQREKRG WTMPGTLWCG VGDSAGNSSE LGVFQGPDLC
CREHDRCPQN ISPLQYNYGI RNYRFHTISH CDCDTRFQQC LQNQHDSISD IVGVAFFNVL
EIPCFVLEEQ EACVAWYWWG GCRMYGTVPL ARLQPRTFYN ASWSSRATSP TPSSRSPAPP
KPRQKQHLRK GPPHQKGSKR PSKANTTALQ DPMVSPRLDV APTGLQGPQG GLKPQGARWV
CRSFRRHLDQ CEHQIGPREI EFQLLNSAQE PLFHCNCTRR LARFLRLHSP PEVTNMLWEL
LGTTCFKLAP PLDCVEGKNC SRDPRAIRVS ARHLRRLQQR RHQLQDKGTD ERQPWPSEPL
RGPMSFYNQC LQLTQAARRP DRQQKSWSQ
