PA2G3_MOUSE
ID PA2G3_MOUSE Reviewed; 504 AA.
AC Q8BZT7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Group 3 secretory phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q9NZ20};
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|MGI:MGI:2444945};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20424323; DOI=10.1172/jci40493;
RA Sato H., Taketomi Y., Isogai Y., Miki Y., Yamamoto K., Masuda S.,
RA Hosono T., Arata S., Ishikawa Y., Ishii T., Kobayashi T., Nakanishi H.,
RA Ikeda K., Taguchi R., Hara S., Kudo I., Murakami M.;
RT "Group III secreted phospholipase A2 regulates epididymal sperm maturation
RT and fertility in mice.";
RL J. Clin. Invest. 120:1400-1414(2010).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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:20424323). Contributes to
CC phospholipid remodeling of low-density lipoprotein (LDL) and high-
CC density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids
CC releasing unsaturated fatty acids that regulate macrophage
CC differentiation toward foam cells (By similarity). May act in an
CC autocrine and paracrine manner (PubMed:23624557). Secreted by immature
CC mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize
CC prostaglandin D2 (PGD2), which in turn promotes mast cell maturation
CC and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal
CC epithelium, acts on immature sperm cells within the duct, modulating
CC the degree of unsaturation of the fatty acyl components of
CC phosphatidylcholines required for acrosome assembly and sperm cell
CC motility (PubMed:20424323). Facilitates the replacement of fatty acyl
CC chains in phosphatidylcholines in sperm membranes from omega-6 and
CC omega-9 to omega-3 polyunsaturated fatty acids (PUFAs)
CC (PubMed:20424323). Coupled to lipoxygenase pathway, may process omega-6
CC PUFAs to generate oxygenated lipid mediators in the male reproductive
CC tract (PubMed:20424323). At pericentrosomal preciliary compartment,
CC negatively regulates ciliogenesis likely by regulating endocytotic
CC recycling of ciliary membrane protein (By similarity). Coupled to
CC cyclooxygenase pathway provides arachidonate to generate prostaglandin
CC E2 (PGE2), a potent immunomodulatory lipid in inflammation and
CC tumorigenesis (By similarity). At colonic epithelial barrier,
CC preferentially hydrolyzes phospholipids having arachidonate and
CC docosahexaenoate at sn-2 position, contributing to the generation of
CC 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:Q9NZ20,
CC ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:20424323,
CC ECO:0000269|PubMed:23624557, 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:0000250|UniProtKB:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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:20424323};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:20424323};
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:0000250|UniProtKB:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NZ20}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9NZ20}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9NZ20}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9NZ20}. Note=Localized at pericentrosomal
CC preciliary compartment. {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- TISSUE SPECIFICITY: Expressed in dermal mast cells (at protein level)
CC (PubMed:23624557). Highly expressed in EPCAM-positive colonic
CC epithelial cells throughout the proximal to distal colon (at protein
CC level) (PubMed:28947740). Expressed at lower levels in ileum section of
CC small intestine and immune organs including bone marrow, spleen and
CC lymph nodes (PubMed:28947740, PubMed:20424323). Expressed in stomach
CC and lung (at protein level) (PubMed:17868035). Expressed in testis and
CC epididymis and to a lesser extent in the seminal vesicles and prostate
CC (PubMed:20424323). Detected in ovary, oviduct and uterus
CC (PubMed:20424323). Expressed in Sertoli and Leydig cells as well as in
CC epididymal epithelium particularly in apical border of principal cells
CC in the corpus (at protein level) (PubMed:20424323). Present in cauda
CC epididymal fluid (at protein level) (PubMed:20424323). Expressed in
CC central nervous system, with high levels in spinal cord and at a lesser
CC extent in brain (at protein level) (PubMed:17868035, PubMed:20424323).
CC {ECO:0000269|PubMed:17868035, ECO:0000269|PubMed:20424323,
CC ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:28947740}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in dorsal root ganglia of the
CC developing brain at 12.5 dpc (at protein level).
CC {ECO:0000269|PubMed:17868035}.
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:0000250|UniProtKB:Q9NZ20}.
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:0000250|UniProtKB:Q9NZ20}.
CC -!- PTM: In several cell types, the N- and C-termini are cleaved off.
CC {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- DISRUPTION PHENOTYPE: Male mutant mice have reduced fertility
CC associated with reduced sperm cell motility, aberrant acrosomes and
CC flagella resulting in poor morula development. The litter size after
CC intercrossing heterozygous mutant male and female mice is significantly
CC smaller when compared to wild-type mice. Nevertheless, mutant offspring
CC are born at approximately Mendelian proportions, have normal survival,
CC appearance and behavior (PubMed:20424323). Mutant mice are resistant to
CC both passive systemic and active cutaneous anaphylaxis
CC (PubMed:23624557). In models of colon carcinogenesis either induced by
CC azoxymethane procarcinogen or upon activation of oncogenic Wnt/beta-
CC catenin signal due to a mutation in the APC gene (model of human
CC familial adenomatous polyposis), mutant mice are resistant to
CC tumorigeneis showing markedly decreased total tumor burden in the
CC colon. In a colitis model induced by toxic dextran sulfate sodium,
CC mutant mice are protected from shortening of the colon length and
CC mucosal inflammation and rapidly recover from epithelial injury
CC (PubMed:28947740). {ECO:0000269|PubMed:20424323,
CC ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:28947740}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AK033572; BAC28367.1; -; mRNA.
DR EMBL; AL713875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48740.1; -.
DR RefSeq; NP_766379.2; NM_172791.2.
DR AlphaFoldDB; Q8BZT7; -.
DR SMR; Q8BZT7; -.
DR STRING; 10090.ENSMUSP00000068699; -.
DR GlyGen; Q8BZT7; 2 sites.
DR PhosphoSitePlus; Q8BZT7; -.
DR PaxDb; Q8BZT7; -.
DR ProteomicsDB; 340549; -.
DR Antibodypedia; 11027; 189 antibodies from 23 providers.
DR DNASU; 237625; -.
DR Ensembl; ENSMUST00000064265; ENSMUSP00000068699; ENSMUSG00000034579.
DR GeneID; 237625; -.
DR KEGG; mmu:237625; -.
DR UCSC; uc007hsz.1; mouse.
DR CTD; 50487; -.
DR MGI; MGI:2444945; Pla2g3.
DR VEuPathDB; HostDB:ENSMUSG00000034579; -.
DR eggNOG; ENOG502QTYI; Eukaryota.
DR GeneTree; ENSGT00940000161662; -.
DR InParanoid; Q8BZT7; -.
DR OMA; CPQNISP; -.
DR OrthoDB; 893757at2759; -.
DR PhylomeDB; Q8BZT7; -.
DR TreeFam; TF324679; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR BioGRID-ORCS; 237625; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8BZT7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BZT7; protein.
DR Bgee; ENSMUSG00000034579; Expressed in interventricular septum and 64 other tissues.
DR ExpressionAtlas; Q8BZT7; baseline and differential.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IDA:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0019372; P:lipoxygenase pathway; IMP:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0042116; P:macrophage activation; IDA:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IMP:MGI.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IDA:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:MGI.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IMP:MGI.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IMP:UniProtKB.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0060376; P:positive regulation of mast cell differentiation; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:MGI.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IMP:MGI.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
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; 2.
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..504
FT /note="Group 3 secretory phospholipase A2"
FT /evidence="ECO:0000255"
FT /id="PRO_5015099043"
FT REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..287
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ20"
FT REGION 285..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..177
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 176..216
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 183..209
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 207..240
FT /evidence="ECO:0000250|UniProtKB:P00630"
SQ SEQUENCE 504 AA; 56687 MW; DAE0A7ED90915A53 CRC64;
MGVLGVLLGV LAFLEGSHTR HWDSTSCHLV QPIPGNPLGS LSFLGKDAQG LALFQAFWDT
HHRLQVCIRQ DESELITAFR ALCAHEPLQH SFIQTPGPAL QRALATLQSQ WEACQRSQDS
PTGAREKRAI EQSGAPDREH RRRRRGWTIP GTLWCGVGNS AENASELGVF HGPDLCCREH
DQCPQTISPL QYNYGIRNFR FHTISHCDCD ARFQQCLRSQ GDSISDIMGV AFFNVLEIPC
FVLKEQEACV AWNWWGGCRA YGSTPLAHLR PRTYYNASWK AEATSYTPSP QSPAPSKHPQ
KRGPQQTQAR RHSTTTTTPF QTPAISSRPD MIPRGQPGVP HLGFQDGPKH QSAHRVCRSL
RHLDQCEHQI KPQETKFHLL NSAQMPLFHC DCTRRLARFL RLHSPPAGTD KVWDLLGTTC
FKLAPQLDCA EGKGCSRDHR AIKVSARHLQ RLHKSRLHFR DKGTGGALAQ PVEPPGSTMS
FYSQCLQVTQ AIWRRRGQKK FWSS
