PA2GD_MOUSE
ID PA2GD_MOUSE Reviewed; 144 AA.
AC Q9WVF6; Q3V4B8; Q9JLK0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Group IID secretory phospholipase A2;
DE Short=GIID sPLA2;
DE Short=sPLA2-IID;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10531313};
DE AltName: Full=PLA2IID;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2D;
DE AltName: Full=Secretory-type PLA, stroma-associated homolog;
DE Flags: Precursor;
GN Name=Pla2g2d; Synonyms=Pla2a2, Splash;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION BY LIPOPOLYSACCHARIDE, AND SUBCELLULAR LOCATION (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=10455175; DOI=10.1074/jbc.274.35.24973;
RA Ishizaki J., Suzuki N., Higashino K., Yokota Y., Ono T., Kawamoto K.,
RA Fujii N., Arita H., Hanasaki K.;
RT "Cloning and characterization of novel mouse and human secretory
RT phospholipase A2s.";
RL J. Biol. Chem. 274:24973-24979(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10383420; DOI=10.1074/jbc.274.27.19152;
RA Valentin E., Koduri R.S., Scimeca J.-C., Carle G., Gelb M.H., Lazdunski M.,
RA Lambeau G.;
RT "Cloning and recombinant expression of a novel mouse-secreted phospholipase
RT A2.";
RL J. Biol. Chem. 274:19152-19160(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X 129;
RX PubMed=11196711; DOI=10.1038/sj.gene.6363659;
RA Shakhov A.N., Rubtsov A.V., Lyakhov I.G., Tumanov A.V., Nedospasov S.A.;
RT "SPLASH (PLA(2)IID), a novel member of phospholipase A2 family, is
RT associated with lymphotoxin-deficiency.";
RL Genes Immun. 1:191-199(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=10531313; DOI=10.1074/jbc.274.44.31195;
RA Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.;
RT "On the diversity of secreted phospholipases A2. Cloning, tissue
RT distribution, and functional expression of two novel mouse group II
RT enzymes.";
RL J. Biol. Chem. 274:31195-31202(1999).
RN [6]
RP FUNCTION.
RX PubMed=11694541; DOI=10.1074/jbc.m109699200;
RA Koduri R.S., Groenroos J.O., Laine V.J., Le Calvez C., Lambeau G.,
RA Nevalainen T.J., Gelb M.H.;
RT "Bactericidal properties of human and murine groups I, II, V, X, and XII
RT secreted phospholipases A(2).";
RL J. Biol. Chem. 277:5849-5857(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY TGFB1, SUBCELLULAR LOCATION
RP (ISOFORM 1), AND MUTAGENESIS OF HIS-66.
RX PubMed=19564598; DOI=10.1073/pnas.0812569106;
RA von Allmen C.E., Schmitz N., Bauer M., Hinton H.J., Kurrer M.O.,
RA Buser R.B., Gwerder M., Muntwiler S., Sparwasser T., Beerli R.R.,
RA Bachmann M.F.;
RT "Secretory phospholipase A2-IID is an effector molecule of CD4+CD25+
RT regulatory T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11673-11678(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23690440; DOI=10.1084/jem.20121887;
RA Miki Y., Yamamoto K., Taketomi Y., Sato H., Shimo K., Kobayashi T.,
RA Ishikawa Y., Ishii T., Nakanishi H., Ikeda K., Taguchi R., Kabashima K.,
RA Arita M., Arai H., Lambeau G., Bollinger J.M., Hara S., Gelb M.H.,
RA Murakami M.;
RT "Lymphoid tissue phospholipase A2 group IID resolves contact
RT hypersensitivity by driving antiinflammatory lipid mediators.";
RL J. Exp. Med. 210:1217-1234(2013).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26392224; DOI=10.1084/jem.20150632;
RA Vijay R., Hua X., Meyerholz D.K., Miki Y., Yamamoto K., Gelb M.,
RA Murakami M., Perlman S.;
RT "Critical role of phospholipase A2 group IID in age-related susceptibility
RT to severe acute respiratory syndrome-CoV infection.";
RL J. Exp. Med. 212:1851-1868(2015).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27226632; DOI=10.1074/jbc.m116.734624;
RA Miki Y., Kidoguchi Y., Sato M., Taketomi Y., Taya C., Muramatsu K.,
RA Gelb M.H., Yamamoto K., Murakami M.;
RT "Dual Roles of Group IID Phospholipase A2 in Inflammation and Cancer.";
RL J. Biol. Chem. 291:15588-15601(2016).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular lipids, exerting anti-inflammatory and
CC immunosuppressive functions (PubMed:10531313, PubMed:23690440,
CC PubMed:26392224, PubMed:10455175). Hydrolyzes the ester bond of the
CC fatty acyl group attached at sn-2 position of phospholipids
CC (phospholipase A2 activity) with preference for
CC phosphatidylethanolamines and phosphatidylglycerols over
CC phosphatidylcholines (By similarity). In draining lymph nodes,
CC selectively hydrolyzes diacyl and alkenyl forms of
CC phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty
CC acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are
CC precursors of the anti-inflammatory lipid mediators, resolvins
CC (PubMed:23690440). During the resolution phase of acute inflammation
CC drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses
CC dendritic cell activation and T-helper 1 immune response
CC (PubMed:23690440, PubMed:27226632). May act in an autocrine and
CC paracrine manner. Via a mechanism independent of its catalytic
CC activity, promotes differentiation of regulatory T cells (Tregs) and
CC participates in the maintenance of immune tolerance (PubMed:19564598).
CC May contribute to lipid remodeling of cellular membranes and generation
CC of lipid mediators involved in pathogen clearance. Displays
CC bactericidal activity against Gram-positive bacteria by directly
CC hydrolyzing phospholipids of the bacterial membrane (PubMed:11694541).
CC {ECO:0000250|UniProtKB:Q9UNK4, ECO:0000269|PubMed:10455175,
CC ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11694541,
CC ECO:0000269|PubMed:19564598, ECO:0000269|PubMed:23690440,
CC ECO:0000269|PubMed:26392224, ECO:0000269|PubMed:27226632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
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:0000250|UniProtKB:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O
CC = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000305|PubMed:10531313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
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:0000255|PROSITE-ProRule:PRU10035,
CC ECO:0000269|PubMed:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:10531313};
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:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:10531313};
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:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
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:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9UNK4};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UNK4};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000269|PubMed:10455175}. Cell membrane
CC {ECO:0000269|PubMed:19564598}. Note=Localizes to cell membrane likely
CC through binding to heparan sulfate proteoglycans.
CC {ECO:0000269|PubMed:19564598}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVF6-2; Sequence=VSP_004508;
CC -!- TISSUE SPECIFICITY: Highly expressed in secondary lymphoid tissues,
CC spleen and lymph nodes. Expressed at a lesser extent in thymus
CC (PubMed:11196711, PubMed:10455175, PubMed:10531313, PubMed:23690440).
CC Expressed in CD4-positive, IL2RA/CD25-positive, FOXP3-positive Tregs
CC (at protein level) (PubMed:19564598, PubMed:23690440). Expressed in
CC myeloid cell subsets resident in spleen and lymph nodes, ITGAX/CD11C-
CC positive dendritic cells and macrophages (at protein level). Enriched
CC in CD4-positive, ITGAM/CD11B-positive dendritic cell subset
CC (PubMed:19564598, PubMed:23690440). Expressed in pulmonary ITGAX/CD11C-
CC positive dendritic cell subset (at protein level) (PubMed:26392224).
CC {ECO:0000269|PubMed:10455175, ECO:0000269|PubMed:10531313,
CC ECO:0000269|PubMed:11196711, ECO:0000269|PubMed:19564598,
CC ECO:0000269|PubMed:23690440, ECO:0000269|PubMed:26392224}.
CC -!- DEVELOPMENTAL STAGE: Undetectable in embryonic spleens. Weak expression
CC is detected the first week after birth, with further increase to normal
CC levels by 4-6 weeks after birth. {ECO:0000269|PubMed:11196711}.
CC -!- INDUCTION: Up-regulated in thymus upon endotoxin challenge
CC (PubMed:10455175). Up-regulated during Treg differention in response to
CC TGFB1 (PubMed:19564598). Up-regulated in pulmonary ITGAX/CD11C-positive
CC dendritic cell subset upon chronic oxidative stress associated with
CC aging (PubMed:26392224). {ECO:0000269|PubMed:10455175,
CC ECO:0000269|PubMed:19564598, ECO:0000269|PubMed:26392224}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are born at the expected Mendelian
CC rate and have normal embryonic and postnatal development
CC (PubMed:23690440). They are susceptible to acute and chronic
CC inflammatory reactions and resistant to tumorigenesis. In a model of
CC hapten-induced contact hypersensitivity, mutant mice show an enhanced
CC T-helper 1 immune response in skin lymph nodes at sensitization phase
CC followed by delayed inflammation resolution with more severe ear
CC swelling, epidermal hyperplasia, and inflammatory cell infiltration at
CC elicitation phase (PubMed:23690440, PubMed:27226632). In a psoriasis
CC model, mutant mice show enhanced T-helper 17 immune response and
CC epidermal hyperplasia associated with decreased synthesis of omega-3
CC PUFAs (PubMed:27226632). In a model of chemically-induced skin
CC carcinogenesis, mutant mice show resistance to cutaneous papilloma
CC formation (PubMed:27226632). In response to SARS-CoV infection, mutant
CC middle-aged (10-13 month old) mice mount a potent antiviral T cell
CC response, resulting in more rapid virus clearance and significantly
CC decreased mortality compared with wild-type ones. This represents a
CC relevant model for SARS-CoV increased susceptibility with aging in
CC human (PubMed:26392224). {ECO:0000269|PubMed:23690440,
CC ECO:0000269|PubMed:26392224, ECO:0000269|PubMed:27226632}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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; AF112983; AAD51391.1; -; mRNA.
DR EMBL; AF124374; AAD42773.1; -; mRNA.
DR EMBL; AF188624; AAF09019.1; -; Genomic_DNA.
DR EMBL; AF169407; AAF42987.1; -; mRNA.
DR EMBL; AF169408; AAF42988.1; -; mRNA.
DR EMBL; AK004232; BAE43166.1; -; mRNA.
DR EMBL; AK018005; BAB31033.1; -; mRNA.
DR CCDS; CCDS18833.1; -. [Q9WVF6-1]
DR CCDS; CCDS84811.1; -. [Q9WVF6-2]
DR RefSeq; NP_001334159.1; NM_001347230.1. [Q9WVF6-2]
DR RefSeq; NP_035239.1; NM_011109.2. [Q9WVF6-1]
DR AlphaFoldDB; Q9WVF6; -.
DR SMR; Q9WVF6; -.
DR STRING; 10090.ENSMUSP00000030528; -.
DR BindingDB; Q9WVF6; -.
DR ChEMBL; CHEMBL5537; -.
DR GlyGen; Q9WVF6; 1 site.
DR PhosphoSitePlus; Q9WVF6; -.
DR PaxDb; Q9WVF6; -.
DR PRIDE; Q9WVF6; -.
DR ProteomicsDB; 294236; -. [Q9WVF6-1]
DR ProteomicsDB; 294237; -. [Q9WVF6-2]
DR Antibodypedia; 47984; 193 antibodies from 20 providers.
DR DNASU; 18782; -.
DR Ensembl; ENSMUST00000030528; ENSMUSP00000030528; ENSMUSG00000041202. [Q9WVF6-1]
DR Ensembl; ENSMUST00000105806; ENSMUSP00000101432; ENSMUSG00000041202. [Q9WVF6-2]
DR GeneID; 18782; -.
DR KEGG; mmu:18782; -.
DR UCSC; uc008vlg.1; mouse. [Q9WVF6-1]
DR CTD; 26279; -.
DR MGI; MGI:1341796; Pla2g2d.
DR VEuPathDB; HostDB:ENSMUSG00000041202; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000161938; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; Q9WVF6; -.
DR OMA; GDIQCSD; -.
DR PhylomeDB; Q9WVF6; -.
DR TreeFam; TF319283; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 18782; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Pla2g2d; mouse.
DR PRO; PR:Q9WVF6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WVF6; protein.
DR Bgee; ENSMUSG00000041202; Expressed in mesenteric lymph node and 56 other tissues.
DR ExpressionAtlas; Q9WVF6; baseline and differential.
DR Genevisible; Q9WVF6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0050868; P:negative regulation of T cell activation; IDA:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:MGI.
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:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0002864; P:regulation of acute inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Hydrolase; Inflammatory response; Lipid metabolism; Membrane;
KW Metal-binding; Phospholipid metabolism; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..144
FT /note="Group IID secretory phospholipase A2"
FT /id="PRO_0000022756"
FT ACT_SITE 66
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..137
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 47..63
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 62..117
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 68..144
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 69..110
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 78..103
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 96..108
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_004508"
FT MUTAGEN 66
FT /note="H->A: Has no effect on Treg effector functions."
FT /evidence="ECO:0000269|PubMed:19564598"
SQ SEQUENCE 144 AA; 16164 MW; 7697ADA07F8D270A CRC64;
MRLALLCGLL LAGITATQGG LLNLNKMVTH MTGKKAFFSY WPYGCHCGLG GKGQPKDATD
WCCQKHDCCY AHLKIDGCKS LTDNYKYSIS QGTIQCSDNG SWCERQLCAC DKEVALCLKQ
NLDSYNKRLR YYWRPRCKGK TPAC
