ID   PA2GD_HUMAN             Reviewed;         145 AA.
AC   Q9UNK4; A0A087WZT4; A8K2Z1; B1AEL9; Q9UK01;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 2.
DT   22-FEB-2023, entry version 182.
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:10455175, ECO:0000269|PubMed:10681567};
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=SPLASH;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND VARIANT GLY-80.
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=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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   GLY-80.
RC   TISSUE=Umbilical cord blood;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-65; ARG-73; GLY-80;
RP   ARG-96; CYS-121 AND LEU-121.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas, and Spleen;
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   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10681567; DOI=10.1074/jbc.275.8.5785;
RA   Suzuki N., Ishizaki J., Yokota Y., Higashino K., Ono T., Ikeda M.,
RA   Fujii N., Kawamoto K., Hanasaki K.;
RT   "Structures, enzymatic properties, and expression of novel human and mouse
RT   secretory phospholipase A(2)s.";
RL   J. Biol. Chem. 275:5785-5793(2000).
CC   -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC       targets extracellular lipids, exerting anti-inflammatory and
CC       immunosuppressive functions (PubMed:10455175, PubMed:10681567).
CC       Hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC       position of phospholipids (phospholipase A2 activity) with preference
CC       for phosphatidylethanolamines and phosphatidylglycerols over
CC       phosphatidylcholines (PubMed:10455175). 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 (By
CC       similarity). During the resolution phase of acute inflammation drives
CC       docosahexaenoate-derived resolvin D1 synthesis, which suppresses
CC       dendritic cell activation and T-helper 1 immune response (By
CC       similarity). May act in an autocrine and paracrine manner (By
CC       similarity). Via a mechanism independent of its catalytic activity,
CC       promotes differentiation of regulatory T cells (Tregs) and participates
CC       in the maintenance of immune tolerance (By similarity). May contribute
CC       to lipid remodeling of cellular membranes and generation of lipid
CC       mediators involved in pathogen clearance. Displays bactericidal
CC       activity against Gram-positive bacteria by directly hydrolyzing
CC       phospholipids of the bacterial membrane (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WVF6, ECO:0000269|PubMed:10455175,
CC       ECO:0000269|PubMed:10681567}.
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:0000269|PubMed:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:0000269|PubMed:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:0000250|UniProtKB:Q9WVF6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC         Evidence={ECO:0000250|UniProtKB:Q9WVF6};
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:0000269|PubMed:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:10455175, ECO:0000269|PubMed:10681567};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:10455175, ECO:0000305|PubMed:10681567};
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:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:0000269|PubMed:10455175,
CC         ECO:0000269|PubMed:10681567};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000305|PubMed:10455175, ECO:0000305|PubMed:10681567};
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:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000305|PubMed:10455175};
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:0000269|PubMed:10455175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC         Evidence={ECO:0000305|PubMed:10455175};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:10455175};
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-9. {ECO:0000269|PubMed:10455175};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10455175}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UNK4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UNK4-2; Sequence=VSP_060595, VSP_060596;
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreas and spleen and less
CC       abundantly in colon, thymus, placenta, small intestine, and prostate.
CC       {ECO:0000269|PubMed:10455175}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/pla2g2d/";
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DR   EMBL; AF112982; AAD51390.1; -; mRNA.
DR   EMBL; AF188625; AAF09020.1; -; mRNA.
DR   EMBL; AK290406; BAF83095.1; -; mRNA.
DR   EMBL; AK310156; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EU447440; ACA06110.1; -; Genomic_DNA.
DR   EMBL; AL158172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025706; AAH25706.1; -; mRNA.
DR   CCDS; CCDS203.1; -. [Q9UNK4-1]
DR   CCDS; CCDS72721.1; -. [Q9UNK4-2]
DR   RefSeq; NP_001258743.1; NM_001271814.1. [Q9UNK4-2]
DR   RefSeq; NP_036532.1; NM_012400.3. [Q9UNK4-1]
DR   AlphaFoldDB; Q9UNK4; -.
DR   SMR; Q9UNK4; -.
DR   BioGRID; 117662; 29.
DR   STRING; 9606.ENSP00000364246; -.
DR   BindingDB; Q9UNK4; -.
DR   ChEMBL; CHEMBL4281; -.
DR   DrugBank; DB03017; Lauric acid.
DR   DrugBank; DB03193; Stearic acid.
DR   GuidetoPHARMACOLOGY; 1418; -.
DR   SwissLipids; SLP:000000652; -.
DR   GlyCosmos; Q9UNK4; 1 site, No reported glycans.
DR   GlyGen; Q9UNK4; 1 site.
DR   iPTMnet; Q9UNK4; -.
DR   PhosphoSitePlus; Q9UNK4; -.
DR   BioMuta; PLA2G2D; -.
DR   DMDM; 20139286; -.
DR   MassIVE; Q9UNK4; -.
DR   PaxDb; Q9UNK4; -.
DR   PeptideAtlas; Q9UNK4; -.
DR   Antibodypedia; 47984; 193 antibodies from 20 providers.
DR   DNASU; 26279; -.
DR   Ensembl; ENST00000375105.8; ENSP00000364246.3; ENSG00000117215.15. [Q9UNK4-1]
DR   Ensembl; ENST00000617227.1; ENSP00000482871.1; ENSG00000117215.15. [Q9UNK4-2]
DR   GeneID; 26279; -.
DR   KEGG; hsa:26279; -.
DR   MANE-Select; ENST00000375105.8; ENSP00000364246.3; NM_012400.4; NP_036532.1.
DR   UCSC; uc001bcz.5; human. [Q9UNK4-1]
DR   AGR; HGNC:9033; -.
DR   CTD; 26279; -.
DR   DisGeNET; 26279; -.
DR   GeneCards; PLA2G2D; -.
DR   HGNC; HGNC:9033; PLA2G2D.
DR   HPA; ENSG00000117215; Tissue enriched (lymphoid).
DR   MIM; 605630; gene.
DR   neXtProt; NX_Q9UNK4; -.
DR   OpenTargets; ENSG00000117215; -.
DR   PharmGKB; PA33363; -.
DR   VEuPathDB; HostDB:ENSG00000117215; -.
DR   eggNOG; KOG4087; Eukaryota.
DR   GeneTree; ENSGT00940000161938; -.
DR   HOGENOM; CLU_090683_3_0_1; -.
DR   InParanoid; Q9UNK4; -.
DR   OMA; GDIQCSD; -.
DR   OrthoDB; 638584at2759; -.
DR   PhylomeDB; Q9UNK4; -.
DR   TreeFam; TF319283; -.
DR   BRENDA; 3.1.1.4; 2681.
DR   PathwayCommons; Q9UNK4; -.
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-1483166; Synthesis of PA.
DR   SignaLink; Q9UNK4; -.
DR   BioGRID-ORCS; 26279; 9 hits in 1144 CRISPR screens.
DR   ChiTaRS; PLA2G2D; human.
DR   GeneWiki; PLA2G2D; -.
DR   GenomeRNAi; 26279; -.
DR   Pharos; Q9UNK4; Tchem.
DR   PRO; PR:Q9UNK4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UNK4; protein.
DR   Bgee; ENSG00000117215; Expressed in lymph node and 66 other tissues.
DR   Genevisible; Q9UNK4; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0004623; F:phospholipase A2 activity; TAS:ProtInc.
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; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR   GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0046471; P:phosphatidylglycerol metabolic process; IEA:Ensembl.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0002864; P:regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 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:SF57; GROUP IID SECRETORY PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..145
FT                   /note="Group IID secretory phospholipase A2"
FT                   /id="PRO_0000022755"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..138
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        63..118
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        69..145
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        70..111
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        79..104
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        97..109
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   VAR_SEQ         62
FT                   /note="W -> C (in isoform 2)"
FT                   /id="VSP_060595"
FT   VAR_SEQ         63..145
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060596"
FT   VARIANT         65
FT                   /note="Q -> H (in dbSNP:rs62541890)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055387"
FT   VARIANT         73
FT                   /note="H -> R (in dbSNP:rs62541891)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055388"
FT   VARIANT         80
FT                   /note="S -> G (in dbSNP:rs584367)"
FT                   /evidence="ECO:0000269|PubMed:10455175,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT                   /id="VAR_012741"
FT   VARIANT         96
FT                   /note="H -> R (in dbSNP:rs62541892)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055389"
FT   VARIANT         121
FT                   /note="R -> C (in dbSNP:rs62541900)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055390"
FT   VARIANT         121
FT                   /note="R -> L (in dbSNP:rs62541901)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055391"
SQ   SEQUENCE   145 AA;  16546 MW;  CF3A49DE516BD1EF CRC64;
     MELALLCGLV VMAGVIPIQG GILNLNKMVK QVTGKMPILS YWPYGCHCGL GGRGQPKDAT
     DWCCQTHDCC YDHLKTQGCS IYKDYYRYNF SQGNIHCSDK GSWCEQQLCA CDKEVAFCLK
     RNLDTYQKRL RFYWRPHCRG QTPGC
//