PA2GD_HUMAN
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 03-AUG-2022, entry version 179.
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 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 PRIDE; Q9UNK4; -.
DR ProteomicsDB; 85300; -.
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 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; 1422829at2759; -.
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 1066 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; -; 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; 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
