PA2GA_HUMAN
ID PA2GA_HUMAN Reviewed; 144 AA.
AC P14555; A8K5I7; Q6DN24; Q6IBD9; Q9UCD2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Phospholipase A2, membrane associated;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10455175, ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:2925633};
DE AltName: Full=GIIC sPLA2;
DE AltName: Full=Group IIA phospholipase A2;
DE AltName: Full=Non-pancreatic secretory phospholipase A2;
DE Short=NPS-PLA2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2A;
DE Flags: Precursor;
GN Name=PLA2G2A; Synonyms=PLA2B, PLA2L, RASF-A;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Rheumatoid arthritic synovial fluid;
RX PubMed=2925608; DOI=10.1016/s0021-9258(18)83549-9;
RA Seilhamer J.J., Pruzanski W., Vadas P., Plant S., Miller J.A., Kloss J.,
RA Johnson L.K.;
RT "Cloning and recombinant expression of phospholipase A2 present in
RT rheumatoid arthritic synovial fluid.";
RL J. Biol. Chem. 264:5335-5338(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-39, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=2925633; DOI=10.1016/s0021-9258(18)83616-x;
RA Kramer R.M., Hession C., Johansen B., Hayes G., McGray P., Chow E.P.,
RA Tizard R., Pepinsky R.B.;
RT "Structure and properties of a human non-pancreatic phospholipase A2.";
RL J. Biol. Chem. 264:5768-5775(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2239446; DOI=10.1007/978-1-4684-5805-3_3;
RA Kramer R.M., Johansen B., Hession C., Pepinsky R.B.;
RT "Structure and properties of a secretable phospholipase A2 from human
RT platelets.";
RL Adv. Exp. Med. Biol. 275:35-53(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Liang N.S., Fang Z.W., Li Y., Yang F., Lu Y., Xie Y.A.;
RT "Cloning and sequence determination of human platelet phospholipase A2 from
RT liver tissues.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-19.
RG NIEHS SNPs program;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [11]
RP PROTEIN SEQUENCE OF 21-144, AND SUBCELLULAR LOCATION.
RC TISSUE=Spleen;
RX PubMed=2775276; DOI=10.1016/0006-291x(89)92096-2;
RA Kanda A., Ono T., Yoshida N., Tojo H., Okamoto M.;
RT "The primary structure of a membrane-associated phospholipase A2 from human
RT spleen.";
RL Biochem. Biophys. Res. Commun. 163:42-48(1989).
RN [12]
RP PROTEIN SEQUENCE OF 21-54.
RC TISSUE=Synovial fluid;
RX PubMed=3240982; DOI=10.1093/oxfordjournals.jbchem.a122467;
RA Hara S., Kudo I., Matsuta K., Miyamoto T., Inoue K.;
RT "Amino acid composition and NH2-terminal amino acid sequence of human
RT phospholipase A2 purified from rheumatoid synovial fluid.";
RL J. Biochem. 104:326-328(1988).
RN [13]
RP PROTEIN SEQUENCE OF 21-33.
RC TISSUE=Synovial fluid;
RX PubMed=3202859; DOI=10.1016/s0006-291x(88)80275-4;
RA Lai C.Y., Wada K.;
RT "Phospholipase A2 from human synovial fluid: purification and structural
RT homology to the placental enzyme.";
RL Biochem. Biophys. Res. Commun. 157:488-493(1988).
RN [14]
RP PROTEIN SEQUENCE OF 21-75.
RC TISSUE=Ileal mucosa;
RX PubMed=8399335;
RA Minami T., Tojo H., Shinomura Y., Matsuzawa Y., Okamoto M.;
RT "Purification and characterization of a phospholipase A2 from human ileal
RT mucosa.";
RL Biochim. Biophys. Acta 1170:125-130(1993).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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 [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10358193;
RA Laine V.J., Grass D.S., Nevalainen T.J.;
RT "Protection by group II phospholipase A2 against Staphylococcus aureus.";
RL J. Immunol. 162:7402-7408(1999).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF ARG-27; LYS-30; LYS-35; LYS-57; LYS-72;
RP ARG-73; ARG-77; LYS-87; LYS-99; ARG-104; LYS-122; LYS-127; LYS-128; LYS-135
RP AND ARG-138.
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 [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14998370; DOI=10.1042/bj20040031;
RA Sun Y.X., Tsuboi K., Okamoto Y., Tonai T., Murakami M., Kudo I., Ueda N.;
RT "Biosynthesis of anandamide and N-palmitoylethanolamine by sequential
RT actions of phospholipase A2 and lysophospholipase D.";
RL Biochem. J. 380:749-756(2004).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF ARG-62; HIS-67; ARG-73; ARG-94 AND ARG-120.
RX PubMed=18635536; DOI=10.1074/jbc.m804835200;
RA Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S., Liu F.T.,
RA Takada Y.K., Takada Y.;
RT "Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins
RT alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in
RT an integrin-dependent manner.";
RL J. Biol. Chem. 283:26107-26115(2008).
RN [21]
RP INHIBITION OF INTEGRIN BINDING.
RX PubMed=23164706; DOI=10.1016/j.bmcl.2012.10.080;
RA Ye L., Dickerson T., Kaur H., Takada Y.K., Fujita M., Liu R., Knapp J.M.,
RA Lam K.S., Schore N.E., Kurth M.J., Takada Y.;
RT "Identification of inhibitors against interaction between pro-inflammatory
RT sPLA2-IIA protein and integrin alphavbeta3.";
RL Bioorg. Med. Chem. Lett. 23:340-345(2013).
RN [22]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-67.
RX PubMed=25082876; DOI=10.1182/blood-2014-05-573543;
RA Boudreau L.H., Duchez A.C., Cloutier N., Soulet D., Martin N.,
RA Bollinger J., Pare A., Rousseau M., Naika G.S., Levesque T., Laflamme C.,
RA Marcoux G., Lambeau G., Farndale R.W., Pouliot M., Hamzeh-Cognasse H.,
RA Cognasse F., Garraud O., Nigrovic P.A., Guderley H., Lacroix S.,
RA Thibault L., Semple J.W., Gelb M.H., Boilard E.;
RT "Platelets release mitochondria serving as substrate for bactericidal group
RT IIA-secreted phospholipase A2 to promote inflammation.";
RL Blood 124:2173-2183(2014).
RN [23]
RP FUNCTION, AND MUTAGENESIS OF GLY-49; HIS-67; ASP-68; ARG-94 AND ARG-120.
RX PubMed=25398877; DOI=10.1074/jbc.m114.579946;
RA Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J., Takada Y.K.,
RA Takada Y.;
RT "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT integrin activation through direct binding to a newly identified binding
RT site (site 2) in integrins alphavbeta3, alpha4beta1, and alpha5beta1.";
RL J. Biol. Chem. 290:259-271(2015).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-144, AND DISULFIDE BOND.
RX PubMed=2062381; DOI=10.1038/352079a0;
RA Wery J.-P., Schevitz R.W., Clawson D.K., Bobbitt J.L., Dow E.R., Gamboa G.,
RA Goodson T. Jr., Hermann R.B., Kramer R.M., McClure D.B., Mihelich E.D.,
RA Putnam J.E., Sharp J.D., Stark D.H., Teater C., Warrick M.W., Jones N.D.;
RT "Structure of recombinant human rheumatoid arthritic synovial fluid
RT phospholipase A2 at 2.2-A resolution.";
RL Nature 352:79-82(1991).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-144 IN COMPLEX WITH CALCIUM,
RP AND DISULFIDE BOND.
RX PubMed=1948070; DOI=10.1126/science.1948070;
RA Scott D.L., White S.P., Browning J.L., Rosa J.J., Gelb M.H., Sigler P.B.;
RT "Structures of free and inhibited human secretory phospholipase A2 from
RT inflammatory exudate.";
RL Science 254:1007-1010(1991).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-144 IN COMPLEX WITH CALCIUM,
RP AND DISULFIDE BOND.
RX PubMed=7664108; DOI=10.1038/nsb0695-458;
RA Schevitz R.W., Bach N.J., Carlson D.G., Chirgadze N.Y., Clawson D.K.,
RA Dillard R.D., Draheim S.E., Hartley L.W., Jones N.D., Mihelich E.D.,
RA Olkowski J.L., Snyder D.W., Dand S.C., Wery J.-P.;
RT "Structure-based design of the first potent and selective inhibitor of
RT human non-pancreatic secretory phospholipase A2.";
RL Nat. Struct. Biol. 2:458-465(1995).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=9538252; DOI=10.1093/oxfordjournals.jbchem.a021982;
RA Kitadokoro K., Hagishita S., Sato T., Ohtan M., Miki K.;
RT "Crystal structure of human secretory phospholipase A2-IIA complex with the
RT potent indolizine inhibitor 120-1032.";
RL J. Biochem. 123:619-623(1998).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids with implications in host
CC antimicrobial defense, inflammatory response and tissue regeneration
CC (PubMed:10455175, PubMed:10681567, PubMed:2925633). Hydrolyzes the
CC ester bond of the fatty acyl group attached at sn-2 position of
CC phospholipids (phospholipase A2 activity) with preference for
CC phosphatidylethanolamines and phosphatidylglycerols over
CC phosphatidylcholines (PubMed:10455175, PubMed:10681567). Contributes to
CC 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 (PubMed:11694541,
CC PubMed:10358193). Upon sterile inflammation, targets membrane
CC phospholipids of extracellular mitochondria released from activated
CC platelets, generating free unsaturated fatty acids such as arachidonate
CC that is used by neighboring leukocytes to synthesize inflammatory
CC eicosanoids such as leukotrienes. Simultaneously, by compromising
CC mitochondrial membrane integrity, promotes the release in circulation
CC of potent damage-associated molecular pattern molecules that activate
CC the innate immune response (PubMed:25082876). Plays a stem cell
CC regulator role in the intestinal crypt. Within intracellular
CC compartment mediates Paneth cell differentiation and its stem cell
CC supporting functions by inhibiting Wnt signaling pathway in intestinal
CC stem cell (ICS). Secreted in the intestinal lumen upon inflammation,
CC acts in an autocrine way and promotes prostaglandin E2 synthesis that
CC stimulates Wnt signaling pathway in ICS cells and tissue regeneration
CC (By similarity). May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism and inflammation.
CC Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370).
CC Independent of its catalytic activity, acts as a ligand for integrins
CC (PubMed:18635536, PubMed:25398877). Binds to and activates integrins
CC ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 (PubMed:18635536,
CC PubMed:25398877). Binds to a site (site 2) which is distinct from the
CC classical ligand-binding site (site 1) and induces integrin
CC conformational changes and enhanced ligand binding to site 1
CC (PubMed:25398877). Induces cell proliferation in an integrin-dependent
CC manner (PubMed:18635536). {ECO:0000250|UniProtKB:P31482,
CC ECO:0000269|PubMed:10358193, ECO:0000269|PubMed:10455175,
CC ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:11694541,
CC ECO:0000269|PubMed:14998370, ECO:0000269|PubMed:25082876,
CC ECO:0000269|PubMed:2925633}.
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, ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000305|PubMed:10455175, ECO:0000305|PubMed:10681567};
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, ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
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 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, ECO:0000269|PubMed:10681567,
CC ECO:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:10455175, ECO:0000305|PubMed:10681567,
CC ECO:0000305|PubMed:14998370};
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:10358193, ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:10358193, ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000305|PubMed:14998370};
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:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000305|PubMed:10681567};
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:10455175,
CC ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:2925633};
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, ECO:0000269|PubMed:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:10455175, ECO:0000305|PubMed:10681567};
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:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={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:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:10681567};
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:10681567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000305|PubMed:10681567};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:2925633};
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- INTERACTION:
CC PRO_0000022750; P05106: ITGB3; NbExp=3; IntAct=EBI-16414951, EBI-702847;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2925608,
CC ECO:0000269|PubMed:2925633}. Cell membrane
CC {ECO:0000269|PubMed:2775276}; Peripheral membrane protein
CC {ECO:0000305}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:25082876}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in various tissues including heart,
CC kidney, liver, lung, pancreas, placenta, skeletal muscle, prostate,
CC ovary, colon and small intestine. Not detected in lymphoid organs and
CC brain (PubMed:10455175, PubMed:10681567). Expressed in platelets (at
CC protein level) (PubMed:25082876). {ECO:0000269|PubMed:10455175,
CC ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:25082876}.
CC -!- MISCELLANEOUS: Group II phospholipase A2 is found in many cells and
CC also extracellularly. The membrane-bound and secreted forms are
CC identical and are encoded by a single gene.
CC -!- MISCELLANEOUS: Interaction with integrin ITGA4:ITGB3 is inhibited by a
CC number of synthetic peptides including R-Ala-Trp-Asp-Ile and R-Gly-Arg-
CC Gly-Asp-Asp-Asp which bind to PLA2G2A and disrupt its integrin-binding
CC activity. {ECO:0000269|PubMed:23164706}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pla2g2a/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLA2G2AID41730ch1p36.html";
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DR EMBL; M22430; AAA36550.1; -; mRNA.
DR EMBL; M22431; AAA36549.1; -; Genomic_DNA.
DR EMBL; AY656695; AAT73043.1; -; mRNA.
DR EMBL; CR456865; CAG33146.1; -; mRNA.
DR EMBL; AY462114; AAR16084.1; -; Genomic_DNA.
DR EMBL; AL358253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK291302; BAF83991.1; -; mRNA.
DR EMBL; CH471134; EAW94907.1; -; Genomic_DNA.
DR EMBL; BC005919; AAH05919.1; -; mRNA.
DR CCDS; CCDS201.1; -.
DR PIR; A32862; PSHUYF.
DR RefSeq; NP_000291.1; NM_000300.3.
DR RefSeq; NP_001155199.1; NM_001161727.1.
DR RefSeq; NP_001155200.1; NM_001161728.1.
DR RefSeq; NP_001155201.1; NM_001161729.1.
DR PDB; 1AYP; X-ray; 2.57 A; A/B/C/D/E/F=21-144.
DR PDB; 1BBC; X-ray; 2.20 A; A=21-144.
DR PDB; 1DB4; X-ray; 2.20 A; A=21-144.
DR PDB; 1DB5; X-ray; 2.80 A; A=21-144.
DR PDB; 1DCY; X-ray; 2.70 A; A=21-144.
DR PDB; 1J1A; X-ray; 2.20 A; A/B=21-144.
DR PDB; 1KQU; X-ray; 2.10 A; A=21-144.
DR PDB; 1KVO; X-ray; 2.00 A; A/B/C/D/E/F=21-144.
DR PDB; 1N28; X-ray; 1.50 A; A/B=21-144.
DR PDB; 1N29; X-ray; 2.60 A; A=21-144.
DR PDB; 1POD; X-ray; 2.10 A; A=21-144.
DR PDB; 1POE; X-ray; 2.10 A; A/B=21-144.
DR PDB; 3U8B; X-ray; 2.30 A; A=21-144.
DR PDB; 3U8D; X-ray; 1.80 A; A/B=21-144.
DR PDB; 3U8H; X-ray; 2.30 A; A/B=21-144.
DR PDB; 3U8I; X-ray; 1.10 A; A/B=21-144.
DR PDB; 5G3N; X-ray; 1.80 A; A/B=21-144.
DR PDBsum; 1AYP; -.
DR PDBsum; 1BBC; -.
DR PDBsum; 1DB4; -.
DR PDBsum; 1DB5; -.
DR PDBsum; 1DCY; -.
DR PDBsum; 1J1A; -.
DR PDBsum; 1KQU; -.
DR PDBsum; 1KVO; -.
DR PDBsum; 1N28; -.
DR PDBsum; 1N29; -.
DR PDBsum; 1POD; -.
DR PDBsum; 1POE; -.
DR PDBsum; 3U8B; -.
DR PDBsum; 3U8D; -.
DR PDBsum; 3U8H; -.
DR PDBsum; 3U8I; -.
DR PDBsum; 5G3N; -.
DR AlphaFoldDB; P14555; -.
DR SMR; P14555; -.
DR BioGRID; 111337; 29.
DR IntAct; P14555; 6.
DR MINT; P14555; -.
DR STRING; 9606.ENSP00000383364; -.
DR BindingDB; P14555; -.
DR ChEMBL; CHEMBL3474; -.
DR DrugBank; DB03121; (1-Benzyl-5-methoxy-2-methyl-1H-indol-3-yl)acetic acid.
DR DrugBank; DB04112; (2R)-2-Acetamido-3-(octadecyloxy)propyl 2-(methylsulfanyl)ethyl hydrogen phosphate.
DR DrugBank; DB01955; 1,4-Butanediol.
DR DrugBank; DB02080; 1-{2-[2-(2-Methoxyethoxy)Ethoxy]Ethoxy}-4-(1,1,3,3-Tetramethylbutyl)Benzene.
DR DrugBank; DB02936; 4-(1-Benzyl-3-Carbamoylmethyl-2-Methyl-1h-Indol-5-Yloxy)-Butyric Acid.
DR DrugBank; DB03471; 6-phenyl-4(R)-(7-phenyl-heptanoylamino)-hexanoic acid.
DR DrugBank; DB02504; [3-(1-Benzyl-3-Carbamoylmethyl-2-Methyl-1h-Indol-5-Yloxy)-Propyl-]-Phosphonic Acid.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB03784; Elaidamide.
DR DrugBank; DB01381; Ginkgo biloba.
DR DrugBank; DB00328; Indomethacin.
DR DrugBank; DB04287; KH064.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB02448; N-Tridecanoic Acid.
DR DrugBank; DB04786; Suramin.
DR DrugBank; DB05737; Varespladib methyl.
DR GuidetoPHARMACOLOGY; 1417; -.
DR SwissLipids; SLP:000000653; -.
DR iPTMnet; P14555; -.
DR PhosphoSitePlus; P14555; -.
DR BioMuta; PLA2G2A; -.
DR DMDM; 129483; -.
DR jPOST; P14555; -.
DR MassIVE; P14555; -.
DR PaxDb; P14555; -.
DR PeptideAtlas; P14555; -.
DR PRIDE; P14555; -.
DR ProteomicsDB; 53059; -.
DR Antibodypedia; 29745; 250 antibodies from 29 providers.
DR DNASU; 5320; -.
DR Ensembl; ENST00000375111.7; ENSP00000364252.3; ENSG00000188257.12.
DR Ensembl; ENST00000400520.8; ENSP00000383364.3; ENSG00000188257.12.
DR Ensembl; ENST00000482011.2; ENSP00000504762.1; ENSG00000188257.12.
DR GeneID; 5320; -.
DR KEGG; hsa:5320; -.
DR MANE-Select; ENST00000482011.3; ENSP00000504762.1; NM_001395463.1; NP_001382392.1.
DR UCSC; uc001bcv.4; human.
DR CTD; 5320; -.
DR DisGeNET; 5320; -.
DR GeneCards; PLA2G2A; -.
DR HGNC; HGNC:9031; PLA2G2A.
DR HPA; ENSG00000188257; Group enriched (adipose tissue, intestine, placenta, urinary bladder).
DR MalaCards; PLA2G2A; -.
DR MIM; 172411; gene.
DR neXtProt; NX_P14555; -.
DR OpenTargets; ENSG00000188257; -.
DR PharmGKB; PA270; -.
DR VEuPathDB; HostDB:ENSG00000188257; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000155096; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; P14555; -.
DR OMA; CQCDKAA; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P14555; -.
DR TreeFam; TF319283; -.
DR BRENDA; 3.1.1.4; 2681.
DR PathwayCommons; P14555; -.
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 Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SABIO-RK; P14555; -.
DR SignaLink; P14555; -.
DR BioGRID-ORCS; 5320; 6 hits in 1067 CRISPR screens.
DR ChiTaRS; PLA2G2A; human.
DR EvolutionaryTrace; P14555; -.
DR GeneWiki; PLA2G2A; -.
DR GenomeRNAi; 5320; -.
DR Pharos; P14555; Tchem.
DR PRO; PR:P14555; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P14555; protein.
DR Bgee; ENSG00000188257; Expressed in palpebral conjunctiva and 147 other tissues.
DR ExpressionAtlas; P14555; baseline and differential.
DR Genevisible; P14555; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
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:0004623; F:phospholipase A2 activity; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; TAS:BHF-UCL.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:CACAO.
DR GO; GO:0050729; P:positive regulation of inflammatory response; TAS:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL.
DR GO; GO:1902563; P:regulation of neutrophil activation; IDA: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 3D-structure; Antimicrobial; Bacteriolytic enzyme; Calcium; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Hydrolase;
KW Inflammatory response; Lipid metabolism; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2775276,
FT ECO:0000269|PubMed:2925633, ECO:0000269|PubMed:3202859,
FT ECO:0000269|PubMed:3240982, ECO:0000269|PubMed:8399335"
FT CHAIN 21..144
FT /note="Phospholipase A2, membrane associated"
FT /id="PRO_0000022750"
FT ACT_SITE 67
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:7664108, ECO:0000312|PDB:1DB4,
FT ECO:0000312|PDB:1DB5, ECO:0000312|PDB:1DCY,
FT ECO:0000312|PDB:1POE"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:7664108, ECO:0000312|PDB:1DB4,
FT ECO:0000312|PDB:1DB5, ECO:0000312|PDB:1DCY,
FT ECO:0000312|PDB:1POE"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:7664108, ECO:0000312|PDB:1DB4,
FT ECO:0000312|PDB:1DB5, ECO:0000312|PDB:1DCY,
FT ECO:0000312|PDB:1POE"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:7664108, ECO:0000312|PDB:1DB4,
FT ECO:0000312|PDB:1DB5, ECO:0000312|PDB:1DCY,
FT ECO:0000312|PDB:1POE"
FT SITE 94
FT /note="Important for integrin binding"
FT /evidence="ECO:0000269|PubMed:18635536"
FT SITE 120
FT /note="Important for integrin binding"
FT /evidence="ECO:0000269|PubMed:18635536"
FT DISULFID 46..137
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 48..64
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 63..117
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 69..144
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 70..110
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 79..103
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT DISULFID 97..108
FT /evidence="ECO:0000269|PubMed:1948070,
FT ECO:0000269|PubMed:2062381, ECO:0000269|PubMed:7664108,
FT ECO:0000269|PubMed:9538252, ECO:0000312|PDB:1BBC,
FT ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5,
FT ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POD,
FT ECO:0000312|PDB:1POE"
FT VARIANT 19
FT /note="H -> Y (in dbSNP:rs11573162)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018953"
FT MUTAGEN 27
FT /note="R->E: Reduces bactericidal activity to 20% against
FT B. subtilis and to 4% against S. aureus. Complete loss of
FT bactericidal activity; when associated with E-30 and E-35."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 30
FT /note="K->E: Complete loss of bactericidal activity; when
FT associated with E-27 and E-35."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 35
FT /note="K->E: Complete loss of bactericidal activity; when
FT associated with E-27 and E-30."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 49
FT /note="G->S: No effect on integrin binding; when associated
FT with K-68."
FT /evidence="ECO:0000269|PubMed:25398877"
FT MUTAGEN 57
FT /note="K->E: Impairs bactericidal activity; when associated
FT with E-128."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 62
FT /note="R->E: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:18635536"
FT MUTAGEN 67
FT /note="H->Q: Catalytically inactive but does not affect
FT integrin binding. Impairs leukotriene B4 synthesis in
FT activated neutrophils."
FT /evidence="ECO:0000269|PubMed:18635536,
FT ECO:0000269|PubMed:25082876, ECO:0000269|PubMed:25398877"
FT MUTAGEN 68
FT /note="D->K: No effect on integrin binding; when associated
FT with S-49."
FT /evidence="ECO:0000269|PubMed:25398877"
FT MUTAGEN 72
FT /note="K->E: Impairs bactericidal activity; when associated
FT with E-73 and E-77."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 73
FT /note="R->E: Impairs bactericidal activity; when associated
FT with E-72 and E-77."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 73
FT /note="R->E: Slightly reduced integrin binding."
FT /evidence="ECO:0000269|PubMed:18635536"
FT MUTAGEN 77
FT /note="R->E: Impairs bactericidal activity; when associated
FT with E-72 and E-73."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 87
FT /note="K->E: Reduces bactericidal activity to 20% against
FT B. subtilis and to 10% against S. aureus. Complete loss of
FT bactericidal activity; when associated with E-99 and E-
FT 104."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 94
FT /note="R->E: Moderately reduced integrin binding. Greatly
FT reduced integrin binding but no effect on catalytic
FT activity; when associated with E-120."
FT /evidence="ECO:0000269|PubMed:18635536,
FT ECO:0000269|PubMed:25398877"
FT MUTAGEN 99
FT /note="K->E: Reduces bactericidal activity to 25% against
FT B. subtilis and to 10% against S. aureus. Complete loss of
FT bactericidal activity; when associated with E-87 and E-
FT 104."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 104
FT /note="R->E: Reduces bactericidal activity to 18% against
FT B. subtilis and to 12% against S. aureus. Complete loss of
FT bactericidal activity; when associated with E-87 and E-99."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 120
FT /note="R->E: Moderately reduced integrin binding. Greatly
FT reduced integrin binding but no effect on catalytic
FT activity; when associated with E-94."
FT /evidence="ECO:0000269|PubMed:18635536,
FT ECO:0000269|PubMed:25398877"
FT MUTAGEN 122
FT /note="K->E: Impairs bactericidal activity; when associated
FT with E-127."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 127
FT /note="K->E: Impairs bactericidal activity; when associated
FT with E-122."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 128
FT /note="K->E: Impairs bactericidal activity; when associated
FT with E-57."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 135
FT /note="K->E: Impairs bactericidal activity; when associated
FT with D-138."
FT /evidence="ECO:0000269|PubMed:11694541"
FT MUTAGEN 138
FT /note="R->D: Impairs bactericidal activity; when associated
FT with E-135."
FT /evidence="ECO:0000269|PubMed:11694541"
FT CONFLICT 12
FT /note="I -> Y (in Ref. 4; AAT73043)"
FT /evidence="ECO:0000305"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3U8I"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3U8I"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3U8I"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:3U8I"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1POE"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3U8I"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3U8I"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3U8I"
SQ SEQUENCE 144 AA; 16083 MW; 923C5FA0C6979CDA CRC64;
MKTLLLLAVI MIFGLLQAHG NLVNFHRMIK LTTGKEAALS YGFYGCHCGV GGRGSPKDAT
DRCCVTHDCC YKRLEKRGCG TKFLSYKFSN SGSRITCAKQ DSCRSQLCEC DKAAATCFAR
NKTTYNKKYQ YYSNKHCRGS TPRC
