PA21B_HUMAN
ID PA21B_HUMAN Reviewed; 148 AA.
AC P04054; B2R4H5; Q3KPI1;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:17603006};
DE AltName: Full=Group IB phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Precursor;
GN Name=PLA2G1B; Synonyms=PLA2, PLA2A, PPLA2;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RX PubMed=3028739; DOI=10.1089/dna.1.1986.5.519;
RA Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.;
RT "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from
RT porcine pancreas and human lung.";
RL DNA 5:519-527(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PROTEIN SEQUENCE OF 16-22.
RC TISSUE=Pancreas;
RX PubMed=7060561; DOI=10.1111/j.1432-1033.1982.tb05855.x;
RA Grataroli R., Dijkman R., Dutilh C.E., van der Ouderaa F., de Haas G.H.,
RA Figarella C.;
RT "Studies on prophospholipase A2 and its enzyme from human pancreatic juice.
RT Catalytic properties and sequence of the N-terminal region.";
RL Eur. J. Biochem. 122:111-117(1982).
RN [8]
RP PROTEIN SEQUENCE OF 23-148, AND PROTEOLYTIC CLEAVAGE.
RC TISSUE=Pancreas;
RX PubMed=6349696; DOI=10.1016/0167-4838(83)90126-7;
RA Verheij H.M., Westerman J., Sternby B., de Haas G.H.;
RT "The complete primary structure of phospholipase A2 from human pancreas.";
RL Biochim. Biophys. Acta 747:93-99(1983).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1420353; DOI=10.1016/0167-4781(92)90133-k;
RA Kanda A., Tamaki M., Nakamura E., Teraoka H., Yoshida N.;
RT "Characterization of recombinant human and rat pancreatic phospholipases A2
RT secreted from Saccharomyces cerevisiae: difference in proteolytic
RT processing.";
RL Biochim. Biophys. Acta 1171:1-10(1992).
RN [10]
RP FUNCTION, AND INTERACTION WITH PLA2R1.
RX PubMed=7721806; DOI=10.1074/jbc.270.15.8963;
RA Ancian P., Lambeau G., Mattei M.-G., Lazdunski M.;
RT "The human 180-kDa receptor for secretory phospholipases A2. Molecular
RT cloning, identification of a secreted soluble form, expression, and
RT chromosomal localization.";
RL J. Biol. Chem. 270:8963-8970(1995).
RN [11]
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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=17603006; DOI=10.1016/j.bbamem.2007.05.019;
RA Yu B.Z., Apitz-Castro R.J., Jain M.K., Berg O.G.;
RT "Role of 57-72 loop in the allosteric action of bile salts on pancreatic IB
RT phospholipase A(2): regulation of fat and cholesterol homeostasis.";
RL Biochim. Biophys. Acta 1768:2478-2490(2007).
RN [13]
RP FUNCTION.
RX PubMed=25335547; DOI=10.1038/srep06660;
RA Pan Y., Wan J., Liu Y., Yang Q., Liang W., Singhal P.C., Saleem M.A.,
RA Ding G.;
RT "sPLA2 IB induces human podocyte apoptosis via the M-type phospholipase A2
RT receptor.";
RL Sci. Rep. 4:6660-6660(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 16-148, DISULFIDE BONDS, SUBUNIT,
RP AUTOPROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=19297324; DOI=10.1074/jbc.m808029200;
RA Xu W., Yi L., Feng Y., Chen L., Liu J.;
RT "Structural insight into the activation mechanism of human pancreatic
RT prophospholipase A2.";
RL J. Biol. Chem. 284:16659-16666(2009).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets dietary phospholipids in the intestinal tract (PubMed:1420353,
CC PubMed:10681567, PubMed:17603006). 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 (PubMed:1420353, PubMed:10681567,
CC PubMed:17603006). May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism and inflammation in the
CC intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (By similarity).
CC May act in an autocrine and paracrine manner (PubMed:7721806,
CC PubMed:25335547). Upon binding to the PLA2R1 receptor can regulate
CC podocyte survival and glomerular homeostasis (PubMed:25335547). Has
CC anti-helminth activity in a process regulated by gut microbiota. Upon
CC helminth infection of intestinal epithelia, directly affects
CC phosphatidylethanolamine contents in the membrane of helminth larvae,
CC likely controlling an array of phospholipid-mediated cellular processes
CC such as membrane fusion and cell division while providing for better
CC immune recognition, ultimately reducing larvae integrity and
CC infectivity (By similarity). {ECO:0000250|UniProtKB:P04055,
CC ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:10681567,
CC ECO:0000269|PubMed:1420353, ECO:0000269|PubMed:17603006,
CC ECO:0000269|PubMed:25335547, ECO:0000269|PubMed:7721806}.
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:10681567,
CC ECO:0000269|PubMed:17603006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC Evidence={ECO:0000269|PubMed:17603006};
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:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:1420353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000305|PubMed:1420353};
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:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
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:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) +
CC N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00593};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
CC -!- ACTIVITY REGULATION: Regulated by bile acid salts. Up-regulated by
CC cholate and down-regulated by taurochenodeoxycholate. Cholate-activated
CC rate of hydrolysis is lowered by hypolipidemic drug ezetimibe.
CC {ECO:0000269|PubMed:17603006}.
CC -!- SUBUNIT: The inactive pro-form is a homotrimer (PubMed:19297324). When
CC anchored into the cell membrane, the inactive homotrimer is likely
CC cleaved either by trypsin or by itself, producing an active trimer. The
CC resulting conformational changes are thought to open up a center hole
CC forming a channel for substrate entry (PubMed:19297324). Interacts with
CC PLA2R1; this interaction mediates intracellular signaling as well as
CC clearance of extracellular PLA2G1B via endocytotic pathway
CC (PubMed:7721806). {ECO:0000269|PubMed:19297324,
CC ECO:0000269|PubMed:7721806}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19297324}.
CC Note=Secreted from pancreatic acinar cells in its inactive form.
CC -!- TISSUE SPECIFICITY: Selectively expressed in pancreas, lung, liver and
CC kidney. Also detected at lower levels in ovary and testis.
CC {ECO:0000269|PubMed:10681567}.
CC -!- PTM: Activated by trypsin cleavage in the duodenum. Can also be
CC activated by thrombin or autocatalytically.
CC {ECO:0000269|PubMed:19297324, ECO:0000269|PubMed:6349696}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS SNPs;
CC URL="http://egp.gs.washington.edu/data/pla2g1b/";
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DR EMBL; M21056; AAA60107.1; -; Genomic_DNA.
DR EMBL; M22970; AAA60107.1; JOINED; Genomic_DNA.
DR EMBL; M21054; AAA36450.1; -; mRNA.
DR EMBL; AK311830; BAG34772.1; -; mRNA.
DR EMBL; AY438977; AAR05441.1; -; Genomic_DNA.
DR EMBL; AC003982; AAB95635.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW98184.1; -; Genomic_DNA.
DR EMBL; BC106725; AAI06726.1; -; mRNA.
DR EMBL; BC106726; AAI06727.1; -; mRNA.
DR CCDS; CCDS9195.1; -.
DR PIR; C25793; PSHU.
DR RefSeq; NP_000919.1; NM_000928.2.
DR PDB; 3ELO; X-ray; 1.55 A; A=16-148.
DR PDB; 6Q42; X-ray; 1.90 A; A/B=23-148.
DR PDBsum; 3ELO; -.
DR PDBsum; 6Q42; -.
DR AlphaFoldDB; P04054; -.
DR SMR; P04054; -.
DR BioGRID; 111336; 7.
DR IntAct; P04054; 1.
DR STRING; 9606.ENSP00000312286; -.
DR BindingDB; P04054; -.
DR ChEMBL; CHEMBL4426; -.
DR DrugBank; DB07836; 1-DECYL-3-TRIFLUORO ETHYL-SN-GLYCERO-2-PHOSPHOMETHANOL.
DR DrugBank; DB03565; 1-O-Octyl-2-Heptylphosphonyl-Sn-Glycero-3-Phosphoethanolamine.
DR DrugBank; DB00972; Azelastine.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB02938; Heptanoic acid.
DR DrugBank; DB02210; Hexane-1,6-Diol.
DR DrugBank; DB03633; Lpc-Ether.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB02448; N-Tridecanoic Acid.
DR DrugBank; DB04552; Niflumic acid.
DR DrugBank; DB02795; P-Anisic Acid.
DR DrugBank; DB07657; PHOSPHONIC ACID 2-DODECANOYLAMINO-HEXYL ESTER PROPYL ESTER.
DR DrugBank; DB03587; Pyruvaldehyde.
DR DrugBank; DB00795; Sulfasalazine.
DR DrugCentral; P04054; -.
DR GuidetoPHARMACOLOGY; 1416; -.
DR SwissLipids; SLP:000001083; -.
DR BioMuta; PLA2G1B; -.
DR DMDM; 129404; -.
DR MassIVE; P04054; -.
DR PaxDb; P04054; -.
DR PeptideAtlas; P04054; -.
DR PRIDE; P04054; -.
DR ProteomicsDB; 51641; -.
DR Antibodypedia; 31466; 335 antibodies from 39 providers.
DR DNASU; 5319; -.
DR Ensembl; ENST00000308366.9; ENSP00000312286.4; ENSG00000170890.14.
DR GeneID; 5319; -.
DR KEGG; hsa:5319; -.
DR MANE-Select; ENST00000308366.9; ENSP00000312286.4; NM_000928.3; NP_000919.1.
DR UCSC; uc001tyd.3; human.
DR CTD; 5319; -.
DR DisGeNET; 5319; -.
DR GeneCards; PLA2G1B; -.
DR HGNC; HGNC:9030; PLA2G1B.
DR HPA; ENSG00000170890; Tissue enriched (pancreas).
DR MIM; 172410; gene.
DR neXtProt; NX_P04054; -.
DR OpenTargets; ENSG00000170890; -.
DR PharmGKB; PA33361; -.
DR VEuPathDB; HostDB:ENSG00000170890; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000154885; -.
DR InParanoid; P04054; -.
DR OMA; ELDTCCQ; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P04054; -.
DR TreeFam; TF319283; -.
DR BioCyc; MetaCyc:HS10199-MON; -.
DR PathwayCommons; P04054; -.
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; P04054; -.
DR SIGNOR; P04054; -.
DR BioGRID-ORCS; 5319; 40 hits in 1074 CRISPR screens.
DR ChiTaRS; PLA2G1B; human.
DR EvolutionaryTrace; P04054; -.
DR GeneWiki; PLA2G1B; -.
DR GenomeRNAi; 5319; -.
DR Pharos; P04054; Tchem.
DR PRO; PR:P04054; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P04054; protein.
DR Bgee; ENSG00000170890; Expressed in body of pancreas and 103 other tissues.
DR ExpressionAtlas; P04054; baseline and differential.
DR Genevisible; P04054; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
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:0005102; F:signaling receptor binding; IDA:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; TAS:ProtInc.
DR GO; GO:0032431; P:activation of phospholipase A2 activity; TAS:BHF-UCL.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; TAS:BHF-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0016042; P:lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:BHF-UCL.
DR GO; GO:0002446; P:neutrophil mediated immunity; ISS:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR GO; GO:0050778; P:positive regulation of immune response; ISS:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; IDA:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; TAS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0046324; P:regulation of glucose import; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Autocatalytic cleavage; Calcium; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid metabolism; Metal-binding;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:7060561"
FT PROPEP 16..22
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:6349696"
FT /id="PRO_0000022739"
FT CHAIN 23..148
FT /note="Phospholipase A2"
FT /evidence="ECO:0000269|PubMed:3028739"
FT /id="PRO_0000022740"
FT ACT_SITE 70
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT ACT_SITE 121
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 33..99
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 49..146
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 51..67
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 66..127
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 73..120
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 83..113
FT /evidence="ECO:0000269|PubMed:19297324"
FT DISULFID 106..118
FT /evidence="ECO:0000269|PubMed:19297324"
FT VARIANT 16
FT /note="D -> A (in dbSNP:rs5632)"
FT /id="VAR_011911"
FT VARIANT 89
FT /note="N -> K (in dbSNP:rs5636)"
FT /id="VAR_011913"
FT VARIANT 89
FT /note="N -> T (in dbSNP:rs5635)"
FT /id="VAR_011912"
FT CONFLICT 144
FT /note="Missing (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3ELO"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3ELO"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3ELO"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3ELO"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:3ELO"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6Q42"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3ELO"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3ELO"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3ELO"
SQ SEQUENCE 148 AA; 16360 MW; C8E38B2B64AEE8CB CRC64;
MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY CGLGGSGTPV
DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS GSAITCSSKN KECEAFICNC
DRNAAICFSK APYNKAHKNL DTKKYCQS
