ID   PA24B_HUMAN             Reviewed;         781 AA.
AC   P0C869; B4DRT9; O95712; Q19KD5; Q19KD6; Q59GF9; Q8TB10; Q9UKV7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Cytosolic phospholipase A2 beta {ECO:0000303|PubMed:16617059};
DE            Short=cPLA2-beta {ECO:0000303|PubMed:16617059};
DE            EC=3.1.1.4 {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059};
DE   AltName: Full=Lysophospholipase A1 group IVB {ECO:0000305|PubMed:16617059};
DE            EC=3.1.1.5 {ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059};
DE   AltName: Full=Phospholipase A2 group IVB;
GN   Name=PLA2G4B;
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 5), FUNCTION (ISOFORM 5), CATALYTIC
RP   ACTIVITY (ISOFORM 5), ACTIVITY REGULATION (ISOFORM 5), TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF SER-335; HIS-417; ASP-615 AND ARG-632.
RX   PubMed=10085124; DOI=10.1074/jbc.274.13.8823;
RA   Pickard R.T., Strifler B.A., Kramer R.M., Sharp J.D.;
RT   "Molecular cloning of two new human paralogs of 85-kDa cytosolic
RT   phospholipase A2.";
RL   J. Biol. Chem. 274:8823-8831(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION (ISOFORM 5), CATALYTIC
RP   ACTIVITY (ISOFORM 5), ACTIVITY REGULATION (ISOFORM 5), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10358058; DOI=10.1074/jbc.274.24.17063;
RA   Song C., Chang X.J., Bean K.M., Proia M.S., Knopf J.L., Kriz R.W.;
RT   "Molecular characterization of cytosolic phospholipase A2-beta.";
RL   J. Biol. Chem. 274:17063-17067(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORMS 3 AND 5),
RP   CATALYTIC ACTIVITY (ISOFORMS 3 AND 5), BIOPHYSICOCHEMICAL PROPERTIES
RP   (ISOFORMS 3 AND 5), SUBCELLULAR LOCATION (ISOFORMS 3 AND 5), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16617059; DOI=10.1074/jbc.m601770200;
RA   Ghosh M., Loper R., Gelb M.H., Leslie C.C.;
RT   "Identification of the expressed form of human cytosolic phospholipase
RT   A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria
RT   and early endosomes.";
RL   J. Biol. Chem. 281:16615-16624(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-191.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
CC   -!- FUNCTION: Calcium-dependent phospholipase A1 and A2 and
CC       lysophospholipase that may play a role in membrane phospholipid
CC       remodeling. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC       ECO:0000269|PubMed:16617059}.
CC   -!- FUNCTION: [Isoform 3]: Calcium-dependent phospholipase A2 and
CC       lysophospholipase. Cleaves the ester bond of the fatty acyl group
CC       attached to the sn-2 position of phosphatidylethanolamines, producing
CC       lysophospholipids that may be used in deacylation-reacylation cycles.
CC       Hydrolyzes lysophosphatidylcholines with low efficiency but is
CC       inefficient toward phosphatidylcholines. {ECO:0000269|PubMed:16617059}.
CC   -!- FUNCTION: [Isoform 5]: Calcium-dependent phospholipase A1 and A2 and
CC       lysophospholipase. Cleaves the ester bond of the fatty acyl group
CC       attached to the sn-1 or sn-2 position of diacyl phospholipids
CC       (phospholipase A1 and A2 activity, respectively), producing
CC       lysophospholipids that may be used in deacylation-reacylation cycles.
CC       Can further hydrolyze lysophospholipids enabling complete deacylation.
CC       Has no activity toward alkylacyl phospholipids.
CC       {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC       ECO:0000269|PubMed:16617059}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
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:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC         ECO:0000269|PubMed:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:10085124, ECO:0000305|PubMed:10358058,
CC         ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC         Evidence={ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
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:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000305|PubMed:10085124, ECO:0000305|PubMed:10358058};
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:16617059};
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC         glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC         Evidence={ECO:0000269|PubMed:10358058};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC         Evidence={ECO:0000305|PubMed:10358058};
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
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:10358058, ECO:0000269|PubMed:16617059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC         Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:16617059};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00041};
CC   -!- ACTIVITY REGULATION: [Isoform 5]: Stimulated by cytosolic Ca(2+).
CC       {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 3]:
CC       Kinetic parameters:
CC         Note=The specific activity is 0.8 nmol/min/ug enzyme with
CC         1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine
CC         as substrate. The specific activity is 0.3 nmol/min/ug enzyme with
CC         1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine
CC         as substrate. The specific activity is 1.6 nmol/min/ug enzyme with
CC         1-hexadecanoyl-sn-glycero-3-phosphocholine as substrate.
CC         {ECO:0000269|PubMed:16617059};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 5]:
CC       Kinetic parameters:
CC         Note=The specific activity is 2.1 nmol/min/ug enzyme with
CC         1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC         as substrate. The specific activity is 0.6 nmol/min/ug enzyme with
CC         1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine
CC         as substrate. The specific activity is 140 nmol/min/ug enzyme with
CC         1-hexadecanoyl-sn-glycero-3-phosphocholine as substrate.
CC         {ECO:0000269|PubMed:16617059};
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:16617059}. Mitochondrion membrane
CC       {ECO:0000269|PubMed:16617059}; Peripheral membrane protein. Early
CC       endosome membrane {ECO:0000269|PubMed:16617059}; Peripheral membrane
CC       protein. Note=Translocates to membrane vesicles in a calcium-dependent
CC       fashion. {ECO:0000269|PubMed:16617059}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:16617059}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P0C869-1, O95712-1; Sequence=Displayed;
CC       Name=2; Synonyms=beta2;
CC         IsoId=P0C869-7; Sequence=VSP_039387, VSP_039389, VSP_039390;
CC       Name=3; Synonyms=beta3;
CC         IsoId=P0C869-8; Sequence=VSP_039387, VSP_039388;
CC       Name=4;
CC         IsoId=P0C869-4, O95712-4; Sequence=VSP_019871;
CC       Name=5; Synonyms=Beta1;
CC         IsoId=P0C869-6; Sequence=VSP_039387;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain, heart, liver, cerebellum and pancreas.
CC       {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058,
CC       ECO:0000269|PubMed:16617059}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. It modulates enzyme activity by presenting the active
CC       site to its substrate in response to elevations of cytosolic Ca(2+) (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Based on a naturally occurring readthrough
CC       transcript which produces a JMJD7-PLA2G4B fusion protein.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Based on a naturally occurring readthrough
CC       transcript which produces a JMJD7-PLA2G4B fusion protein.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: Based on a naturally occurring readthrough
CC       transcript which produces a JMJD7-PLA2G4B fusion protein.
CC       {ECO:0000305}.
CC   -!- CAUTION: Most tissues also express read-through transcripts from this
CC       gene into the upstream gene (JMJD7), some of which may encode fusion
CC       proteins. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92387.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF065215; AAC78836.1; -; mRNA.
DR   EMBL; AF121908; AAD32135.1; -; mRNA.
DR   EMBL; DQ523799; ABF69195.1; -; mRNA.
DR   EMBL; DQ523800; ABF69196.1; -; mRNA.
DR   EMBL; AK299419; BAG61401.1; -; mRNA.
DR   EMBL; AB209150; BAD92387.1; ALT_INIT; mRNA.
DR   EMBL; AC020659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS45241.1; -.
DR   RefSeq; NP_001108105.1; NM_001114633.1. [P0C869-1]
DR   RefSeq; NP_001185517.1; NM_001198588.1. [P0C869-7]
DR   RefSeq; NP_005081.1; NM_005090.3. [P0C869-6]
DR   AlphaFoldDB; P0C869; -.
DR   SMR; P0C869; -.
DR   BioGRID; 114229; 33.
DR   BioGRID; 936685; 9.
DR   IntAct; P0C869; 6.
DR   STRING; 9606.ENSP00000396045; -.
DR   BindingDB; P0C869; -.
DR   ChEMBL; CHEMBL4136; -.
DR   SwissLipids; SLP:000000616; -. [P0C869-8]
DR   SwissLipids; SLP:000000617; -. [P0C869-6]
DR   iPTMnet; P0C869; -.
DR   PhosphoSitePlus; P0C869; -.
DR   BioMuta; PLA2G4B; -.
DR   DMDM; 300669659; -.
DR   EPD; P0C869; -.
DR   jPOST; P0C869; -.
DR   MassIVE; P0C869; -.
DR   MaxQB; P0C869; -.
DR   PaxDb; 9606-ENSP00000396045; -.
DR   PeptideAtlas; P0C869; -.
DR   ProteomicsDB; 52403; -.
DR   ProteomicsDB; 52404; -. [P0C869-4]
DR   ProteomicsDB; 52405; -. [P0C869-6]
DR   ProteomicsDB; 52406; -. [P0C869-7]
DR   ProteomicsDB; 52407; -. [P0C869-8]
DR   Antibodypedia; 70595; 123 antibodies from 16 providers.
DR   DNASU; 8681; -.
DR   Ensembl; ENST00000452633.5; ENSP00000396045.1; ENSG00000243708.11. [P0C869-1]
DR   Ensembl; ENST00000458483.4; ENSP00000416610.1; ENSG00000243708.11. [P0C869-1]
DR   GeneID; 100137049; -.
DR   GeneID; 8681; -.
DR   KEGG; hsa:100137049; -.
DR   KEGG; hsa:8681; -.
DR   MANE-Select; ENST00000458483.4; ENSP00000416610.1; NM_001114633.2; NP_001108105.1.
DR   UCSC; uc010bco.4; human.
DR   AGR; HGNC:34449; -.
DR   AGR; HGNC:9036; -.
DR   CTD; 100137049; -.
DR   CTD; 8681; -.
DR   DisGeNET; 100137049; -.
DR   DisGeNET; 8681; -.
DR   GeneCards; PLA2G4B; -.
DR   HGNC; HGNC:9036; PLA2G4B.
DR   HPA; ENSG00000243708; Low tissue specificity.
DR   MIM; 606088; gene.
DR   neXtProt; NX_P0C869; -.
DR   OpenTargets; ENSG00000168970; -.
DR   OpenTargets; ENSG00000243708; -.
DR   PharmGKB; PA165479070; -.
DR   VEuPathDB; HostDB:ENSG00000243708; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   GeneTree; ENSGT01030000234606; -.
DR   HOGENOM; CLU_011663_0_0_1; -.
DR   InParanoid; P0C869; -.
DR   OMA; ECHAFSD; -.
DR   OrthoDB; 4250045at2759; -.
DR   PhylomeDB; P0C869; -.
DR   TreeFam; TF325228; -.
DR   PathwayCommons; P0C869; -.
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-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR   SignaLink; P0C869; -.
DR   BioGRID-ORCS; 100137049; 31 hits in 1113 CRISPR screens.
DR   BioGRID-ORCS; 8681; 12 hits in 977 CRISPR screens.
DR   GeneWiki; PLA2G4B; -.
DR   Pharos; P0C869; Tchem.
DR   PRO; PR:P0C869; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P0C869; Protein.
DR   Bgee; ENSG00000243708; Expressed in lower esophagus mucosa and 94 other cell types or tissues.
DR   ExpressionAtlas; P0C869; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
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:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR   GO; GO:0004623; F:phospholipase A2 activity; TAS:Reactome.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; NAS:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR   GO; GO:0007567; P:parturition; NAS:UniProtKB.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR   GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR   GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   CDD; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF32; CYTOSOLIC PHOSPHOLIPASE A2 BETA; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
DR   Genevisible; P0C869; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cytoplasm; Endosome; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW   Mitochondrion; Reference proteome.
FT   CHAIN           1..781
FT                   /note="Cytosolic phospholipase A2 beta"
FT                   /id="PRO_0000247021"
FT   DOMAIN          1..112
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          246..781
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        615
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   VAR_SEQ         1..299
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_019871"
FT   VAR_SEQ         1..3
FT                   /note="MAV -> MAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDW
FT                   VCPNRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDRFMMPAE
FT                   RRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLESHVPWASEALGKMPDA
FT                   VNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFHPPSDRPFIPYELYTPATYQLTEEG
FT                   TFKVVDEEAMEK (in isoform 2, isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10085124,
FT                   ECO:0000303|PubMed:10358058, ECO:0000303|PubMed:16617059"
FT                   /id="VSP_039387"
FT   VAR_SEQ         641..765
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16617059"
FT                   /id="VSP_039388"
FT   VAR_SEQ         650..662
FT                   /note="QLQLLGRFCQEQG -> GSGGHPRRRQLGR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16617059"
FT                   /id="VSP_039389"
FT   VAR_SEQ         663..781
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16617059"
FT                   /id="VSP_039390"
FT   VARIANT         191
FT                   /note="R -> C (in dbSNP:rs3816533)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_027047"
FT   VARIANT         239
FT                   /note="M -> I (in dbSNP:rs2290552)"
FT                   /id="VAR_027048"
FT   VARIANT         391
FT                   /note="R -> H (in dbSNP:rs34807597)"
FT                   /id="VAR_034365"
FT   VARIANT         591
FT                   /note="T -> I (in dbSNP:rs36126315)"
FT                   /id="VAR_060082"
FT   MUTAGEN         335
FT                   /note="S->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:10085124"
FT   MUTAGEN         417
FT                   /note="H->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10085124"
FT   MUTAGEN         615
FT                   /note="D->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:10085124"
FT   MUTAGEN         632
FT                   /note="R->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:10085124"
FT   CONFLICT        138
FT                   /note="L -> F (in Ref. 2; AAD32135)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="Q -> P (in Ref. 3; ABF69195/ABF69196)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="A -> V (in Ref. 3; ABF69195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="S -> P (in Ref. 3; ABF69195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="R -> C (in Ref. 4; BAG61401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723
FT                   /note="G -> E (in Ref. 4; BAG61401)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   781 AA;  87978 MW;  4C5C6861E7BAB1B8 CRC64;
     MAVAEVSRTC LLTVRVLQAH RLPSKDLVTP SDCYVTLWLP TACSHRLQTR TVKNSSSPVW
     NQSFHFRIHR QLKNVMELKV FDQDLVTGDD PVLSVLFDAG TLRAGEFRRE SFSLSPQGEG
     RLEVEFRLQS LADRGEWLVS NGVLVARELS CLHVQLEETG DQKSSEHRVQ LVVPGSCEGP
     QEASVGTGTF RFHCPACWEQ ELSIRLQDAP EEQLKAPLSA LPSGQVVRLV FPTSQEPLMR
     VELKKEAGLR ELAVRLGFGP CAEEQAFLSR RKQVVAAALR QALQLDGDLQ EDEIPVVAIM
     ATGGGIRAMT SLYGQLAGLK ELGLLDCVSY ITGASGSTWA LANLYEDPEW SQKDLAGPTE
     LLKTQVTKNK LGVLAPSQLQ RYRQELAERA RLGYPSCFTN LWALINEALL HDEPHDHKLS
     DQREALSHGQ NPLPIYCALN TKGQSLTTFE FGEWCEFSPY EVGFPKYGAF IPSELFGSEF
     FMGQLMKRLP ESRICFLEGI WSNLYAANLQ DSLYWASEPS QFWDRWVRNQ ANLDKEQVPL
     LKIEEPPSTA GRIAEFFTDL LTWRPLAQAT HNFLRGLHFH KDYFQHPHFS TWKATTLDGL
     PNQLTPSEPH LCLLDVGYLI NTSCLPLLQP TRDVDLILSL DYNLHGAFQQ LQLLGRFCQE
     QGIPFPPISP SPEEQLQPRE CHTFSDPTCP GAPAVLHFPL VSDSFREYSA PGVRRTPEEA
     AAGEVNLSSS DSPYHYTKVT YSQEDVDKLL HLTHYNVCNN QEQLLEALRQ AVQRRRQRRP
     H
//