PA24B_HUMAN
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 03-AUG-2022, entry version 114.
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;
CC Evidence={ECO:0000255|PROSITE-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 1-
CC hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphoethanolamine as substrate. The specific activity is 0.3
CC nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine as substrate. The specific activity is
CC 1.6 nmol/min/ug enzyme with 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine as substrate. {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 1-
CC hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphocholine as substrate. The specific activity is 0.6 nmol/min/ug
CC enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphoethanolamine as substrate. The specific activity is
CC 140 nmol/min/ug enzyme with 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine as substrate. {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;
CC 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;
CC 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; 32.
DR BioGRID; 936685; 6.
DR IntAct; P0C869; 5.
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; P0C869; -.
DR PeptideAtlas; P0C869; -.
DR PRIDE; 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; 75 antibodies from 15 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 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; YFSTWKA; -.
DR OrthoDB; 302848at2759; -.
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; 30 hits in 1035 CRISPR screens.
DR BioGRID-ORCS; 8681; 12 hits in 931 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 92 other tissues.
DR ExpressionAtlas; P0C869; baseline and differential.
DR Genevisible; P0C869; HS.
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; IBA:GO_Central.
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 Gene3D; 2.60.40.150; -; 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 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; SSF49562; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51210; PLA2C; 1.
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
