PA24B_MOUSE
ID PA24B_MOUSE Reviewed; 782 AA.
AC P0C871; A2AP62; Q4QQM1; Q80VV8; Q91W88;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cytosolic phospholipase A2 beta;
DE Short=cPLA2-beta {ECO:0000303|PubMed:20705608};
DE EC=3.1.1.4 {ECO:0000269|PubMed:20705608};
DE AltName: Full=Lysophospholipase A1 group IVB {ECO:0000305|PubMed:20705608};
DE EC=3.1.1.5 {ECO:0000269|PubMed:20705608};
DE AltName: Full=Phospholipase A2 group IVB;
GN Name=Pla2g4b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-24; HIS-44; ARG-49; LYS-52; LYS-78 AND
RP HIS-82.
RX PubMed=20705608; DOI=10.1074/jbc.m110.165647;
RA Ghomashchi F., Naika G.S., Bollinger J.G., Aloulou A., Lehr M.,
RA Leslie C.C., Gelb M.H.;
RT "Interfacial kinetic and binding properties of mammalian group IVB
RT phospholipase A2 (cPLA2beta) and comparison with the other cPLA2
RT isoforms.";
RL J. Biol. Chem. 285:36100-36111(2010).
CC -!- FUNCTION: Calcium-dependent phospholipase A1 and A2 and
CC lysophospholipase that may play a role in membrane phospholipid
CC remodeling. Cleaves the ester bond of the fatty acyl group attached to
CC the sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2
CC activity, respectively), producing lysophospholipids that may be used
CC in deacylation-reacylation cycles. The PLA1 versus PLA2 activity ratio
CC appears to depend on the phospholipid headgroup, with mainly PLA2
CC activity toward anionic phospholipids such as phosphatidylglycerols.
CC Hydrolyzes with high efficiency lysophospholipids enabling complete
CC deacylation. {ECO:0000269|PubMed:20705608}.
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:0000269|PubMed:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:20705608};
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:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:20705608};
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:0000269|PubMed:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:20705608};
CC -!- CATALYTIC ACTIVITY:
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:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:20705608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753;
CC Evidence={ECO:0000305|PubMed:20705608};
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:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000305|PubMed:20705608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphate +
CC H(+); Xref=Rhea:RHEA:63996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:20705608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63997;
CC Evidence={ECO:0000305|PubMed:20705608};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Activated by cytosolic Ca(2+) in the presence of
CC cardiolipin. Activated by phosphoinositides. Inhibited by electrophilic
CC ketone inhibitors. {ECO:0000269|PubMed:20705608}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=The specific activity is 394 nmol/min/ug enzyme with 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine. The specific PLA2 activity
CC is 11 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine (in the presence of
CC cardiolipin). The specific PLA1 activity is 0.13 nmol/min/ug with 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-phosphatidylcholine. The specific
CC PLA2 activity is 0.04 nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z-
CC octadecenoyl)-phosphatidylethanolamine. The specific PLA2 activity is
CC 0.13 nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z-octadecenoyl)-
CC phosphatidylserine. The specific PLA2 activity is 0.03 with 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-phosphatidylinositol. The specific
CC PLA2 activity is 0.24 with 1-hexadecanoyl-2-(9Z-octadecenoyl)-
CC phosphatidylglycerol. The specific PLA2 activity is 0.25 with 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate.
CC {ECO:0000269|PubMed:20705608};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P0C869}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P0C869}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0C869}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P0C869}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0C869}. Note=Translocates to membrane vesicles
CC in a calcium-dependent fashion. {ECO:0000250|UniProtKB:P0C869}.
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 -!- 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=CAM22684.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL833774; CAM22684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC042758; AAH42758.1; -; mRNA.
DR EMBL; BC098210; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_663353.3; NM_145378.3.
DR AlphaFoldDB; P0C871; -.
DR SMR; P0C871; -.
DR BioGRID; 229231; 1.
DR STRING; 10090.ENSMUSP00000118458; -.
DR iPTMnet; P0C871; -.
DR PhosphoSitePlus; P0C871; -.
DR MaxQB; P0C871; -.
DR PaxDb; P0C871; -.
DR PRIDE; P0C871; -.
DR ProteomicsDB; 295449; -.
DR GeneID; 211429; -.
DR KEGG; mmu:211429; -.
DR UCSC; uc008luz.2; mouse.
DR CTD; 100137049; -.
DR MGI; MGI:2384819; Pla2g4b.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR InParanoid; P0C871; -.
DR OrthoDB; 302848at2759; -.
DR BRENDA; 3.1.1.4; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR PRO; PR:P0C871; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P0C871; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISO:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:MGI.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISO:MGI.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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 Calcium; Cytoplasm; Endosome; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..782
FT /note="Cytosolic phospholipase A2 beta"
FT /id="PRO_0000247022"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 245..782
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 613
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MUTAGEN 24
FT /note="K->N: Impairs calcium-dependent binding to
FT phospholipids; when associated with N-49 and N-52."
FT /evidence="ECO:0000269|PubMed:20705608"
FT MUTAGEN 44
FT /note="H->N: Significantly decreases calcium-dependent
FT binding to phospholipids; when associated with N-82."
FT /evidence="ECO:0000269|PubMed:20705608"
FT MUTAGEN 49
FT /note="R->N: Impairs calcium-dependent binding to
FT phospholipids; when associated with N-24 and N-52."
FT /evidence="ECO:0000269|PubMed:20705608"
FT MUTAGEN 52
FT /note="K->N: Impairs calcium-dependent binding to
FT phospholipids; when associated with N-24 and N-49."
FT /evidence="ECO:0000269|PubMed:20705608"
FT MUTAGEN 78
FT /note="K->N: Significantly decreases calcium-dependent
FT binding to phospholipids."
FT /evidence="ECO:0000269|PubMed:20705608"
FT MUTAGEN 82
FT /note="H->N: Significantly decreases calcium-dependent
FT binding to phospholipids; when associated with N-44."
FT /evidence="ECO:0000269|PubMed:20705608"
FT CONFLICT 75
FT /note="M -> I (in Ref. 2; BC098210)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> A (in Ref. 2; BC098210)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="T -> A (in Ref. 2; AAH42758)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="L -> F (in Ref. 2; AAH42758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 88448 MW; BD803A02439F6846 CRC64;
MQAKVPETCL LTVRVLRASG LPSKDLVTSS DCYVTLNLPT ASSHTLQTRT VKNSRNPVWN
QNFHFRIHRQ LKNVMELKVF DHDLVTRDDP VLSVLFDVGT LQIGTQRQSF SLGTQEKGCL
EVEFRLQTLT DCEEQLISNG IVVARELSCL HVELKRTGDP KRSERKVQLV VAGACEGPQD
ASAGTGSFHF HYPACWEQEL NVHLQDDPHE QLKVPLRTLP SSQLVRLVFP TSQEPLMRLE
LKKEEGPKEL AVRLGCGPCP EEQAFLSKRK QVVAAALKKA LQLDQDLHED EIPVIAVMAT
GGGIRAMTSL YGQLAGLQEL GLLDCISYIT GASGSTWALA NLYEDPEWSQ KDLAGPTEVL
KTQVTKSKLG ALAPSQLWRY RQELAERARL GHPTCFTNLW ALINEALLHD KPHEHKLSDQ
REALSRGQNP LPIYCALNSK EQGLSTFDFG EWCEFSPYEV GFPKYGAFIS SELFGSEFFM
GRLVKQLPES RICFLEGIWS NLFAASLQDS LYWSSEPSQF WDRWAQDQAN LDKEQVPHLK
IAEPPTMAGR IAELFTDLLT KRPLAHATHN FTRGLHFHKD YFQNSHFSAW KASKLDRLPN
QLTPTEPHLC LLDVGYLINT SCPPLLQPTR DVDLILSLDY NLYGAFQQLQ LLSRFCQEQG
IPFPSISPSP EEQRQPQECH LFCDPAQPEA PAVLHFPLVN DSFQDYSAPG VPRTSEEKAA
GEVNLSSSDS PYHYTKVTYS QEDVDKLLRL THYNICNNQD RLREAMHQAV QRRRKRKQFR
PE
