PA24A_XENTR
ID PA24A_XENTR Reviewed; 749 AA.
AC B1WAZ6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cytosolic phospholipase A2;
DE Short=cPLA2;
DE AltName: Full=Phospholipase A2 group IVA;
DE Includes:
DE RecName: Full=Phospholipase A2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Includes:
DE RecName: Full=Lysophospholipase;
DE EC=3.1.1.5;
GN Name=pla2g4a; Synonyms=cpla2, pla2g4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Intestine;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2
CC position releasing arachidonic acid. Together with its lysophospholipid
CC activity, it is implicated in the initiation of the inflammatory
CC response (By similarity). {ECO:0000250}.
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 -!- 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 -!- ACTIVITY REGULATION: Stimulated by agonists such as ATP, EGF, thrombin
CC and bradykinin as well as by cytosolic Ca(2+). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Translocates to membrane vesicles in a calcium-
CC dependent fashion. {ECO:0000250}.
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}.
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DR EMBL; BC161557; AAI61557.1; -; mRNA.
DR RefSeq; NP_001120577.1; NM_001127105.1.
DR RefSeq; XP_012816089.1; XM_012960635.1.
DR RefSeq; XP_012816090.1; XM_012960636.2.
DR RefSeq; XP_012816091.1; XM_012960637.2.
DR RefSeq; XP_012816092.1; XM_012960638.2.
DR AlphaFoldDB; B1WAZ6; -.
DR SMR; B1WAZ6; -.
DR PaxDb; B1WAZ6; -.
DR GeneID; 100145731; -.
DR KEGG; xtr:100145731; -.
DR CTD; 5321; -.
DR Xenbase; XB-GENE-5838849; pla2g4a.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_011663_1_1_1; -.
DR InParanoid; B1WAZ6; -.
DR OrthoDB; 302848at2759; -.
DR BRENDA; 3.1.1.4; 8483.
DR Reactome; R-XTR-111995; phospho-PLA2 pathway.
DR Reactome; R-XTR-1482788; Acyl chain remodelling of PC.
DR Reactome; R-XTR-1482798; Acyl chain remodeling of CL.
DR Reactome; R-XTR-1482801; Acyl chain remodelling of PS.
DR Reactome; R-XTR-1482839; Acyl chain remodelling of PE.
DR Reactome; R-XTR-1482922; Acyl chain remodelling of PI.
DR Reactome; R-XTR-1482925; Acyl chain remodelling of PG.
DR Reactome; R-XTR-1483115; Hydrolysis of LPC.
DR Reactome; R-XTR-1483166; Synthesis of PA.
DR Reactome; R-XTR-2142753; Arachidonic acid metabolism.
DR Reactome; R-XTR-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017371; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; B1WAZ6; baseline.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
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; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF00168; 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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Reference proteome.
FT CHAIN 1..749
FT /note="Cytosolic phospholipase A2"
FT /id="PRO_0000345137"
FT DOMAIN 1..124
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 138..740
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 1..178
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
FT REGION 417..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 549
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 749 AA; 85413 MW; 18EC0E15ED902CAE CRC64;
MASIDPYQHI IVEHQYSHRF TVTVIKATNV TKGTFGDMLD TPDPYVELYI SSAPDSRKRT
KHFNNNINPV WNETFEFILD PNQDNVLEIT LMDANYVMDE SLGTTTFPIS SVKPGEKKQV
PFTFNKVTEM ILEFLLEVCS STDLRFSMAL CDQEKFFRQK RKNQVINGLR KLLGPEKTKD
LNPTSRDVPV IAVLGSGGGF RAMIGFSGVM KALFESGVLD CVTYIAGLSG STWYMSALYS
HADFPNKGPK EINKELMNNV SHNPLLLLTP QKVKRYIEAL WKKKSSGQPV TFTDIFAMLI
GETLIKDRMN RKLSHMQEKI SHGQCPLPLF TCLHVKPDVS ELMFADWVEF SPYEIGMAKY
GTFMPPDHFG SKFFMGTVIK KYEENPLHFL MGVWGSAFSI LINRVLGVST NNQGSTMEEE
IENLKPKHIL GNDSSDSDDE MQEPKGTENS KAEEEYQRNN QASWVQRMLM ALLGDSALFN
TREGRAGKVH NFMLGLNLNT SYPYSPLSGL CTQQSMEEDE FDAAVADPDE FEQIYEPLDV
KSKKIHIVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWARMN
KLPFPKIDPH VFDREGLKEC YIFKPKNPSV EKDCPTVIHF VLANLQFRNF KAPGVPRETA
EEKEFADFDI FDDPETPFST FNFQYPNEAF KRLHDLMEFN TLNNINVIKQ AMVESIEYRK
QHPSRCSVSL NDVEARKLLH KDSQSKFQM
