PA24A_XENLA
ID PA24A_XENLA Reviewed; 749 AA.
AC Q7T0T9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) 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; BC056041; AAH56041.1; -; mRNA.
DR RefSeq; NP_001080867.1; NM_001087398.1.
DR RefSeq; XP_018111992.1; XM_018256503.1.
DR AlphaFoldDB; Q7T0T9; -.
DR SMR; Q7T0T9; -.
DR MaxQB; Q7T0T9; -.
DR PRIDE; Q7T0T9; -.
DR GeneID; 380561; -.
DR KEGG; xla:380561; -.
DR CTD; 380561; -.
DR Xenbase; XB-GENE-5838883; pla2g4a.L.
DR OMA; KFFMGKV; -.
DR OrthoDB; 302848at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 380561; Expressed in spleen and 18 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
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_0000345136"
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:0000250"
FT REGION 428..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
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; 85282 MW; CE769904144C4DE2 CRC64;
MASIDPYQHI IVEHQYSHRF TVTVIKATNV TKGTFGDMLD TPDPYVELYI SSAPDSRKRT
KHFNNNINPV WNETFEFILD PNQDNVLEIT LMDANYVMDE SLGTTTFPIL SVKPGEKKQV
PFTFNKVTEM ILEFSLEVCS STDLRFSMAL CDQEKLFRQK RKNKVINGLR KLLGPEKTQD
LNSTSRDVPV IAVLGSGGGF RAMIGFSGVM KALYESGVLD CATYVAGLSG STWYMSTLYS
HPDFPTKGPK EINKELMHNV SYNPLLLLTP QKVKRYVEAL WKKKSSGQPV TFTDIFAMLI
GETLIKDRMN RKLSHMQEKI NDGQCPLPLF TCLHVKPDVS ELMFADWVEF SPYEIGMAKY
GTFMPPGLFG SKFFMGTVIK KYEENPLHFF MGVWGSAFSI LINRVLGVSN NSKGSTMEEE
IENLKPKHIL GNDSSDSDDE MQEPKGTENA KAEEEYLRNN QASWVQRMLM AILGDSAIFN
TREGRAGKVH NFMLGLNLNT SYPYSPLSGL CTQQSMEEDE LDAAVADPDE FEQIYEPLDV
KSKKIHIVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWARMN
KLPFPKIDPH VFDREGLKEC YIFKPKNTSV EKDCPTVIHF VLANLQFRNF KAPGVPRETT
EEKESADFDI FDDPETPFST FNFQYPNVAF KQLHDLMEFN TLNNINVIKQ AMVESIEYRR
QHPSRCSVSL NDVESRKLHH KDSQSKFQM
