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   16-JUN-2009, entry version 8.
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;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   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
CC       sn-2 position releasing arachidonic acid. Together with its
CC       lysophospholipid activity, it is implicated in the initiation of
CC       the inflammatory response (By similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Stimulated by agonists such as ATP, EGF,
CC       thrombin and bradykinin as well as by cytosolic Ca(2+) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC       vesicle (By similarity). Note=Translocates to membrane vesicles in
CC       a calcium-dependent fashion (By similarity).
CC   -!- DOMAIN: The N-terminal C2 domain, by its association with lipid
CC       membranes, mediates the regulation of CPLA2 by presenting the
CC       active site to its substrate in response to elevations of
CC       cytosolic Ca(2+) (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PLA2c domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC161557; AAI61557.1; -; mRNA.
DR   RefSeq; NP_001120577.1; -.
DR   UniGene; Str.52630; -.
DR   GeneID; 100145731; -.
DR   KEGG; xtr:100145731; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR002642; PLA2_B.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 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.
FT   CHAIN         1    749       Cytosolic phospholipase A2.
FT                                /FTId=PRO_0000345137.
FT   DOMAIN        5    106       C2.
FT   DOMAIN      138    740       PLA2c.
FT   REGION        1    178       Phospholipid binding (Probable).
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
//