ID   PA23_NAJNA              Reviewed;          15 AA.
AC   P86542;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Phospholipase A2 3 {ECO:0000303|PubMed:20203422};
DE            Short=PLA23 {ECO:0000303|PubMed:20203422};
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P00598};
DE   Flags: Fragment;
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:20203422};
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {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         Evidence={ECO:0000250|UniProtKB:P00598, ECO:0000255|PROSITE-
CC         ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20203422}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
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DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW   Secreted.
FT   CHAIN           1..>15
FT                   /note="Phospholipase A2 3"
FT                   /id="PRO_0000394694"
FT   DISULFID        11..?
FT                   /evidence="ECO:0000250|UniProtKB:P00598"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|PubMed:20203422"
SQ   SEQUENCE   15 AA;  1786 MW;  B009834BB585F0A0 CRC64;
     NLYQFKNMIQ CTVPS