ID   PA2_BUNFA               Reviewed;          16 AA.
AC   B3EWQ8;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Phospholipase A2;
DE            Short=PLA2;
DE            EC=3.1.1.4 {ECO:0000250|UniProtKB:Q10756};
DE   AltName: Full=BF-CT1 {ECO:0000303|PubMed:23981271};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:Q10756};
DE   Flags: Fragment;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:23981271};
RX   PubMed=23981271; DOI=10.1016/j.toxicon.2013.08.052;
RA   Bhattacharya S., Das T., Biswas A., Gomes A., Gomes A., Dungdung S.R.;
RT   "A cytotoxic protein (BF-CT1) purified from Bungarus fasciatus venom acts
RT   through apoptosis, modulation of PI3K/AKT, MAPKinase pathway and cell cycle
RT   regulation.";
RL   Toxicon 74:138-150(2013).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. Cytotoxic in Ehrlich ascites
CC       carcinoma model in mice and towards human cancer cell line U937
CC       (IC(50)=610 ug/ml). {ECO:0000250|UniProtKB:Q10756,
CC       ECO:0000269|PubMed:23981271}.
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:Q10756, ECO:0000305|PubMed:23981271};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P0CAS0};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P0CAS0};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23981271}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23981271}.
CC   -!- MASS SPECTROMETRY: Mass=13044.67; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23981271};
CC   -!- MISCELLANEOUS: Is not lethal to mice up to 4.7 mg/kg by intraperitoneal
CC       injection. {ECO:0000269|PubMed:23981271}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; B3EWQ8; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Secreted; Toxin.
FT   CHAIN           1..>16
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000429376"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|PubMed:23981271"
SQ   SEQUENCE   16 AA;  1830 MW;  9F6DCF5C47C03830 CRC64;
     NLYQFKNMIE EAATGT