ID   PA2N3_BUNFA             Reviewed;         120 AA.
AC   P14615; Q0PUV9;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Neutral phospholipase A2 3;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Kbf III;
DE   AltName: Full=Kbf-3;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2599763; DOI=10.1111/j.1399-3011.1989.tb01572.x;
RA   Liu C.-S., Leu H.-L., Chang C.-S., Chen S.-W., Lo T.-B.;
RT   "Amino acid sequence of a neutral phospholipase A2 (III) in the venom of
RT   Bungarus fasciatus.";
RL   Int. J. Pept. Protein Res. 34:257-261(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17166178; DOI=10.1111/j.1742-4658.2006.05598.x;
RA   Tsai I.-H., Tsai H.-Y., Saha A., Gomes A.;
RT   "Sequences, geographic variations and molecular phylogeny of venom
RT   phospholipases and three-finger toxins of eastern India Bungarus fasciatus
RT   and kinetic analyses of its Pro31 phospholipases A2.";
RL   FEBS J. 274:512-525(2007).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13412; Mass_error=1; Method=Electrospray;
CC       Note=In Kbf-3.; Evidence={ECO:0000269|PubMed:17166178};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; DQ768745; ABG75909.1; -; mRNA.
DR   PIR; JK0223; JK0223.
DR   AlphaFoldDB; P14615; -.
DR   SMR; P14615; -.
DR   PRIDE; P14615; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT   CHAIN           1..120
FT                   /note="Neutral phospholipase A2 3"
FT                   /id="PRO_0000161635"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..43
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..89
FT                   /evidence="ECO:0000250"
FT   VARIANT         40
FT                   /note="D -> L"
FT   VARIANT         118..120
FT                   /note="NDI -> Q"
SQ   SEQUENCE   120 AA;  13425 MW;  F377D6219B05B600 CRC64;
     NLFQFKNMIQ CAGTRSWTDY VSYGCYCGKG GSGTPVDQLD RCCKVHDDCY GDAEKIPKCK
     PYYKTYSYDC SEGKLTCKAD NDECAAFICN CDRVAAICFA GAPYNDNNFM IDSKTRCNDI