ID   PA2A_BOTPA              Reviewed;         139 AA.
AC   D0UGJ0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Acidic phospholipase A2 BpPLA2-TXI;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1042543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-31, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=22480909; DOI=10.1016/j.jprot.2012.03.028;
RA   Rodrigues R.S., Boldrini-Franca J., Fonseca F.P., de la Torre P.,
RA   Henrique-Silva F., Sanz L., Calvete J.J., Rodrigues V.M.;
RT   "Combined snake venomics and venom gland transcriptomic analysis of
RT   Bothropoides pauloensis.";
RL   J. Proteomics 75:2707-2720(2012).
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:0000255|PROSITE-ProRule:PRU10035};
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   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; GQ850458; ACX71493.1; -; mRNA.
DR   AlphaFoldDB; D0UGJ0; -.
DR   SMR; D0UGJ0; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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; 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; 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; Signal;
KW   Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:22480909"
FT   CHAIN           17..139
FT                   /note="Acidic phospholipase A2 BpPLA2-TXI"
FT                   /id="PRO_0000423029"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         45
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   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15395 MW;  5AD9BC1B574C7DED CRC64;
     MRTLWIMAVL LVGVEGNLVQ FETLIMKIAG RSGVWYYGSY GCYCGSGGQG RPQDASDRCC
     FVHDCCYGKV TDCDPKADVY TYSEENGVVV CGGDDPCKKQ ICEVRQGCGN LLPRHKDTYE
     HNILVFPAKT FAKKESEPC