PA2A_BOTIN
ID PA2A_BOTIN Reviewed; 138 AA.
AC Q8QG87;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acidic phospholipase A2 BITP01A;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=BinTX-I;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12459276; DOI=10.1016/s0378-1119(02)01080-6;
RA Junqueira-de-Azevedo I.L.M., Ho P.L.;
RT "A survey of gene expression and diversity in the venom glands of the
RT pitviper snake Bothrops insularis through the generation of expressed
RT sequence tags (ESTs).";
RL Gene 299:279-291(2002).
RN [2]
RP PROTEIN SEQUENCE OF 17-138, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17140721; DOI=10.1016/j.biochi.2006.10.006;
RA Cogo J.C., Lilla S., Souza G.H.M.F., Hyslop S., de Nucci G.;
RT "Purification, sequencing and structural analysis of two acidic
RT phospholipases A2 from the venom of Bothrops insularis (jararaca ilhoa).";
RL Biochimie 88:1947-1959(2006).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces edema in
CC mice, produces neuromuscular blockade in chick biventer cervicis,
CC increases CK release and produces myonecrosis. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:17140721}.
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;
CC Evidence={ECO:0000250|UniProtKB:P59071};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P59071};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17140721}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17140721}.
CC -!- MASS SPECTROMETRY: Mass=13975; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17140721};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF490535; AAM09694.1; -; mRNA.
DR AlphaFoldDB; Q8QG87; -.
DR SMR; Q8QG87; -.
DR BRENDA; 3.1.1.4; 9397.
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; 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; Myotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:17140721"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 BITP01A"
FT /id="PRO_0000022820"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 138 AA; 15759 MW; DFB41FD618A1CE54 CRC64;
MRTLWIMAVL LVGVEGNLWQ FGKMMNYVMG QSVVYKYFYY GCYCGWGGIG QPRDATDRCC
FVHDCCYGKV TGCDPKTDSY TYSKENGDVV CGGDDPCKKQ ICECDRVAAT CFRDNKDTYD
MKYWLYGAKN CQEESEPC
