PA2AB_BUNCA
ID PA2AB_BUNCA Reviewed; 142 AA.
AC Q802I1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Acidic phospholipase A2 Bc-PL;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor; Fragment;
OS Bungarus candidus (Malayan krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=92438;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=12220723; DOI=10.1016/s0041-0101(02)00150-2;
RA Tsai I.-H., Hsu H.Y., Wang Y.M.;
RT "A novel phospholipase A(2) from the venom glands of Bungarus candidus:
RT cloning and sequence-comparison.";
RL Toxicon 40:1363-1367(2002).
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:12220723}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein is not found in the crude venom.
CC {ECO:0000305|PubMed:12220723}.
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DR EMBL; AF492561; AAO84769.1; -; mRNA.
DR AlphaFoldDB; Q802I1; -.
DR SMR; Q802I1; -.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal.
FT SIGNAL <1..9
FT /evidence="ECO:0000255"
FT PROPEP 10..17
FT /evidence="ECO:0000250"
FT /id="PRO_0000293099"
FT CHAIN 18..142
FT /note="Acidic phospholipase A2 Bc-PL"
FT /id="PRO_0000293100"
FT ACT_SITE 65
FT /evidence="ECO:0000250"
FT ACT_SITE 116
FT /evidence="ECO:0000250"
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 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 28..94
FT /evidence="ECO:0000250"
FT DISULFID 44..141
FT /evidence="ECO:0000250"
FT DISULFID 46..62
FT /evidence="ECO:0000250"
FT DISULFID 61..122
FT /evidence="ECO:0000250"
FT DISULFID 68..115
FT /evidence="ECO:0000250"
FT DISULFID 78..108
FT /evidence="ECO:0000250"
FT DISULFID 101..113
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 142 AA; 15641 MW; A611D062B12F9781 CRC64;
AVCVSLLGAA NIPPQPLTFL QFNEMIECTI PGSFPLLDNM DCGCYCGTGG RGTPVDMLDR
CCKEHDDCYA QIKENLKCSS LLNVPYVKQY SFTCSEGDLT CSDAAGTCAR IVCDCDRTAA
LCFAEAPYKR RNFKIDYKTR CQ
