PA2B3_BUNFA
ID PA2B3_BUNFA Reviewed; 135 AA.
AC P00629; A2CKF8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Basic phospholipase A2 Vb-2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Toxin V-3;
DE Flags: Precursor; 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]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-37, 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).
RN [2]
RP PROTEIN SEQUENCE OF 18-135.
RC TISSUE=Venom;
RX PubMed=6784277; DOI=10.1016/0041-0101(81)90122-7;
RA Lu H.-S., Lo T.-B.;
RT "Complete amino acid sequences of two cardiotoxin-like analogues from
RT Bungarus fasciatus (banded krait) snake venom.";
RL Toxicon 19:103-111(1981).
RN [3]
RP SEQUENCE REVISION.
RC TISSUE=Venom;
RX PubMed=2089739; DOI=10.1016/0041-0101(90)90159-5;
RA Liu C.-S., Chen J.-M., Chang C.-H., Chen S.-W., Tsai I.-H., Lu H.-S.,
RA Lo T.-B.;
RT "Revised amino acid sequences of the three major phospholipases A2 from
RT Bungarus fasciatus (banded krait) venom.";
RL Toxicon 28:1457-1468(1990).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has only a weak
CC enzymatic activity. Inhibits neuromuscular transmission by blocking
CC acetylcholine release from the nerve termini. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC 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=13093; Mass_error=1; Method=Electrospray;
CC 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; DQ835584; ABI33872.1; -; mRNA.
DR PIR; B36487; PSKFT3.
DR AlphaFoldDB; P00629; -.
DR SMR; P00629; -.
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; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL <1..?
FT /evidence="ECO:0000250"
FT PROPEP ?..17
FT /evidence="ECO:0000269|PubMed:17166178,
FT ECO:0000269|PubMed:6784277"
FT /id="PRO_0000291949"
FT CHAIN 18..135
FT /note="Basic phospholipase A2 Vb-2"
FT /id="PRO_0000161637"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 28..87
FT /evidence="ECO:0000250"
FT DISULFID 42..134
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..115
FT /evidence="ECO:0000250"
FT DISULFID 66..108
FT /evidence="ECO:0000250"
FT DISULFID 76..101
FT /evidence="ECO:0000250"
FT DISULFID 94..106
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 135 AA; 14752 MW; 450B95BA809A4632 CRC64;
AVCVSLLGAA NIPPQPLNLL QFKNMIQCAG SRLWVAYVKY GCYCGPGGTG TPLDQLDRCC
QTHDHCYDNA KKFGNCIPYF KTYEYTCNKP DITCTDAKGS CGRTVCDCDR AAAICFAAAP
YNLANFGIDK EKHCQ
