PA2B2_BUNFA
ID PA2B2_BUNFA Reviewed; 145 AA.
AC Q90WA8;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Basic phospholipase A2 2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=KBf II {ECO:0000303|PubMed:17166178};
DE AltName: Full=KBf-2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 isozyme II;
DE Flags: Precursor;
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].
RC TISSUE=Venom gland;
RA Zha H., Zhang Y.;
RT "cDNA cloning and characterization of phospholipase A2 from the snake
RT Bungarus fasciatus.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-145, PROTEIN SEQUENCE OF 28-47, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
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: Snake venom phospholipase A2 (PLA2) that inhibits
CC neuromuscular transmission by blocking acetylcholine release from the
CC nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC 2-acyl groups in 3-sn-phosphoglycerides (By similarity). {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, 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:0000269|PubMed:17166178}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17166178}.
CC -!- MASS SPECTROMETRY: Mass=13003; Mass_error=1; Method=Electrospray;
CC Note=In KBf-2.; 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; DQ508412; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF387594; AAK62361.1; -; mRNA.
DR AlphaFoldDB; Q90WA8; -.
DR SMR; Q90WA8; -.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:17166178"
FT /id="PRO_0000022831"
FT CHAIN 28..145
FT /note="Basic phospholipase A2 2"
FT /id="PRO_0000022832"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..97
FT /evidence="ECO:0000250"
FT DISULFID 52..144
FT /evidence="ECO:0000250"
FT DISULFID 54..70
FT /evidence="ECO:0000250"
FT DISULFID 69..125
FT /evidence="ECO:0000250"
FT DISULFID 76..118
FT /evidence="ECO:0000250"
FT DISULFID 86..111
FT /evidence="ECO:0000250"
FT DISULFID 104..116
FT /evidence="ECO:0000250"
FT VARIANT 18
FT /note="A -> G"
FT VARIANT 114
FT /note="T -> N"
FT VARIANT 124
FT /note="L -> I"
SQ SEQUENCE 145 AA; 15769 MW; 5599DA79109D0700 CRC64;
MNPAHLLVLL AVCVSLLAAA NIPPQSLNLL QFKNMIECAG TRTWMAYVKY GCYCGPGGTG
TPLDELDRCC QTHDQCYDNA KKFGNCIPYF KTYVYTCNKP DITCTGAKGS CGRTVCDCDR
AAALCFAAAP YNLANFGINK ETHCQ
