PA2BA_BUNFA
ID PA2BA_BUNFA Reviewed; 135 AA.
AC P14411;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Basic phospholipase A2 10;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=KBf X;
DE AltName: Full=KBf-10;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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].
RC TISSUE=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=3072971; DOI=10.1515/bchm3.1988.369.2.1227;
RA Liu C.-S., Chang C.-S., Leu H.-L., Chen S.-W., Lo T.-B.;
RT "The complete amino-acid sequence of a basic phospholipase A2 in the venom
RT of Bungarus fasciatus.";
RL Biol. Chem. Hoppe-Seyler 369:1227-1233(1988).
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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:17166178}.
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DR EMBL; DQ508414; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S01801; S01801.
DR AlphaFoldDB; P14411; -.
DR SMR; P14411; -.
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:0000250"
FT /id="PRO_0000291947"
FT CHAIN 18..135
FT /note="Basic phospholipase A2 10"
FT /id="PRO_0000161634"
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 VARIANT 32
FT /note="Q -> R"
FT VARIANT 68
FT /note="H -> D"
FT VARIANT 84
FT /note="E -> S"
FT VARIANT 96
FT /note="G -> D"
FT VARIANT 100..104
FT /note="SCGRN -> TCERF"
FT NON_TER 1
SQ SEQUENCE 135 AA; 14838 MW; EB3BE149E100FD13 CRC64;
AVCVSLLGAA NIPPQPLNLY QFKNMIQCAG TQLWVAYVNY GCYCGKGGSG TPVDQLDRCC
QTHDHCYHNA KRFGKCNPYF KTYEYTCNKP NLTCRGAKGS CGRNVCDCDR AAAICFAAAP
YNLSNFGINK KTHCK
