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Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B1 chain, major component (Beta-1-bungarotoxin)

 VKTH1_BUNMU             Reviewed;          85 AA.
P00987; O42298; P00988; Q9PTA4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
22-NOV-2017, entry version 101.
RecName: Full=Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B1 chain, major component;
AltName: Full=Beta-1-bungarotoxin;
Flags: Precursor;
Bungarus multicinctus (Many-banded krait).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
NCBI_TaxID=8616;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Venom gland;
PubMed=9693106; DOI=10.1042/bj3340087;
Wu P.-F., Wu S.-N., Chang C.-C., Chang L.-S.;
"Cloning and functional expression of B chains of beta-bungarotoxins
from Bungarus multicinctus (Taiwan banded krait).";
Biochem. J. 334:87-92(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=10903499; DOI=10.1046/j.1432-1327.2000.01518.x;
Wu P.-F., Chang L.-S.;
"Genetic organization of A chain and B chain of beta-bungarotoxin from
Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain
genes do not share a common origin.";
Eur. J. Biochem. 267:4668-4675(2000).
[3]
PROTEIN SEQUENCE OF 25-85.
TISSUE=Venom;
PubMed=624701;
Kondo K., Narita K., Lee C.-Y.;
"Amino acid sequences of the two polypeptide chains in beta1-
bungarotoxin from the venom of Bungarus multicinctus.";
J. Biochem. 83:101-115(1978).
[4]
MUTAGENESIS OF CYS-79.
PubMed=11732693; DOI=10.1023/A:1012237005574;
Wu P.-F., Chang L.-S.;
"Expression of A chain and B chain of beta-bungarotoxin from taiwan
banded krait: the functional implication of the interchain disulfide
bond between A chain and B chain.";
J. Protein Chem. 20:413-421(2001).
[5]
SUBUNIT.
TISSUE=Venom;
PubMed=16457863; DOI=10.1016/j.toxicon.2005.11.009;
Cheng Y.-C., Chen K.-C., Lin S.-K., Chang L.-S.;
"Divergence of genes encoding B chains of beta-bungarotoxins.";
Toxicon 47:322-329(2006).
-!- FUNCTION: Beta-1-bungarotoxin is a presynaptic neurotoxin of the
venom. The B chain is homologous to venom basic protease
inhibitors but has no protease inhibitor activity and blocks
voltage-gated potassium channels (Kv) (By similarity).
{ECO:0000250, ECO:0000269|PubMed:9693106}.
-!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have
phospholipase A2 activity and the B chains show homology with the
basic protease inhibitors. {ECO:0000269|PubMed:16457863}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: Belongs to the venom Kunitz-type family.
{ECO:0000305}.
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EMBL; Y12100; CAA72809.1; -; mRNA.
EMBL; AJ251223; CAB62503.1; -; Genomic_DNA.
PIR; A01219; TIKFBY.
ProteinModelPortal; P00987; -.
SMR; P00987; -.
MEROPS; I02.978; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00109; KU; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 1.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Presynaptic neurotoxin; Secreted;
Signal; Toxin; Voltage-gated potassium channel impairing toxin.
SIGNAL 1 24 {ECO:0000269|PubMed:624701}.
CHAIN 25 85 Kunitz-type serine protease inhibitor
homolog beta-bungarotoxin B1 chain, major
component.
/FTId=PRO_0000016863.
DOMAIN 31 81 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 31 81 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 40 64 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 56 77 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 79 79 Interchain (with an A chain).
MUTAGEN 79 79 C->S: Loss of PA2 activity. Weak loss in
folding. {ECO:0000269|PubMed:11732693}.
CONFLICT 16 16 C -> S (in Ref. 2; CAB62503).
{ECO:0000305}.
CONFLICT 45 45 Missing (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 65 70 NGNGNH -> DGDHGN (in Ref. 3; AA
sequence). {ECO:0000305}.
SEQUENCE 85 AA; 9571 MW; A1E3D452AE67DE5C CRC64;
MSSGGLLLLL GLLTLCAELI PVSSRQRHRD CDKPPDKGNC GPVRRAFYYD TRLKTCKAFQ
YRGCNGNGNH FKTETLCRCE CLVYP


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