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Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chain (Beta-2-bungarotoxin)

 VKTH2_BUNMU             Reviewed;          85 AA.
P00989; O42299; Q1RPT1; Q9PRV8; Q9PTA3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
28-MAR-2018, entry version 122.
RecName: Full=Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chain;
AltName: Full=Beta-2-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=Venom gland;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
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).
[4]
PROTEIN SEQUENCE OF 25-85.
TISSUE=Venom;
PubMed=7096304;
Kondo K., Toda H., Narita K., Lee C.-Y.;
"Amino acid sequence of beta 2-bungarotoxin from Bungarus multicinctus
venom. The amino acid substitutions in the B chains.";
J. Biochem. 91:1519-1530(1982).
[5]
PROTEIN SEQUENCE OF 25-63.
PubMed=7945237; DOI=10.1042/bj3030171;
Chu C.C., Chu S.T., Chen S.W., Chen Y.H.;
"The non-phospholipase A2 subunit of beta-bungarotoxin plays an
important role in the phospholipase A2-independent neurotoxic effect:
characterization of three isotoxins with a common phospholipase A2
subunit.";
Biochem. J. 303:171-176(1994).
[6]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=8590005; DOI=10.1016/S0969-2126(01)00246-5;
Kwong P.D., McDonald N.Q., Sigler P.B., Hendrickson W.A.;
"Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz
modules and targeted phospholipase action.";
Structure 3:1109-1119(1995).
-!- FUNCTION: Beta-2-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).
{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:8590005}.
-!- 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; Y12101; CAA72810.1; -; mRNA.
EMBL; AM050151; CAJ18318.1; -; Genomic_DNA.
EMBL; AJ251224; CAB62504.1; -; Genomic_DNA.
PIR; A44550; TIKFB2.
PDB; 1BUN; X-ray; 2.45 A; B=25-85.
PDBsum; 1BUN; -.
ProteinModelPortal; P00989; -.
SMR; P00989; -.
IntAct; P00989; 1.
MINT; P00989; -.
EvolutionaryTrace; P00989; -.
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;
3D-structure; 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:7096304,
ECO:0000269|PubMed:7945237}.
CHAIN 25 85 Kunitz-type serine protease inhibitor
homolog beta-bungarotoxin B2 chain.
/FTId=PRO_0000016864.
DOMAIN 31 81 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 31 81 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:8590005}.
DISULFID 40 64 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:8590005}.
DISULFID 56 77 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:8590005}.
DISULFID 79 79 Interchain (with an A chain).
{ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:8590005}.
CONFLICT 44 44 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 65 70 NGNGNH -> DGDHGN (in Ref. 4; AA
sequence). {ECO:0000305}.
CONFLICT 82 83 LE -> EL (in Ref. 4; AA sequence).
{ECO:0000305}.
TURN 29 32 {ECO:0000244|PDB:1BUN}.
STRAND 40 42 {ECO:0000244|PDB:1BUN}.
STRAND 44 50 {ECO:0000244|PDB:1BUN}.
HELIX 51 53 {ECO:0000244|PDB:1BUN}.
STRAND 55 61 {ECO:0000244|PDB:1BUN}.
STRAND 66 68 {ECO:0000244|PDB:1BUN}.
STRAND 71 73 {ECO:0000244|PDB:1BUN}.
HELIX 74 81 {ECO:0000244|PDB:1BUN}.
SEQUENCE 85 AA; 9568 MW; FE95A59AF92BF2AA CRC64;
MSSGGLLLLL GLLTLCAELT PVSSRKRHPD CDKPPDTKIC QTVVRAFYYK PSAKRCVQFR
YGGCNGNGNH FKSDHLCRCE CLEYR


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