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VKTH1_BUNMU
ID   VKTH1_BUNMU             Reviewed;          85 AA.
AC   P00987; O42298; P00988; Q9PTA4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B1 chain, major component;
DE   AltName: Full=Beta-1-bungarotoxin;
DE   Flags: Precursor;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=9693106; DOI=10.1042/bj3340087;
RA   Wu P.-F., Wu S.-N., Chang C.-C., Chang L.-S.;
RT   "Cloning and functional expression of B chains of beta-bungarotoxins from
RT   Bungarus multicinctus (Taiwan banded krait).";
RL   Biochem. J. 334:87-92(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=10903499; DOI=10.1046/j.1432-1327.2000.01518.x;
RA   Wu P.-F., Chang L.-S.;
RT   "Genetic organization of A chain and B chain of beta-bungarotoxin from
RT   Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain
RT   genes do not share a common origin.";
RL   Eur. J. Biochem. 267:4668-4675(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-85.
RC   TISSUE=Venom;
RX   PubMed=624701; DOI=10.1093/oxfordjournals.jbchem.a131881;
RA   Kondo K., Narita K., Lee C.-Y.;
RT   "Amino acid sequences of the two polypeptide chains in beta1-bungarotoxin
RT   from the venom of Bungarus multicinctus.";
RL   J. Biochem. 83:101-115(1978).
RN   [4]
RP   MUTAGENESIS OF CYS-79.
RX   PubMed=11732693; DOI=10.1023/a:1012237005574;
RA   Wu P.-F., Chang L.-S.;
RT   "Expression of A chain and B chain of beta-bungarotoxin from taiwan banded
RT   krait: the functional implication of the interchain disulfide bond between
RT   A chain and B chain.";
RL   J. Protein Chem. 20:413-421(2001).
RN   [5]
RP   SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=16457863; DOI=10.1016/j.toxicon.2005.11.009;
RA   Cheng Y.-C., Chen K.-C., Lin S.-K., Chang L.-S.;
RT   "Divergence of genes encoding B chains of beta-bungarotoxins.";
RL   Toxicon 47:322-329(2006).
CC   -!- FUNCTION: Beta-1-bungarotoxin is a presynaptic neurotoxin of the venom.
CC       The B chain is homologous to venom basic protease inhibitors but has no
CC       protease inhibitor activity and blocks voltage-gated potassium channels
CC       (Kv) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9693106}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. The A chains have phospholipase
CC       A2 activity and the B chains show homology with the basic protease
CC       inhibitors. {ECO:0000269|PubMed:16457863}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; Y12100; CAA72809.1; -; mRNA.
DR   EMBL; AJ251223; CAB62503.1; -; Genomic_DNA.
DR   PIR; A01219; TIKFBY.
DR   AlphaFoldDB; P00987; -.
DR   SMR; P00987; -.
DR   MEROPS; I02.978; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Presynaptic neurotoxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:624701"
FT   CHAIN           25..85
FT                   /note="Kunitz-type serine protease inhibitor homolog beta-
FT                   bungarotoxin B1 chain, major component"
FT                   /id="PRO_0000016863"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        79
FT                   /note="Interchain (with an A chain)"
FT   MUTAGEN         79
FT                   /note="C->S: Loss of PA2 activity. Weak loss in folding."
FT                   /evidence="ECO:0000269|PubMed:11732693"
FT   CONFLICT        16
FT                   /note="C -> S (in Ref. 2; CAB62503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65..70
FT                   /note="NGNGNH -> DGDHGN (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9571 MW;  A1E3D452AE67DE5C CRC64;
     MSSGGLLLLL GLLTLCAELI PVSSRQRHRD CDKPPDKGNC GPVRRAFYYD TRLKTCKAFQ
     YRGCNGNGNH FKTETLCRCE CLVYP
 
 
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