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KAX95_BUTOC
ID   KAX95_BUTOC             Reviewed;          28 AA.
AC   P84744;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Potassium channel toxin alpha-KTx 9.5 {ECO:0000305};
DE   AltName: Full=Kbot1 {ECO:0000303|PubMed:15165720};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT VAL-28, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15165720; DOI=10.1016/j.peptides.2004.02.017;
RA   Mahjoubi-Boubaker B., Crest M., Khalifa R.B., Ayeb M.E., Kharrat R.;
RT   "Kbot1, a three disulfide bridges toxin from Buthus occitanus tunetanus
RT   venom highly active on both SK and Kv channels.";
RL   Peptides 25:637-645(2004).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels Kv1.1/KCNA1
CC       (IC(50)=145 nM), Kv1.2/KCNA2 (IC(50)=2.5 nM), and Kv1.3/KCNA3
CC       (IC(50)=15). Also inhibits calcium-activated potassium channels
CC       (KCa/KCNN). {ECO:0000269|PubMed:15165720}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15165720}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15165720}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:Q9NJP7}.
CC   -!- MASS SPECTROMETRY: Mass=2942.58; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15165720};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 09 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P84744; -.
DR   SMR; P84744; -.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; IDA:UniProtKB.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR008911; Toxin_alpha-KTx_8/9.
DR   Pfam; PF05453; Toxin_6; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium-activated potassium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..28
FT                   /note="Potassium channel toxin alpha-KTx 9.5"
FT                   /evidence="ECO:0000269|PubMed:15165720"
FT                   /id="PRO_0000045198"
FT   MOD_RES         28
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:15165720"
FT   DISULFID        3..19
FT                   /evidence="ECO:0000250|UniProtKB:Q9NJP7"
FT   DISULFID        6..24
FT                   /evidence="ECO:0000250|UniProtKB:Q9NJP7"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000250|UniProtKB:Q9NJP7"
SQ   SEQUENCE   28 AA;  2949 MW;  DD72AD78A710B98B CRC64;
     VGCEECPMHC KGKHAVPTCD DGVCNCNV
 
 
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