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KAX3H_BUTPA
ID   KAX3H_BUTPA             Reviewed;          38 AA.
AC   P0DL44;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.17 {ECO:0000303|PubMed:23523531};
DE   AltName: Full=Toxin BoPKTX {ECO:0000303|PubMed:23523531};
OS   Buthus paris (Scorpion) (Buthus occitanus paris).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=1388771;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC
RP   DOSE, AND NOMENCLATURE.
RC   TISSUE=Venom;
RX   PubMed=23523531; DOI=10.1016/j.toxicon.2013.03.004;
RA   Martin-Eauclaire M.F., Ceard B., Belghazi M., Lebrun R., Bougis P.E.;
RT   "Characterization of the first K+ channel blockers from the venom of the
RT   Moroccan scorpion Buthus occitanus Paris.";
RL   Toxicon 75:168-176(2013).
CC   -!- FUNCTION: Completely inhibits the (125)I-kaliotoxin binding on rat
CC       brain synaptosomes with high-affinity (IC(50)=0.1 nM). Is a potent
CC       Kv1.3/KCNA3 ligand. {ECO:0000269|PubMed:23523531}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23523531}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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:P24662}.
CC   -!- MASS SPECTROMETRY: Mass=4161; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23523531};
CC   -!- TOXIC DOSE: LD(50) is 10 ug/kg by intracerebroventricular injection
CC       into mice. {ECO:0000269|PubMed:23523531}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 03 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL44; -.
DR   SMR; P0DL44; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   1: Evidence at protein level;
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   CHAIN           1..38
FT                   /note="Potassium channel toxin alpha-KTx 3.17"
FT                   /evidence="ECO:0000269|PubMed:23523531"
FT                   /id="PRO_0000433140"
FT   DISULFID        8..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   38 AA;  4166 MW;  0F8149AD0A7C2BA5 CRC64;
     GVPINVKCSG SRDCLEPCKK AGMRFGKCIN RKCHCTPK
 
 
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