KBX2_TITST
ID KBX2_TITST Reviewed; 91 AA.
AC P0C8W4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Potassium channel toxin TstKMK;
DE AltName: Full=Toxin 5536;
DE AltName: Full=beta-Ktx;
DE Flags: Precursor;
OS Tityus stigmurus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=50344;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom gland;
RX PubMed=23200836; DOI=10.1016/j.bbrc.2012.11.044;
RA Almeida D.D., Torres T.M., Barbosa E.G., Lima J.P.,
RA de Freitas Fernandes-Pedrosa M.;
RT "Molecular approaches for structural characterization of a new potassium
RT channel blocker from Tityus stigmurus venom: cDNA cloning, homology
RT modeling, dynamic simulations and docking.";
RL Biochem. Biophys. Res. Commun. 430:113-118(2013).
RN [2]
RP PROTEIN SEQUENCE OF 43-57, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17270501; DOI=10.1016/j.cbpc.2006.12.004;
RA Batista C.V.F., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z.,
RA Gomez-Lagunas F., Possani L.D.;
RT "Proteomic analysis of the venom from the scorpion Tityus stigmurus:
RT biochemical and physiological comparison with other Tityus species.";
RL Comp. Biochem. Physiol. 146C:147-157(2007).
CC -!- FUNCTION: Blocks voltage-gated potassium channels (Kv). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=5536.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17270501};
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: A mature protein with 47 amino acid residues is predicted in
CC PubMed:17270501 (sequence of 45-91) instead of the chain proposed here
CC (2 amino acids longer). Since the protein sequence and the predicted
CC mass correspond exactly with proteomic data (PubMed:17270501), the 49
CC amino acid chain is shown. {ECO:0000305|PubMed:17270501}.
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DR EMBL; JK483711; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C8W4; -.
DR SMR; P0C8W4; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR029237; Long_scorpion_toxin.
DR Pfam; PF14866; Toxin_38; 1.
DR PROSITE; PS51862; BSPN_CSAB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..42
FT /evidence="ECO:0000269|PubMed:17270501"
FT /id="PRO_0000421251"
FT CHAIN 43..91
FT /note="Potassium channel toxin TstKMK"
FT /id="PRO_0000366102"
FT DOMAIN 58..91
FT /note="BetaSPN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 61..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 68..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ SEQUENCE 91 AA; 10097 MW; 39EED225DDFC4589 CRC64;
MVATNRCCVF ALLFALLLVH SLTEAGKGKE ILGKIKEKII EAKDKMKAGW ERLTSQSEYA
CPAIDKFCED HCAAKKAVGK CDDFKCKCIK L
