ID   KBX2_HOFGE              Reviewed;          79 AA.
AC   Q0GY41;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Potassium channel toxin Hge-beta-KTx;
DE            Short=HgebetaKTx;
DE   Flags: Precursor;
OS   Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Iuroidea; Hadrurus.
OX   NCBI_TaxID=380989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17506894; DOI=10.1186/1471-2164-8-119;
RA   Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D.;
RT   "Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus
RT   gertschi (Arachnida: Scorpiones).";
RL   BMC Genomics 8:119-119(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-59, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17141373; DOI=10.1016/j.peptides.2006.06.012;
RA   Diego-Garcia E., Schwartz E.F., D'Suze G., Gonzalez S.A., Batista C.V.,
RA   Garcia B.I., Rodriguez de la Vega R.C., Possani L.D.;
RT   "Wide phylogenetic distribution of scorpine and long-chain beta-KTx-like
RT   peptides in scorpion venoms: identification of 'orphan' components.";
RL   Peptides 28:31-37(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-59, AND FUNCTION.
RX   PubMed=18030427; DOI=10.1007/s00018-007-7370-x;
RA   Diego-Garcia E., Abdel-Mottaleb Y., Schwartz E.F.,
RA   Rodriguez de la Vega R.C., Tytgat J., Possani L.D.;
RT   "Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like
RT   peptides purified from scorpion venoms.";
RL   Cell. Mol. Life Sci. 65:187-200(2008).
CC   -!- FUNCTION: The full peptide presents antibacterial and cytotoxic
CC       activities. The C-terminus (33-76aa) blocks potassium channels
CC       Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA3.
CC       {ECO:0000269|PubMed:18030427}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=6427.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17141373};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ465350; ABE98266.1; -; mRNA.
DR   EMBL; EL698909; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q0GY41; -.
DR   SMR; Q0GY41; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..79
FT                   /note="Potassium channel toxin Hge-beta-KTx"
FT                   /id="PRO_0000274688"
FT   DOMAIN          48..79
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        51..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        58..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        62..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   79 AA;  8689 MW;  B8E6F447F845CEE8 CRC64;
     MAKSFFAAFL IIMLISSLVD GKSTVGQKLK KKLNQAVDKV KEVLNKSEYM CPVVSSFCKQ
     HCARLGKSGQ CDLLECICS