ID   KA23I_HOTJU             Reviewed;          62 AA.
AC   F1CJ67;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=U10-hottentoxin-Hj2a;
DE   Flags: Precursor;
OS   Hottentotta judaicus (Black scorpion) (Buthotus judaicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Hottentotta.
OX   NCBI_TaxID=6863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=21329713; DOI=10.1016/j.toxicon.2011.02.001;
RA   Morgenstern D., Rohde B.H., King G.F., Tal T., Sher D., Zlotkin E.;
RT   "The tale of a resting gland: transcriptome of a replete venom gland from
RT   the scorpion Hottentotta judaicus.";
RL   Toxicon 57:695-703(2011).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22230549; DOI=10.1016/j.peptides.2011.12.012;
RA   Zeng X.C., Zhang L., Nie Y., Luo X.;
RT   "Identification and molecular characterization of three new K(+)-channel
RT   specific toxins from the Chinese scorpion Mesobuthus martensii Karsch
RT   revealing intronic number polymorphism and alternative splicing in
RT   duplicated genes.";
RL   Peptides 34:311-323(2012).
CC   -!- FUNCTION: May block potassium channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 23 subfamily. {ECO:0000305}.
CC   -!- CAUTION: Has been classified as a the potassium channel toxin alpha-KTx
CC       22.3 in PubMed:22230549. Since the subfamily 22 has already been
CC       attributed, this peptide should be reclassified as alpha-KTx 23.3.
CC       {ECO:0000305}.
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DR   EMBL; HQ288176; ADY39598.1; -; mRNA.
DR   AlphaFoldDB; F1CJ67; -.
DR   SMR; F1CJ67; -.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..62
FT                   /note="U10-hottentoxin-Hj2a"
FT                   /id="PRO_0000417438"
FT   SITE            45
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            62
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..59
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..61
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   62 AA;  7147 MW;  53205DB12C9DADE8 CRC64;
     MQKLLIILIL FCILKFNVDV EGRTAFPCNQ SKCQERCKKE IKKGKCILQF ISVSASQSCR
     CY