ID   KBX1_TITCO              Reviewed;          87 AA.
AC   Q5G8A6; Q5G8A7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Scorpine-like peptide Tco 41.46-2;
DE   Contains:
DE     RecName: Full=Scorpine-like peptide Tco 42.14;
DE     AltName: Full=Tco-beta-KTx;
DE              Short=TcobetaKTx;
DE   Flags: Precursor;
OS   Tityus costatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=309814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-50, PROTEIN SEQUENCE OF
RP   28-59, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15683865; DOI=10.1016/j.toxicon.2004.10.014;
RA   Diego-Garcia E., Batista C.V.F., Garcia-Gomez B.I., Lucas S., Candido D.M.,
RA   Gomez-Lagunas F., Possani L.D.;
RT   "The Brazilian scorpion Tityus costatus Karsch: genes, peptides and
RT   function.";
RL   Toxicon 45:273-283(2005).
CC   -!- FUNCTION: Scorpine-like peptide Tco 41.46-2 may have anti-bacterial
CC       activity. {ECO:0000250}.
CC   -!- FUNCTION: Tco 42.14 may block voltage-gated potassium channels.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15683865}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15683865}.
CC   -!- MASS SPECTROMETRY: [Scorpine-like peptide Tco 41.46-2]: Mass=7678.0;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:15683865};
CC   -!- MASS SPECTROMETRY: [Scorpine-like peptide Tco 42.14]: Mass=6730.0;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:15683865};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY740694; AAW72464.1; -; mRNA.
DR   EMBL; AY740695; AAW72465.1; -; mRNA.
DR   AlphaFoldDB; Q5G8A6; -.
DR   SMR; Q5G8A6; -.
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   GO; GO:0042742; P:defense response to bacterium; 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   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:15683865"
FT   CHAIN           20..87
FT                   /note="Scorpine-like peptide Tco 41.46-2"
FT                   /id="PRO_0000231507"
FT   CHAIN           28..87
FT                   /note="Scorpine-like peptide Tco 42.14"
FT                   /id="PRO_0000231508"
FT   DOMAIN          53..87
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        63..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        67..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   CONFLICT        7
FT                   /note="L -> P (in Ref. 1; AAW72464)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   87 AA;  9776 MW;  FC1A9DDB3858EDFC CRC64;
     MERKLALLLF LGMVTLASCG LREKHVQKLV ALIPNDQLRS ILKAVVHKVA KTQFGCPAYE
     GYCNNHCQDI ERKDGECHGF KCKCAKD