ID   KBX3_HOFGE              Reviewed;          95 AA.
AC   Q0GY40; A8SDT6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Hge-scorpine;
DE   AltName: Full=Hge-scorpine-like 1 {ECO:0000305|PubMed:17141373, ECO:0000305|PubMed:18030427};
DE            Short=HgeScplp1 {ECO:0000303|PubMed:17141373, ECO:0000303|PubMed:18030427};
DE            Short=Hgscplike1;
DE   Contains:
DE     RecName: Full=Hge36 {ECO:0000303|PubMed:18030427};
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 20-64, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
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 20-64, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
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).
RN   [4] {ECO:0007744|PDB:5IPO, ECO:0007744|PDB:5JYH}
RP   STRUCTURE BY NMR OF 48-95, FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF
RP   1-MET--MET-51.
RX   PubMed=27314815; DOI=10.1002/1873-3468.12255;
RA   Flores-Solis D., Toledano Y., Rodriguez-Lima O., Cano-Sanchez P.,
RA   Ramirez-Cordero B.E., Landa A., Rodriguez de la Vega R.C.,
RA   Del Rio-Portilla F.;
RT   "Solution structure and antiparasitic activity of scorpine-like peptides
RT   from Hoffmannihadrurus gertschi.";
RL   FEBS Lett. 590:2286-2296(2016).
CC   -!- FUNCTION: [Hge-scorpine]: Has antibacterial activity against
CC       B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic
CC       activities. Since cell lysis occurs at the tested concentrations,
CC       observation of activity on potassium channels is impossible.
CC       {ECO:0000269|PubMed:18030427}.
CC   -!- FUNCTION: [Hge36]: Blocks Kv1.1/KCNA1 (IC(50)=185 nM) potassium
CC       channels. Shows a weak hemolytic activity.
CC       {ECO:0000269|PubMed:18030427, ECO:0000269|PubMed:27314815}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17141373,
CC       ECO:0000269|PubMed:18030427}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:17141373, ECO:0000269|PubMed:18030427}.
CC   -!- MASS SPECTROMETRY: [Hge-scorpine]: Mass=8370; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17141373};
CC   -!- MASS SPECTROMETRY: [Hge-scorpine]: Mass=8370; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18030427};
CC   -!- MASS SPECTROMETRY: [Hge36]: Mass=5294.95; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18030427};
CC   -!- MISCELLANEOUS: [Hge-scorpine]: The C-terminus (AA 52-95) blocks
CC       Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA2 potassium channels, showing a
CC       potential important role of AA 48-51.
CC   -!- MISCELLANEOUS: [Hge36]: Negative results: does not block Kv1.2/KCNA2
CC       and Kv1.3/KCNA3. {ECO:0000305|PubMed:18030427}.
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ465351; ABE98267.1; -; mRNA.
DR   EMBL; EF613116; ABU94956.1; -; Genomic_DNA.
DR   EMBL; EL698908; -; NOT_ANNOTATED_CDS; mRNA.
DR   PDB; 5IPO; NMR; -; A=48-95.
DR   PDB; 5JYH; NMR; -; A=52-95.
DR   PDBsum; 5IPO; -.
DR   PDBsum; 5JYH; -.
DR   AlphaFoldDB; Q0GY40; -.
DR   SMR; Q0GY40; -.
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   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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   3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Fungicide;
KW   Ion channel impairing toxin; Potassium channel impairing toxin; Secreted;
KW   Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:17141373,
FT                   ECO:0000269|PubMed:18030427"
FT   CHAIN           20..95
FT                   /note="Hge-scorpine"
FT                   /evidence="ECO:0000269|PubMed:17141373,
FT                   ECO:0000269|PubMed:18030427"
FT                   /id="PRO_0000274682"
FT   CHAIN           48..95
FT                   /note="Hge36"
FT                   /evidence="ECO:0000269|PubMed:17141373,
FT                   ECO:0000269|PubMed:18030427"
FT                   /id="PRO_0000356887"
FT   DOMAIN          55..94
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        58..81
FT                   /evidence="ECO:0000269|PubMed:27314815,
FT                   ECO:0007744|PDB:5IPO, ECO:0007744|PDB:5JYH"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000269|PubMed:27314815,
FT                   ECO:0007744|PDB:5IPO, ECO:0007744|PDB:5JYH"
FT   DISULFID        72..88
FT                   /evidence="ECO:0000269|PubMed:27314815,
FT                   ECO:0007744|PDB:5IPO, ECO:0007744|PDB:5JYH"
FT   MUTAGEN         1..51
FT                   /note="Missing: In HgeD; enhanced potassium
FT                   channel-blocking and antiparasitic activities."
FT                   /evidence="ECO:0000269|PubMed:27314815"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:5IPO"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:5IPO"
FT   HELIX           68..74
FT                   /evidence="ECO:0007829|PDB:5IPO"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:5IPO"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:5IPO"
SQ   SEQUENCE   95 AA;  10412 MW;  EA797C1F58CF6C3C CRC64;
     MNTKLTVLCF LGIVTIVSCG WMSEKKVQGI LDKKLPEGII RNAAKAIVHK MAKNQFGCFA
     NVDVKGDCKR HCKAEDKEGI CHGTKCKCGV PISYL
//