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Potassium channel toxin alpha-KTx 2.5 (Hongotoxin-1) (HgTX1)

 KAX25_CENLM             Reviewed;          39 AA.
P59847;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 1.
22-NOV-2017, entry version 72.
RecName: Full=Potassium channel toxin alpha-KTx 2.5;
AltName: Full=Hongotoxin-1 {ECO:0000303|PubMed:9446567};
Short=HgTX1 {ECO:0000303|PubMed:9446567};
Centruroides limbatus (Bark scorpion).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
NCBI_TaxID=244936;
[1]
PROTEIN SEQUENCE, FUNCTION, ACTIVITY PROFILE, MUTAGENESIS OF ALA-19
AND TYR-37, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=9446567; DOI=10.1074/jbc.273.5.2639;
Koschak A., Bugianesi R.M., Mitterdorfer J., Kaczorowski G.J.,
Garcia M.L., Knaus H.-G.;
"Subunit composition of brain voltage-gated potassium channels
determined by hongotoxin-1, a novel peptide derived from Centruroides
limbatus venom.";
J. Biol. Chem. 273:2639-2644(1998).
[2]
STRUCTURE BY NMR, DISULFIDE BONDS, MASS SPECTROMETRY, AND MUTAGENESIS
OF ALA-19 AND TYR-37.
TISSUE=Venom;
PubMed=12009929; DOI=10.1021/bc015543s;
Pragl B., Koschak A., Trieb M., Obermair G., Kaufmann W.A.,
Gerster U., Blanc E., Hahn C., Prinz H., Schuetz G., Darbon H.,
Gruber H.J., Knaus H.-G.;
"Synthesis, characterization, and application of cy-dye- and alexa-
dye-labeled hongotoxin(1) analogues. The first high affinity
fluorescence probes for voltage-gated K+ channels.";
Bioconj. Chem. 13:416-425(2002).
-!- FUNCTION: Potent selective inhibitor of Kv1.1/KCNA1, Kv1.2/KCNA2,
Kv1.3/KCNA3 voltage-gated potassium channels. Weak inhibitor of
Kv1.6/KCNA6 potassium channel. {ECO:0000269|PubMed:9446567}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9446567}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:9446567}.
-!- DOMAIN: Has the structural arrangement of an alpha-helix connected
to a beta-sheet by disulfide bonds (CSalpha/beta).
{ECO:0000269|PubMed:12009929}.
-!- MASS SPECTROMETRY: Mass=4219; Method=Electrospray; Range=1-39;
Evidence={ECO:0000269|PubMed:12009929};
-!- MISCELLANEOUS: Does not block Kv1.4/KCNA4 and Kv1.5/KCNA5
currents. {ECO:0000269|PubMed:9446567}.
-!- SIMILARITY: Belongs to the short scorpion toxin superfamily.
Potassium channel inhibitor family. Alpha-KTx 02 subfamily.
{ECO:0000305}.
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PDB; 1HLY; NMR; -; A=1-39.
PDBsum; 1HLY; -.
ProteinModelPortal; P59847; -.
SMR; P59847; -.
EvolutionaryTrace; P59847; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
Gene3D; 3.30.30.10; -; 1.
InterPro; IPR036574; Scorpion_toxin-like_sf.
InterPro; IPR001947; Scorpion_toxinS_K_inh.
Pfam; PF00451; Toxin_2; 1.
PRINTS; PR00286; CHARYBDTOXIN.
ProDom; PD003586; Scorpion_toxinS; 1.
SUPFAM; SSF57095; SSF57095; 1.
PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Secreted; Toxin;
Voltage-gated potassium channel impairing toxin.
PEPTIDE 1 39 Potassium channel toxin alpha-KTx 2.5.
{ECO:0000269|PubMed:9446567}.
/FTId=PRO_0000044903.
SITE 28 28 Basic residue of the functional dyad.
{ECO:0000250}.
SITE 37 37 Aromatic residue of the functional dyad.
{ECO:0000250}.
DISULFID 7 29 {ECO:0000269|PubMed:12009929}.
DISULFID 13 34 {ECO:0000269|PubMed:12009929}.
DISULFID 17 36 {ECO:0000269|PubMed:12009929}.
MUTAGEN 19 19 A->C: No loss of activity.
{ECO:0000269|PubMed:12009929}.
MUTAGEN 19 19 A->Y: No loss of activity; when
associated with F-37.
{ECO:0000269|PubMed:12009929}.
MUTAGEN 37 37 Y->F: No loss of activity; when
associated with Y-19.
{ECO:0000269|PubMed:12009929}.
STRAND 8 10 {ECO:0000244|PDB:1HLY}.
HELIX 11 13 {ECO:0000244|PDB:1HLY}.
HELIX 14 20 {ECO:0000244|PDB:1HLY}.
STRAND 26 30 {ECO:0000244|PDB:1HLY}.
STRAND 33 37 {ECO:0000244|PDB:1HLY}.
SEQUENCE 39 AA; 4226 MW; B4ABC83F8EE7E637 CRC64;
TVIDVKCTSP KQCLPPCKAQ FGIRAGAKCM NGKCKCYPH


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