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Potassium channel toxin TsTXK-beta (Potassium channel toxin beta-KTx 1) (Tityustoxin K-beta) (TsTX K beta) (TsTX-K beta) (TsTXKbeta) (Ts8) (TsK2)

 KBX1_TITSE              Reviewed;          87 AA.
P69940;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
20-JUN-2018, entry version 45.
RecName: Full=Potassium channel toxin TsTXK-beta;
AltName: Full=Potassium channel toxin beta-KTx 1;
AltName: Full=Tityustoxin K-beta;
Short=TsTX K beta;
Short=TsTX-K beta;
Short=TsTXKbeta;
AltName: Full=Ts8 {ECO:0000303|PubMed:27346450};
AltName: Full=TsK2;
Flags: Precursor;
Tityus serrulatus (Brazilian scorpion).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
NCBI_TaxID=6887;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=11072047; DOI=10.1016/S0041-0101(00)00194-X;
Kalapothakis E., Jardim S., Magalhaes A.C., Mendes T.M., De Marco L.,
Afonso L.C.C., Chavez-Olortegui C.;
"Screening of expression libraries using ELISA: identification of
immunogenic proteins from Tityus bahiensis and Tityus serrulatus
venom.";
Toxicon 39:679-685(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-87, AND MASS SPECTROMETRY.
TISSUE=Venom gland;
PubMed=9714546; DOI=10.1016/S0014-5793(98)00780-7;
Legros C., Ceard B., Bougis P.E., Martin-Eauclaire M.-F.;
"Evidence for a new class of scorpion toxins active against K+
channels.";
FEBS Lett. 431:375-380(1998).
[3]
PROTEIN SEQUENCE OF 20-47, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=18718845; DOI=10.1016/j.toxicon.2008.07.010;
Rates B., Ferraz K.K., Borges M.H., Richardson M., De Lima M.E.,
Pimenta A.M.;
"Tityus serrulatus venom peptidomics: assessing venom peptide
diversity.";
Toxicon 52:611-618(2008).
[4]
PROTEIN SEQUENCE OF 28-72, AND FUNCTION.
TISSUE=Venom;
PubMed=7509073; DOI=10.1073/pnas.91.4.1475;
Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.;
"Tityustoxin K alpha blocks voltage-gated noninactivating K+ channels
and unblocks inactivating K+ channels blocked by alpha-dendrotoxin in
synaptosomes.";
Proc. Natl. Acad. Sci. U.S.A. 91:1475-1479(1994).
[5]
ERRATUM.
Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.;
Proc. Natl. Acad. Sci. U.S.A. 93:12051-12051(1996).
[6]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND BIOASSAY.
PubMed=27346450; DOI=10.1016/j.toxicon.2016.06.014;
Pucca M.B., Cerni F.A., Cordeiro F.A., Peigneur S., Cunha T.M.,
Tytgat J., Arantes E.C.;
"Ts8 scorpion toxin inhibits the Kv4.2 channel and produces
nociception in vivo.";
Toxicon 119:244-252(2016).
[7]
NOMENCLATURE.
PubMed=19689419; DOI=10.2174/092986609788923329;
Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.;
"Tityus serrulatus scorpion venom and toxins: an overview.";
Protein Pept. Lett. 16:920-932(2009).
-!- FUNCTION: Specifically blocks voltage-gated potassium channels
Kv4.2/KCND2. When measured at the peak current, the blocking
effect of this toxin is about 65% and shows an IC(50)=652 nM
(PubMed:27346450). However, when measured at a later moment of the
depolarising test pulse (500 ms), a 100% block of the current is
observed with an IC(50)=313 nM (PubMed:27346450). This may
indicate a preference of the toxin for binding the inactivated
state of the channel. The inhibition is completely reversible
(PubMed:27346450). Using intraplantar injections on rat, this
toxin induces overt nociception (licking and lifting behaviors)
and decreases the mechanical nociceptive threshold (hyperalgesia).
Furthermore, the hyperalgesia is prolonged when intrathecal
injections are performed (PubMed:27346450).
{ECO:0000269|PubMed:27346450, ECO:0000269|PubMed:7509073}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18718845}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- MASS SPECTROMETRY: Mass=6716.15; Method=Electrospray; Range=26-85;
Evidence={ECO:0000269|PubMed:9714546};
-!- MISCELLANEOUS: It is not known if the sequenced fragment
corresponding to the propeptide is the result of the post-
translational maturation process, or if it has a biological
activity of its own. {ECO:0000305|PubMed:18718845}.
-!- MISCELLANEOUS: Does not inhibit voltage-gated sodium channels
tested (Nav1.2, Nav1.4, Nav1.6 and B.germanica BgNav) and most of
the voltage-gated potassium channels tested (Kv1.1, Kv1.2, Kv1.3,
Kv1.4, Kv1.5, Kv1.6, Shaker, Kv2.1, Kv3.1, Kv7.1, Kv7.2, Kv7.4,
Kv7.5, Kv10.1 and hERG). No hemolysis and no pore-forming
activities are induced by this toxin.
{ECO:0000269|PubMed:27346450}.
-!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class
1 subfamily. {ECO:0000305}.
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SMR; P69940; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR029237; Long_scorpion_toxin.
Pfam; PF14866; Toxin_38; 1.
PROSITE; PS51862; BSPN_CSAB; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Secreted; Signal; Toxin;
Voltage-gated potassium channel impairing toxin.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 27 {ECO:0000305|PubMed:7509073}.
/FTId=PRO_0000035342.
CHAIN 28 87 Potassium channel toxin TsTXK-beta.
/FTId=PRO_0000035343.
DOMAIN 53 87 BetaSPN-type CS-alpha/beta.
{ECO:0000255|PROSITE-ProRule:PRU01209}.
DISULFID 56 77 {ECO:0000255|PROSITE-ProRule:PRU01209}.
DISULFID 63 82 {ECO:0000255|PROSITE-ProRule:PRU01209}.
DISULFID 67 84 {ECO:0000255|PROSITE-ProRule:PRU01209}.
SEQUENCE 87 AA; 9729 MW; ADCA961D54841F62 CRC64;
MERKLALLLI LGMVTLASCG LREKHVQKLV ALIPNDQLRS ILKAVVHKVA KTQFGCPAYE
GYCNDHCNDI ERKDGECHGF KCKCAKD


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