KBX1_TITSE
ID KBX1_TITSE Reviewed; 87 AA.
AC P69940; A0A7S8MV52;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Potassium channel toxin TsTXK-beta;
DE Short=TsTXKbeta;
DE AltName: Full=Potassium channel toxin beta-KTx 1;
DE AltName: Full=Tityustoxin K-beta;
DE Short=TsTX K beta;
DE Short=TsTX-K beta;
DE AltName: Full=Tityustoxin-8 {ECO:0000305};
DE Short=Ts8 {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:27346450};
DE AltName: Full=TsK2;
DE Flags: Precursor;
OS Tityus serrulatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=6887;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11072047; DOI=10.1016/s0041-0101(00)00194-x;
RA Kalapothakis E., Jardim S., Magalhaes A.C., Mendes T.M., De Marco L.,
RA Afonso L.C.C., Chavez-Olortegui C.;
RT "Screening of expression libraries using ELISA: identification of
RT immunogenic proteins from Tityus bahiensis and Tityus serrulatus venom.";
RL Toxicon 39:679-685(2001).
RN [2] {ECO:0000312|EMBL:QPD99047.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Telson;
RX PubMed=33181162; DOI=10.1016/j.toxicon.2020.11.001;
RA Kalapothakis Y., Miranda K., Pereira A.H., Witt A.S.A., Marani C.,
RA Martins A.P., Leal H.G., Campos-Junior E., Pimenta A.M.C., Borges A.,
RA Chavez-Olortegui C., Kalapothakis E.;
RT "Novel components of Tityus serrulatus venom: a transcriptomic approach.";
RL Toxicon 189:91-104(2021).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-87, AND MASS SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=9714546; DOI=10.1016/s0014-5793(98)00780-7;
RA Legros C., Ceard B., Bougis P.E., Martin-Eauclaire M.-F.;
RT "Evidence for a new class of scorpion toxins active against K+ channels.";
RL FEBS Lett. 431:375-380(1998).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=18718845; DOI=10.1016/j.toxicon.2008.07.010;
RA Rates B., Ferraz K.K., Borges M.H., Richardson M., De Lima M.E.,
RA Pimenta A.M.;
RT "Tityus serrulatus venom peptidomics: assessing venom peptide diversity.";
RL Toxicon 52:611-618(2008).
RN [5]
RP PROTEIN SEQUENCE OF 28-72, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=7509073; DOI=10.1073/pnas.91.4.1475;
RA Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.;
RT "Tityustoxin K alpha blocks voltage-gated noninactivating K+ channels and
RT unblocks inactivating K+ channels blocked by alpha-dendrotoxin in
RT synaptosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1475-1479(1994).
RN [6]
RP ERRATUM OF PUBMED:7509073.
RA Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.;
RL Proc. Natl. Acad. Sci. U.S.A. 93:12051-12051(1996).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND BIOASSAY.
RX PubMed=27346450; DOI=10.1016/j.toxicon.2016.06.014;
RA Pucca M.B., Cerni F.A., Cordeiro F.A., Peigneur S., Cunha T.M., Tytgat J.,
RA Arantes E.C.;
RT "Ts8 scorpion toxin inhibits the Kv4.2 channel and produces nociception in
RT vivo.";
RL Toxicon 119:244-252(2016).
RN [8]
RP NOMENCLATURE.
RX PubMed=19689419; DOI=10.2174/092986609788923329;
RA Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.;
RT "Tityus serrulatus scorpion venom and toxins: an overview.";
RL Protein Pept. Lett. 16:920-932(2009).
CC -!- FUNCTION: Specifically blocks voltage-gated potassium channels
CC Kv4.2/KCND2. When measured at the peak current, the blocking effect of
CC this toxin is about 65% and shows an IC(50)=652 nM (PubMed:27346450).
CC However, when measured at a later moment of the depolarising test pulse
CC (500 ms), a 100% block of the current is observed with an IC(50)=313 nM
CC (PubMed:27346450). This may indicate a preference of the toxin for
CC binding the inactivated state of the channel. The inhibition is
CC completely reversible (PubMed:27346450). Using intraplantar injections
CC on rat, this toxin induces overt nociception (licking and lifting
CC behaviors) and decreases the mechanical nociceptive threshold
CC (hyperalgesia). Furthermore, the hyperalgesia is prolonged when
CC intrathecal injections are performed (PubMed:27346450).
CC {ECO:0000269|PubMed:27346450, ECO:0000269|PubMed:7509073}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18718845}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18718845}.
CC -!- MASS SPECTROMETRY: Mass=6716.15; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9714546};
CC -!- MISCELLANEOUS: It is not known if the sequenced fragment corresponding
CC to the propeptide is the result of the post-translational maturation
CC process, or if it has a biological activity of its own.
CC {ECO:0000305|PubMed:18718845}.
CC -!- MISCELLANEOUS: Does not inhibit voltage-gated sodium channels tested
CC (Nav1.2, Nav1.4, Nav1.6 and B.germanica BgNav) and most of the voltage-
CC gated potassium channels tested (Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5,
CC Kv1.6, Shaker, Kv2.1, Kv3.1, Kv7.1, Kv7.2, Kv7.4, Kv7.5, Kv10.1 and
CC hERG). No hemolysis and no pore-forming activities are induced by this
CC toxin. {ECO:0000269|PubMed:27346450}.
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC subfamily. {ECO:0000305}.
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DR EMBL; MT450711; QPD99047.1; -; mRNA.
DR AlphaFoldDB; P69940; -.
DR SMR; P69940; -.
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 InterPro; IPR029237; Long_scorpion_toxin.
DR Pfam; PF14866; Toxin_38; 1.
DR PROSITE; PS51862; BSPN_CSAB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000305|PubMed:7509073"
FT /id="PRO_0000035342"
FT CHAIN 28..87
FT /note="Potassium channel toxin TsTXK-beta"
FT /evidence="ECO:0000305|PubMed:11072047,
FT ECO:0000305|PubMed:33181162, ECO:0000305|PubMed:7509073"
FT /id="PRO_0000035343"
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"
SQ SEQUENCE 87 AA; 9729 MW; ADCA961D54841F62 CRC64;
MERKLALLLI LGMVTLASCG LREKHVQKLV ALIPNDQLRS ILKAVVHKVA KTQFGCPAYE
GYCNDHCNDI ERKDGECHGF KCKCAKD
