KBX2_TITSE
ID KBX2_TITSE Reviewed; 91 AA.
AC P86822; A0A7S8MV80; P86823;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Tityustoxin-19 {ECO:0000305|Ref.1};
DE Short=Ts19 {ECO:0000303|Ref.1};
DE AltName: Full=Potassium channel toxin beta-Ktx 2 {ECO:0000303|PubMed:18718845};
DE Contains:
DE RecName: Full=Ts19 fragment I {ECO:0000303|Ref.3};
DE AltName: Full=Potassium channel toxin beta-Ktx 2-1 {ECO:0000305|Ref.3};
DE Contains:
DE RecName: Full=Ts19 fragment II {ECO:0000303|PubMed:26116782, ECO:0000303|Ref.3};
DE Short=Ts19 Frag-II {ECO:0000303|PubMed:26116782};
DE AltName: Full=Potassium channel toxin beta-Ktx 2-2 {ECO:0000305|Ref.3};
DE Contains:
DE RecName: Full=Ts19 fragment III {ECO:0000303|PubMed:26116782};
DE Short=Ts19 Frag-III {ECO:0000303|PubMed:26116782};
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 DOI=10.4236/ojgen.2012.24027;
RA Alvarenga E.R., Mendes T.M., Magalhaes B.F., Siqueira F.F., Dantas A.E.,
RA Barroca T.M., Horta C.C., Kalapothakis E.;
RT "Transcriptome analysis of the Tityus serrulatus scorpion venom gland.";
RL O. J. Gen. 2:210-220(2012).
RN [2] {ECO:0000312|EMBL:QPD99052.1}
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 PROTEIN SEQUENCE OF 34-90, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Cerni F.A., Amorim F.G., Bordon K.C.F., Arantes E.C.;
RT "Isolation and electrophysiological characterization of a new potassium
RT channel blocker from Tityus serrulatus venom.";
RL Submitted (FEB-2013) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 43-91, SYNTHESIS OF 34-42, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=26116782; DOI=10.1016/j.peptides.2015.06.004;
RA Cerni F.A., Pucca M.B., Amorim F.G., de Castro Figueiredo Bordon K.,
RA Echterbille J., Quinton L., De Pauw E., Peigneur S., Tytgat J.,
RA Arantes E.C.;
RT "Isolation and characterization of Ts19 Fragment II, a new long-chain
RT potassium channel toxin from Tityus serrulatus venom.";
RL Peptides 80:9-17(2016).
RN [5]
RP PROTEIN SEQUENCE OF 26-52, 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 [6]
RP PROTEIN SEQUENCE OF 42-63, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=25199494; DOI=10.1016/j.toxicon.2014.08.064;
RA Pucca M.B., Amorim F.G., Cerni F.A., Bordon K.C.F., Cardoso I.A.,
RA Anjolette F.A., Arantes E.C.;
RT "Influence of post-starvation extraction time and prey-specific diet in
RT Tityus serrulatus scorpion venom composition and hyaluronidase activity.";
RL Toxicon 90:326-336(2014).
CC -!- FUNCTION: [Ts19 fragment I]: May function as a voltage-gated potassium
CC channel blocker and may have cytolytic activity (Ref.3). However, it is
CC noteworthy that the toxin often disappears from the venom fractions
CC tested. Hence, the toxin may be frequently processed in the venom,
CC which justifies the absence of Ts19 Frag-I among different venom
CC samples (PubMed:26116782). {ECO:0000269|Ref.3,
CC ECO:0000305|PubMed:26116782}.
CC -!- FUNCTION: [Ts19 fragment II]: Specific and reversible blocker of
CC Kv1.2/KCNA2 (IC(50)=544 nM). {ECO:0000269|PubMed:26116782}.
CC -!- FUNCTION: [Ts19 fragment III]: Shows cytolytic effects on erythrocytes.
CC In addition, induces non-selective pores formation when high
CC concentrations (300 nM) are applied on oocytes.
CC {ECO:0000269|PubMed:26116782}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18718845,
CC ECO:0000269|PubMed:25199494, ECO:0000269|PubMed:26116782,
CC ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18718845}.
CC -!- MISCELLANEOUS: [Ts19 fragment II]: Does not show inhibiting activities
CC on most potassium channels tested and on all sodium channels tested.
CC Here is the list of all channels that are not inhibited by the toxin:
CC Kv1.1/KCNA1, Kv1.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5, Kv1.6/KCNA6,
CC Kv2.1/KCNB1, Kv3.1/KCNC1, Kv4.2/KCND2, Kv7.1/KCNQ1, Kv7.2/KCNQ2,
CC Kv7.4/KCNQ4, Kv7.5/KCNA5, Kv10.1/KCNH1/EAG1, Kv11.1/KCNH2/ERG1,
CC Shaker/Sh, Nav1.2/SCN2A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, and
CC B.germanica Nav. {ECO:0000269|PubMed:26116782}.
CC -!- MISCELLANEOUS: [Ts19 fragment III]: Does not show blocking effet on
CC Kv1.2/KCNA2 potassium channels. {ECO:0000269|PubMed:26116782}.
CC -!- MISCELLANEOUS: The fragments 26-37, 34-42 and 43-52 described in
CC PubMed:18718845 correspond to the propeptide and some additional
CC residues of the chain. The authors do not know if these fragments are
CC the result of the post-translational maturation process, or if they
CC have a biological activity of their own. {ECO:0000305|PubMed:18718845}.
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC subfamily. {ECO:0000255}.
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DR EMBL; MT450716; QPD99052.1; -; mRNA.
DR AlphaFoldDB; P86822; -.
DR SMR; P86822; -.
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:0044179; P:hemolysis in 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 Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..33
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000422387"
FT PEPTIDE 34..90
FT /note="Ts19 fragment I"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000422388"
FT PEPTIDE 34..42
FT /note="Ts19 fragment III"
FT /evidence="ECO:0000269|PubMed:18718845"
FT /id="PRO_0000438647"
FT PEPTIDE 43..91
FT /note="Ts19 fragment II"
FT /evidence="ECO:0000269|PubMed:26116782, ECO:0000269|Ref.3"
FT /id="PRO_0000422389"
FT DOMAIN 58..91
FT /note="BetaSPN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 61..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 68..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT CONFLICT 61
FT /note="C -> W (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 91 AA; 10083 MW; 39EED225DA8C4589 CRC64;
MVATNRCCVF ALLFALLLVH SLTEAGKGKE ILGKIKEKII EAKDKMKAGW ERLTSQSEYA
CPAIDKFCED HCAAKKAVGK CDDFKCNCIK L
