KEX11_TITSE
ID KEX11_TITSE Reviewed; 72 AA.
AC P0C174; A0A218QX37; A0A218QX98;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Potassium channel toxin epsilon-KTx 1.1 {ECO:0000303|PubMed:27706049};
DE AltName: Full=Tityustoxin-11 {ECO:0000305};
DE Short=Ts11 {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:27706049};
DE AltName: Full=TsPep1 {ECO:0000303|PubMed:27706049};
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] {ECO:0000312|EMBL:JAW06973.1, ECO:0000312|EMBL:JAW07010.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Telson;
RX PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT obscurus and T. serrulatus scorpions.";
RL PLoS ONE 13:e0193739-e0193739(2018).
RN [2] {ECO:0000312|EMBL:QPD99049.1}
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 31-59, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=12589824; DOI=10.1016/s0006-291x(03)00082-2;
RA Pimenta A.M.C., Legros C., Almeida F.M., Mansuelle P., De Lima M.E.,
RA Bougis P.E., Martin-Eauclaire M.-F.;
RT "Novel structural class of four disulfide-bridged peptides from Tityus
RT serrulatus venom.";
RL Biochem. Biophys. Res. Commun. 301:1086-1092(2003).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, STRUCTURE BY NMR OF 31-59, DISULFIDE
RP BOND, MASS SPECTROMETRY, AND NOMENCLATURE.
RC TISSUE=Venom;
RX PubMed=27706049; DOI=10.3390/toxins8100288;
RA Cremonez C.M., Maiti M., Peigneur S., Cassoli J.S., Dutra A.A.,
RA Waelkens E., Lescrinier E., Herdewijn P., de Lima M.E., Pimenta A.M.,
RA Arantes E.C., Tytgat J.;
RT "Structural and functional elucidation of peptide Ts11 shows evidence of a
RT novel subfamily of scorpion venom toxins.";
RL Toxins 8:1-14(2016).
RN [5]
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: Potassium channel blocker. At 3 uM, this toxin blocks
CC voltage-independently voltage-gated potassium channels rKv1.2/KCNA2
CC (25%), hKv1.3/KCNA3 (27%), rKv4.2/KCND2 (25%), Kv10.1/KCNH1/EAG1 (15%),
CC Kv11/hERG (12%), and Shaker-IR (10%). On hKv1.3/KCNA3, the IC(50) is
CC 17.1 +-3.3 uM. {ECO:0000269|PubMed:27706049}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12589824,
CC ECO:0000269|PubMed:27706049}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000305|PubMed:27706049}.
CC -!- DOMAIN: Is completely devoid of the classical secondary structure
CC elements (alpha-helix and/or beta-strand).
CC {ECO:0000305|PubMed:27706049}.
CC -!- MASS SPECTROMETRY: Mass=2938.92; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12589824};
CC -!- MASS SPECTROMETRY: Mass=2938.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27706049};
CC -!- MISCELLANEOUS: Does not block all sodium channels tested and several
CC potassium channels. Does not block the following voltage-gated
CC potassium channels: rKv1.1/KCNA1, rKv1.1/KCNA1, rKv1.5/KCNA5,
CC rKv1.6/KCNA6, rKv2.1/KCNB1, hKv3.1/KCNC1, and Kv7.2/KCNQ2. Does not
CC block the following voltage-gated sodium channels: rNav1.1/SCN1A,
CC rNav1.4/SCN4A, hNav1.5/SCN5A, mNav1.6/SCN8A, and DmNav1/para.
CC {ECO:0000269|PubMed:27706049}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Epsilon-KTx 01 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=JAW06973.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GEUW01000035; JAW07010.1; -; mRNA.
DR EMBL; GEUW01000072; JAW06973.1; ALT_INIT; mRNA.
DR EMBL; MT450713; QPD99049.1; -; mRNA.
DR PDB; 2MSF; NMR; -; A=31-59.
DR PDBsum; 2MSF; -.
DR AlphaFoldDB; P0C174; -.
DR BMRB; P0C174; -.
DR SMR; P0C174; -.
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; IPR036574; Scorpion_toxin-like_sf.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Potassium channel impairing toxin;
KW Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..30
FT /evidence="ECO:0000305|PubMed:12589824,
FT ECO:0000305|PubMed:27706049"
FT PEPTIDE 31..59
FT /note="Potassium channel toxin epsilon-KTx 1.1"
FT /evidence="ECO:0000269|PubMed:12589824,
FT ECO:0000269|PubMed:27706049"
FT /id="PRO_0000227819"
FT PROPEP 60..72
FT /evidence="ECO:0000305|PubMed:12589824,
FT ECO:0000305|PubMed:27706049"
FT /id="PRO_0000455731"
FT DISULFID 34..42
FT /evidence="ECO:0000269|PubMed:27706049,
FT ECO:0007744|PDB:2MSF"
FT DISULFID 37..58
FT /evidence="ECO:0000269|PubMed:27706049,
FT ECO:0007744|PDB:2MSF"
FT DISULFID 41..51
FT /evidence="ECO:0000269|PubMed:27706049,
FT ECO:0007744|PDB:2MSF"
FT DISULFID 46..56
FT /evidence="ECO:0000269|PubMed:27706049,
FT ECO:0007744|PDB:2MSF"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2MSF"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2MSF"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2MSF"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2MSF"
SQ SEQUENCE 72 AA; 7721 MW; 11E25A587EF2FB0E CRC64;
MKLSCGFLLI LLVLSAMIAT FSEVEAMKPS KPKCGLCRYR CCSGGCSSGK CVNGACDCSG
RSDLNDELEK YQ
