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KTX21_TITSE
ID   KTX21_TITSE             Reviewed;          65 AA.
AC   A0A218QXT6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Putative potassium channel toxin Ts21 {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Putative KTx {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Tityustoxin-21 {ECO:0000305};
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:JAW06975.1}
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:QPD99054.1}
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).
CC   -!- FUNCTION: This recombinant toxin inhibits the mammalian voltage-gated
CC       potassium channels Kv1.3/KCNA3 in vitro with an IC(50) of 26.40 nM.
CC       {ECO:0000250|UniProtKB:A9QLM3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29561852,
CC       ECO:0000305|PubMed:33181162}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29561852, ECO:0000305|PubMed:33181162}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000250|UniProtKB:A9QLM3}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 11 subfamily. {ECO:0000305}.
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DR   EMBL; GEUW01000070; JAW06975.1; -; mRNA.
DR   EMBL; MT450718; QPD99054.1; -; mRNA.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..65
FT                   /note="Putative potassium channel toxin Ts21"
FT                   /id="PRO_5013370101"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        38..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   65 AA;  6710 MW;  50895457FDD839D1 CRC64;
     MNKVYLVAIL VLSVLLVANV SPIEGVPTGG CPLSDALCAK YCKSNKYGKT GKCTGTSKGT
     CKCLV
 
 
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