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KAX85_ODODO
ID   KAX85_ODODO             Reviewed;          57 AA.
AC   P0CC12; A0A0U4I1L0;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Potassium channel toxin alpha-KTx 8.5 {ECO:0000305};
DE   AltName: Full=OdK1 {ECO:0000303|PubMed:17070524};
DE   AltName: Full=Potassium channel toxin KTx7 {ECO:0000312|EMBL:ALX72349.1};
DE            Short=ODKTx7 {ECO:0000312|EMBL:ALX72349.1};
DE   Flags: Precursor;
OS   Odontobuthus doriae (Yellow Iranian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Odontobuthus.
OX   NCBI_TaxID=342590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Soorki M.N., Galehdari H., Jalali A., Baradaran M.;
RT   "First venom gland transcriptomic analysis of Iranian yellow scorpion
RT   'Odonthubuthus doriae'.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 29-57, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17070524; DOI=10.1016/j.febslet.2006.10.029;
RA   Abdel-Mottaleb Y., Clynen E., Jalali A., Bosmans F., Vatanpour H.,
RA   Schoofs L., Tytgat J.;
RT   "The first potassium channel toxin from the venom of the Iranian scorpion
RT   Odonthobuthus doriae.";
RL   FEBS Lett. 580:6254-6258(2006).
CC   -!- FUNCTION: Selectively inhibits voltage-gated potassium channels
CC       Kv1.2/KCNA2 (IC(50)=183 nM). {ECO:0000269|PubMed:17070524}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17070524}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17070524}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:P80671}.
CC   -!- MASS SPECTROMETRY: Mass=3180.12; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17070524};
CC   -!- MISCELLANEOUS: This toxin does not affect Kv1.1/KCNA1, Kv1.3/KCNA3,
CC       Kv1.4/KCNA4, Kv1.5/KCNA5 and Shaker IR. {ECO:0000305|PubMed:17070524}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 08 subfamily. {ECO:0000305}.
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DR   EMBL; KU365851; ALX72349.1; -; mRNA.
DR   AlphaFoldDB; P0CC12; -.
DR   SMR; P0CC12; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044361; P:negative regulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR008911; Toxin_alpha-KTx_8/9.
DR   Pfam; PF05453; Toxin_6; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:17070524"
FT   PEPTIDE         29..57
FT                   /note="Potassium channel toxin alpha-KTx 8.5"
FT                   /evidence="ECO:0000269|PubMed:17070524"
FT                   /id="PRO_0000390674"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P80671"
FT   DISULFID        34..52
FT                   /evidence="ECO:0000250|UniProtKB:P80671"
FT   DISULFID        38..54
FT                   /evidence="ECO:0000250|UniProtKB:P80671"
SQ   SEQUENCE   57 AA;  6289 MW;  3C1DE8B38AB6340E CRC64;
     MSRLYAIILI ALVLNVIMTI MPDSKVEAVS CEDCPEHCST QKARAKCDND KCVCESV
 
 
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