KAX27_CENLI
ID KAX27_CENLI Reviewed; 36 AA.
AC P45630;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Potassium channel toxin alpha-KTx 2.7;
DE AltName: Full=C.1.limpidus toxin 2 {ECO:0000303|PubMed:7998956};
DE Short=CllTx2 {ECO:0000303|PubMed:7998956};
DE AltName: Full=Toxin II.10.9.2 {ECO:0000303|PubMed:7998956};
DE Flags: Fragment;
OS Centruroides limpidus (Mexican scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6876;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=7998956; DOI=10.1042/bj3040051;
RA Martin B.M., Ramirez A.N., Gurrola G.B., Nobile M., Prestipino G.,
RA Possani L.D.;
RT "Novel K(+)-channel-blocking toxins from the venom of the scorpion
RT Centruroides limpidus limpidus Karsch.";
RL Biochem. J. 304:51-56(1994).
CC -!- FUNCTION: Inhibitor of voltage-gated potassium channels (Kv). This
CC protein is capable of displacing the binding of radio-labeled
CC noxiustoxin (AC P08815) to rat brain synaptosomes with high affinity
CC (about 100 pM). It is also capable of inhibiting transient potassium-
CC currents (resembling I(A)-type currents), in cultured rat cerebellar
CC granule cells. About 50% of the peak currents are reduced by
CC application of a 1.5 uM solution of this toxin. Is lethal to mice (when
CC less than 100 ug are injected). {ECO:0000269|PubMed:7998956}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7998956}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7998956}.
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:P59847}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 02 subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P45630; -.
DR SMR; P45630; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR Pfam; PF00451; Toxin_2; 1.
DR PRINTS; PR00286; CHARYBDTOXIN.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE 1: Evidence at protein level;
KW Calcium-activated potassium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin.
FT CHAIN 1..>36
FT /note="Potassium channel toxin alpha-KTx 2.7"
FT /id="PRO_0000066832"
FT SITE 28
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT DISULFID 7..29
FT /evidence="ECO:0000250|UniProtKB:P59847"
FT DISULFID 13..34
FT /evidence="ECO:0000250|UniProtKB:P59847"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P59847"
FT NON_TER 36
SQ SEQUENCE 36 AA; 3912 MW; C0350A262B6730C1 CRC64;
TVIDVKCTSP KQCLPPCKEI YGRHAGAKCM NGKCKC