KAX29_CENEL
ID KAX29_CENEL Reviewed; 39 AA.
AC P0C162;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Potassium channel toxin alpha-KTx 2.9;
DE AltName: Full=Toxin Ce2 {ECO:0000303|PubMed:16026809};
OS Centruroides elegans (Bark scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=217897;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP AMIDATION AT ASN-39, AND ACTIVITY PROFILE.
RC TISSUE=Venom;
RX PubMed=16026809; DOI=10.1016/j.toxicon.2005.06.001;
RA Olamendi-Portugal T., Somodi S., Fernandez J.A., Zamudio F.Z., Becerril B.,
RA Varga Z., Panyi G., Gaspar R., Possani L.D.;
RT "Novel alpha-KTx peptides from the venom of the scorpion Centruroides
RT elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells.";
RL Toxicon 46:418-429(2005).
CC -!- FUNCTION: Blocks Kv1.3/KCNA3 voltage-gated potassium channels of human
CC T-lymphocytes (Kd=0.25 nM). {ECO:0000269|PubMed:16026809}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16026809}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16026809}.
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:P08815}.
CC -!- MASS SPECTROMETRY: Mass=4267; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16026809};
CC -!- MISCELLANEOUS: Does not inhibit calcium-activated potassium channels
CC (KCa3.1/KCNN4) of human T-lymphocytes. Does not inhibit voltage-gated
CC Shaker potassium channels. Does not inhibit Kv2.1/KCNB1 potassium
CC channels. {ECO:0000269|PubMed:16026809}.
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; P0C162; -.
DR SMR; P0C162; -.
DR PRIDE; P0C162; -.
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 Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..39
FT /note="Potassium channel toxin alpha-KTx 2.9"
FT /evidence="ECO:0000269|PubMed:16026809"
FT /id="PRO_0000226959"
FT SITE 28
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:16026809"
FT DISULFID 7..29
FT /evidence="ECO:0000250|UniProtKB:P08815"
FT DISULFID 13..34
FT /evidence="ECO:0000250|UniProtKB:P08815"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P08815"
SQ SEQUENCE 39 AA; 4274 MW; E07EA5488C920E10 CRC64;
TIINVKCTSP KQCLKPCKDL YGPHAGAKCM NGKCKCYNN
