KAX2D_CENSU
ID KAX2D_CENSU Reviewed; 38 AA.
AC P85529;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Potassium channel toxin alpha-KTx 2.13 {ECO:0000303|PubMed:18786511};
DE AltName: Full=Toxin Css20 {ECO:0000303|PubMed:18786511};
OS Centruroides suffusus (Durango bark scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6880;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP ACTIVITY PROFILE.
RC TISSUE=Venom;
RX PubMed=18786511; DOI=10.1016/j.bcp.2008.08.018;
RA Corzo G., Papp F., Varga Z., Barraza O., Espino-Solis P.G.,
RA Rodriguez de la Vega R.C., Gaspar R., Panyi G., Possani L.D.;
RT "A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venom
RT of the scorpion Centruroides suffusus suffusus.";
RL Biochem. Pharmacol. 76:1142-1154(2008).
CC -!- FUNCTION: Selective inhibitor of voltage-gated potassium channels,
CC blocks the Kv1.2/KCNA2 (Kd=1.3 nM) and Kv1.3/KCNA3 (Kd=7.2 nM)
CC channels. Association and dissociation rates of the toxin are slower
CC for Kv1.2/KCNA2 than for Kv1.3/KCNA3. {ECO:0000269|PubMed:18786511}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18786511}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18786511}.
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:P40755}.
CC -!- MASS SPECTROMETRY: Mass=4000.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18786511};
CC -!- MISCELLANEOUS: Does not inhibit the potassium channels Kv1.1/KCNA1,
CC Kv1.4/KCNA4, Kv1.5/KCNA5, Kv2.1/KCNB1, Kv11.1/KCNH2, KCa3.1/KCNN4,
CC KCa1.1/KCNMA1 and the sodium channel Nav1.5/SCN5A.
CC {ECO:0000305|PubMed:18786511}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 02 subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P85529; -.
DR SMR; P85529; -.
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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT PEPTIDE 1..38
FT /note="Potassium channel toxin alpha-KTx 2.13"
FT /evidence="ECO:0000269|PubMed:18786511"
FT /id="PRO_0000358604"
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 DISULFID 7..29
FT /evidence="ECO:0000250|UniProtKB:P40755"
FT DISULFID 13..34
FT /evidence="ECO:0000250|UniProtKB:P40755"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P40755"
SQ SEQUENCE 38 AA; 4007 MW; 73672C2B221D74A2 CRC64;
IFINVKCSSP QQCLKPCKAA FGISAGGKCI NGKCKCYP
