KAX2H_CENTE
ID KAX2H_CENTE Reviewed; 39 AA.
AC C0HJW5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Potassium channel toxin alpha-KTx 2.17 {ECO:0000303|PubMed:26921461};
DE AltName: Full=Toxin II.12.8 {ECO:0000303|PubMed:26921461};
OS Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=1028682 {ECO:0000303|PubMed:26921461};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP AMIDATION AT ILE-39.
RC TISSUE=Venom;
RX PubMed=26921461; DOI=10.1016/j.toxicon.2016.02.017;
RA Olamendi-Portugal T., Bartok A., Zamudio-Zuniga F., Balajthy A.,
RA Becerril B., Panyi G., Possani L.D.;
RT "Isolation, chemical and functional characterization of several new K(+)-
RT channel blocking peptides from the venom of the scorpion Centruroides
RT tecomanus.";
RL Toxicon 115:1-12(2016).
CC -!- FUNCTION: Blocks human voltage-gated potassium channels Kv1.1/KCNA1
CC (IC(50)=4.8 nM) and Kv1.2/KCNA2 (IC(50)=2.9 nM).
CC {ECO:0000269|PubMed:26921461}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26921461}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26921461}.
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=4211.9; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:26921461};
CC -!- MISCELLANEOUS: Does not block voltage-gated potassium channel
CC Kv1.3/KCNA3, intermediate conductance calcium-activated potassium
CC channel KCa3.1/KCNN4 or the Shaker IR (with inactivation domain
CC removed). {ECO:0000269|PubMed:26921461}.
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; C0HJW5; -.
DR SMR; C0HJW5; -.
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 PEPTIDE 1..39
FT /note="Potassium channel toxin alpha-KTx 2.17"
FT /evidence="ECO:0000269|PubMed:26921461"
FT /id="PRO_0000436538"
FT SITE 28
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250|UniProtKB:O46028"
FT MOD_RES 39
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250|UniProtKB:P0C165,
FT ECO:0000305|PubMed:26921461"
FT DISULFID 7..29
FT /evidence="ECO:0000250|UniProtKB:O46028"
FT DISULFID 13..34
FT /evidence="ECO:0000250|UniProtKB:O46028"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:O46028"
SQ SEQUENCE 39 AA; 4218 MW; E319ACAE23F3BE10 CRC64;
TIINVKCTSP KQCLLPCKQI YGPHAGAKCM NGKCHCSKI
