KA231_VAEMS
ID KA231_VAEMS Reviewed; 36 AA.
AC P0DJ31;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Potassium channel toxin alpha-KTx 23.1 {ECO:0000303|PubMed:22540187, ECO:0000303|PubMed:22622363};
DE AltName: Full=Toxin Vm24 {ECO:0000303|PubMed:22540187, ECO:0000303|PubMed:22622363};
DE AltName: Full=Toxin alpha-KTx 21.1;
OS Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Chactoidea; Vaejovidae; Vaejovis.
OX NCBI_TaxID=1562928;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, DISULFIDE BONDS, AMIDATION AT
RP CYS-36, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Possani L.D., Gurrola G.B., Salas-Castillo S.P., Batista C.V.F., Varga Z.,
RA Panyi G., Caspar R.;
RT "Vm23 and Vm24, two scorpion peptides that block human T-lymphocyte
RT potassium channels sub-type K(v)1.3 w/high selectivity and decrease the in
RT vivo DTH responses in rats.";
RL Patent number US0059064, 10-MAR-2011.
RN [2]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, DISULFIDE BONDS, AMIDATION AT
RP CYS-36, MASS SPECTROMETRY, STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND
RP NOMENCLATURE.
RC TISSUE=Venom;
RX PubMed=22540187; DOI=10.1021/bi300060n;
RA Gurrola G.B., Hernandez-Lopez R.A., Rodriguez de la Vega R.C., Varga Z.,
RA Batista C.V.F., Salas-Castillo S.P., Panyi G., del Rio-Portilla F.,
RA Possani L.D.;
RT "Structure, function, and chemical synthesis of vaejovis mexicanus peptide
RT 24: a novel potent blocker of Kv1.3 potassium channels of human T
RT lymphocytes.";
RL Biochemistry 51:4049-4061(2012).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RC TISSUE=Venom;
RX PubMed=22622363; DOI=10.1124/mol.112.078006;
RA Varga Z., Gurrola-Briones G., Papp F., Rodriguez de la Vega R.C.,
RA Pedraza-Alva G., Tajhya R.B., Gaspar R., Cardenas L., Rosenstein Y.,
RA Beeton C., Possani L.D., Panyi G.;
RT "Vm24, a natural immunosuppressant peptide potently and selectively blocks
RT Kv1.3 potassium channels of human T Cells.";
RL Mol. Pharmacol. 82:372-382(2012).
CC -!- FUNCTION: Selectively and irreversibly binds (K(d)=2.9 pM) and blocks
CC hKv1.3/KCNA3 potassium channels of human T-lymphocytes. Weakly blocks
CC hKCa3.1/KCNN4, mKv1.1/KCNA1, and hKv1.2/KCNA2 channels. In vivo, high
CC doses (200 ug) produce no symptoms of intoxication when injected into
CC mice. {ECO:0000269|PubMed:22540187, ECO:0000269|PubMed:22622363,
CC ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22540187,
CC ECO:0000269|PubMed:22622363, ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22540187, ECO:0000305|PubMed:22622363,
CC ECO:0000305|Ref.1}.
CC -!- DOMAIN: Has the CSalpha/beta fold, which comprises one or two short
CC alpha helices connected to anti-parallel beta-sheets stabilized by
CC three or four disulfide bonds. {ECO:0000269|PubMed:22540187}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=3864.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22540187};
CC -!- MISCELLANEOUS: Does not block hKv1.4/KCNA4, hKv1.5/KCNA5, rKv2.1/KCNB1,
CC hBK, hERG, Nav1.5/SCN5A channels when assayed at a concentration of 10
CC nM. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 23 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 2K9O; NMR; -; A=1-36.
DR PDBsum; 2K9O; -.
DR AlphaFoldDB; P0DJ31; -.
DR BMRB; P0DJ31; -.
DR SMR; P0DJ31; -.
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 3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Secreted; Toxin.
FT CHAIN 1..36
FT /note="Potassium channel toxin alpha-KTx 23.1"
FT /evidence="ECO:0000269|PubMed:22540187, ECO:0000269|Ref.1"
FT /id="PRO_0000415929"
FT SITE 25
FT /note="Basic residue of the functional dyad"
FT SITE 34
FT /note="Aromatic residue of the functional dyad"
FT MOD_RES 36
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:22540187, ECO:0000269|Ref.1"
FT DISULFID 6..26
FT /evidence="ECO:0000269|PubMed:22540187,
FT ECO:0000312|PDB:2K9O"
FT DISULFID 12..31
FT /evidence="ECO:0000269|PubMed:22540187,
FT ECO:0000312|PDB:2K9O"
FT DISULFID 16..33
FT /evidence="ECO:0000269|PubMed:22540187,
FT ECO:0000312|PDB:2K9O"
FT DISULFID 21..36
FT /evidence="ECO:0000269|PubMed:22540187,
FT ECO:0000312|PDB:2K9O"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2K9O"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2K9O"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:2K9O"
FT STRAND 22..34
FT /evidence="ECO:0007829|PDB:2K9O"
SQ SEQUENCE 36 AA; 3873 MW; D7A77050D7902995 CRC64;
AAAISCVGSP ECPPKCRAQG CKNGKCMNRK CKCYYC
