KAX2J_RHOJU
ID KAX2J_RHOJU Reviewed; 37 AA.
AC C0HJT0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Potassium channel toxin alpha-KTx 2.19 {ECO:0000303|Ref.2};
DE AltName: Full=Peptide Rj1m2 {ECO:0000303|PubMed:26169670};
DE AltName: Full=Potassium channel toxin alpha-KTx 2.15 {ECO:0000303|PubMed:26169670};
OS Rhopalurus junceus (Caribbean blue scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Rhopalurus.
OX NCBI_TaxID=419285;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=26169670; DOI=10.1016/j.toxicon.2015.06.026;
RA Rodriguez-Ravelo R., Batista C.V., Coronas F.I., Zamudio F.Z.,
RA Hernandez-Orihuela L., Espinosa-Lopez G., Ruiz-Urquiola A., Possani L.D.;
RT "Comparative proteomic analysis of male and female venoms from the Cuban
RT scorpion Rhopalurus junceus.";
RL Toxicon 107:327-334(2015).
RN [2]
RP NOMENCLATURE.
RA Possani L.D.;
RL Submitted (NOV-2017) to UniProtKB.
CC -!- FUNCTION: Inhibitor of voltage-gated potassium channels.
CC {ECO:0000250|UniProtKB:P59847}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26169670}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26169670}.
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=3944.89; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:26169670};
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 02 subfamily. {ECO:0000305}.
CC -!- CAUTION: According to mail exchange with L.D. Possani, the recommended
CC name of this toxin has been updated to alpha-KTx 2.19, since alpha-KTx
CC 2.15 is already used for Toxin II.10.5 (AC C0HJW1).
CC {ECO:0000305|Ref.2}.
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DR AlphaFoldDB; C0HJT0; -.
DR SMR; C0HJT0; -.
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.
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..37
FT /note="Potassium channel toxin alpha-KTx 2.19"
FT /evidence="ECO:0000269|PubMed:26169670"
FT /id="PRO_0000441010"
FT SITE 27
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250|UniProtKB:O46028"
FT SITE 36
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250|UniProtKB:O46028"
FT DISULFID 7..28
FT /evidence="ECO:0000250|UniProtKB:P59847"
FT DISULFID 13..33
FT /evidence="ECO:0000250|UniProtKB:P59847"
FT DISULFID 17..35
FT /evidence="ECO:0000250|UniProtKB:P59847"
SQ SEQUENCE 37 AA; 3951 MW; CC87E4CFE23AA6FC CRC64;
TVIDVKCTSP KQCVPACKAA MGTVRAKCMN GKCKCYI