KBX23_LYCMC
ID KBX23_LYCMC Reviewed; 85 AA.
AC P0CI42;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Neurotoxin beta-KTx 14.3;
DE Flags: Precursor;
OS Lychas mucronatus (Chinese swimming scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX NCBI_TaxID=172552;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Yunnan; TISSUE=Venom gland;
RX PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT mucronatus reveals intraspecific toxic gene diversity and new venomous
RT components.";
RL BMC Genomics 11:452-452(2010).
CC -!- FUNCTION: Isoform 1 has a very weak effect to block voltage-gated
CC potassium channel Kv1.1/KCNA1. {ECO:0000269|PubMed:20663230}.
CC -!- FUNCTION: Isoform 2 has a very weak effect to block voltage-gated
CC potassium channel Kv1.1/KCNA1. {ECO:0000269|PubMed:20663230}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0CI42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0CI42-2; Sequence=VSP_040456;
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC 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 EMBL; GT028643; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT028645; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 7LGV; NMR; -; A=38-85.
DR PDBsum; 7LGV; -.
DR AlphaFoldDB; P0CI42; -.
DR SMR; P0CI42; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR029237; Long_scorpion_toxin.
DR Pfam; PF14866; Toxin_38; 1.
DR PROSITE; PS51862; BSPN_CSAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..37
FT /evidence="ECO:0000305"
FT /id="PRO_0000403850"
FT CHAIN 38..85
FT /note="Neurotoxin beta-KTx 14.3"
FT /id="PRO_0000403851"
FT DOMAIN 49..85
FT /note="BetaSPN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 52..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 59..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 63..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT VAR_SEQ 37..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20663230"
FT /id="VSP_040456"
SQ SEQUENCE 85 AA; 9425 MW; 4647B291E448A789 CRC64;
MKQYIFFLAL IVLTATFAEA GKKTEILDKV KKVFSKGIAG VADLNNMSEL GCPFIEKWCE
DHCESKKQVG KCENFDCSCV KLGGK