SCXD_CENLI
ID SCXD_CENLI Reviewed; 68 AA.
AC C0HK69;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Beta-toxin Cl13 {ECO:0000303|PubMed:27871874, ECO:0000303|PubMed:32569846};
DE AltName: Full=CliNaTxBet37 {ECO:0000303|PubMed:31052267};
OS Centruroides limpidus (Mexican scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6876;
RN [1]
RP PROTEIN SEQUENCE OF 1-66, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=27871874; DOI=10.1016/j.peptides.2016.11.008;
RA Olamendi-Portugal T., Restano-Cassulini R., Riano-Umbarila L., Becerril B.,
RA Possani L.D.;
RT "Functional and immuno-reactive characterization of a previously
RT undescribed peptide from the venom of the scorpion Centruroides limpidus.";
RL Peptides 87:34-40(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-68, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=31052267; DOI=10.3390/toxins11050247;
RA Cid-Uribe J.I., Meneses E.P., Batista C.V.F., Ortiz E., Possani L.D.;
RT "Dissecting toxicity: the venom gland transcriptome and the venom proteome
RT of the highly venomous scorpion Centruroides limpidus (Karsch, 1879).";
RL Toxins 11:0-0(2019).
RN [3]
RP STRUCTURE BY NMR, SEQUENCE REVISION TO 58 AND 66, AMIDATION AT LYS-66, AND
RP DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=32569846; DOI=10.1016/j.toxicon.2020.06.011;
RA Lopez-Giraldo A.E., Olamendi-Portugal T., Riano-Umbarila L., Becerril B.,
RA Possani L.D., Delepierre M., Del Rio-Portilla F.;
RT "The three-dimensional structure of the toxic peptide Cl13 from the
RT scorpion Centruroides limpidus.";
RL Toxicon 184:158-166(2020).
CC -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing (By similarity). Inhibits sodium
CC channels Nav1.4/SCN4A, Nav1.5/SCN5A and Nav1.6/SCN8A (PubMed:27871874).
CC Also has a weak inhibitory effect on Nav1.2/SCN2A (PubMed:27871874). Is
CC lethal to mice (PubMed:27871874). {ECO:0000250|UniProtKB:P60266,
CC ECO:0000269|PubMed:27871874}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27871874}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27871874}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000269|PubMed:32569846}.
CC -!- MASS SPECTROMETRY: Mass=7846.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:27871874};
CC -!- TOXIC DOSE: Is lethal to mice by intraperitoneal injection of 0.5 ug
CC (and higher doses). {ECO:0000269|PubMed:27871874}.
CC -!- MISCELLANEOUS: Has no inhibitory effect on Nav1.1/SCN1A, Nav1.3/SCN3A
CC and Nav1.7/SCN9A. {ECO:0000269|PubMed:27871874}.
CC -!- MISCELLANEOUS: Is not neutralized by the two single-chain antibody
CC fragments LR and 10FG2. {ECO:0000269|PubMed:32569846}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR PDB; 6VXW; NMR; -; A=1-66.
DR PDBsum; 6VXW; -.
DR AlphaFoldDB; C0HK69; -.
DR BMRB; C0HK69; -.
DR SMR; C0HK69; -.
DR ABCD; C0HK69; 3 sequenced antibodies.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..66
FT /note="Beta-toxin Cl13"
FT /evidence="ECO:0000269|PubMed:27871874"
FT /id="PRO_0000439882"
FT DOMAIN 1..66
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 66
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:32569846"
FT DISULFID 12..65
FT /evidence="ECO:0000269|PubMed:32569846,
FT ECO:0007744|PDB:6VXW"
FT DISULFID 16..41
FT /evidence="ECO:0000269|PubMed:32569846,
FT ECO:0007744|PDB:6VXW"
FT DISULFID 25..46
FT /evidence="ECO:0000269|PubMed:32569846,
FT ECO:0007744|PDB:6VXW"
FT DISULFID 29..48
FT /evidence="ECO:0000269|PubMed:32569846,
FT ECO:0007744|PDB:6VXW"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:6VXW"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6VXW"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:6VXW"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:6VXW"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6VXW"
SQ SEQUENCE 68 AA; 8041 MW; 8AD239CF2995115A CRC64;
KEGYLVDYHT GCKYTCAKLG DNDYCVRECR LRYYQSAHGY CYAFACWCTH LYEQAVVWPL
PNKRCKGK
