SC2B_CENLI
ID SC2B_CENLI Reviewed; 87 AA.
AC P59899; Q7M4H5;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Toxin Cll2b;
DE Short=Cll 2b;
DE AltName: Full=Toxin II.6;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Corona M., Possani L.D.;
RT "Genes and peptides from the scorpion Centruroides limpidus, that recognize
RT Na(+)-channels.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-49.
RC TISSUE=Venom;
RX PubMed=2451580; DOI=10.1016/0305-0491(88)90277-5;
RA Alagon A.C., Guzman H.S., Martin B.M., Ramirez A.N., Carbone E.,
RA Possani L.D.;
RT "Isolation and characterization of two toxins from the Mexican scorpion
RT Centruroides limpidus limpidus Karsch.";
RL Comp. Biochem. Physiol. 89B:153-161(1988).
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). This toxin had also
CC a depressive action on the classical calcium current activated at high
CC membrane potentials. This toxin is active on mammals. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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 -!- 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 EMBL; AF488349; AAP49027.1; -; mRNA.
DR PIR; B60791; B60791.
DR AlphaFoldDB; P59899; -.
DR SMR; P59899; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
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 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 Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2451580"
FT CHAIN 20..85
FT /note="Toxin Cll2b"
FT /id="PRO_0000035266"
FT DOMAIN 20..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 85
FT /note="Asparagine amide"
FT /evidence="ECO:0000250"
FT DISULFID 31..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 44..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 87 AA; 9761 MW; 15EF747B4BB66FD3 CRC64;
MNSLLMITAC LALVGTVWAK EGYLVNHSTG CKYECYKLGD NDYCLRECKQ QYGKGAGGYC
YAFGCWCTHL YEQAVVWPLP KKTCNGK
