ID   TX51A_SCOMU             Reviewed;         129 AA.
AC   I6R1R5;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Omega-scoloptoxin(05)-Ssm1a {ECO:0000303|PubMed:24847043};
DE            Short=Omega-SLPTX(05)-Ssm1a {ECO:0000303|PubMed:24847043};
DE   AltName: Full=Omega-scoloptoxin-Ssm1a {ECO:0000303|PubMed:22595790};
DE            Short=Omega-SLPTX-Ssm1a {ECO:0000303|PubMed:22595790};
DE   Flags: Precursor;
OS   Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra
OS   subspinipes mutilans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=2836329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-129, FUNCTION, BIOASSAY,
RP   DISULFIDE BONDS, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=22595790; DOI=10.1074/mcp.m112.018853;
RA   Yang S., Liu Z., Xiao Y., Li Y., Rong M., Liang S., Zhang Z., Yu H.,
RA   King G.F., Lai R.;
RT   "Chemical punch packed in venoms makes centipedes excellent predators.";
RL   Mol. Cell. Proteomics 11:640-650(2012).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=24847043; DOI=10.1093/molbev/msu162;
RA   Undheim E.A., Jones A., Clauser K.R., Holland J.W., Pineda S.S., King G.F.,
RA   Fry B.G.;
RT   "Clawing through evolution: toxin diversification and convergence in the
RT   ancient lineage Chilopoda (centipedes).";
RL   Mol. Biol. Evol. 31:2124-2148(2014).
CC   -!- FUNCTION: Toxin that increase voltage-gated calcium channel (Cav)
CC       currents in DRG neurons by 70% and 120%, when 1 uM and 10 uM are
CC       tested, respectively. {ECO:0000269|PubMed:22595790}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22595790}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22595790}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=8810.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22595790};
CC   -!- MISCELLANEOUS: Does not show insecticidal activity.
CC       {ECO:0000305|PubMed:22595790}.
CC   -!- SIMILARITY: Belongs to the scoloptoxin-05 family. {ECO:0000305}.
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DR   EMBL; JN646117; AFM55006.1; -; mRNA.
DR   AlphaFoldDB; I6R1R5; -.
DR   SMR; I6R1R5; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..46
FT                   /evidence="ECO:0000305|PubMed:22595790"
FT                   /id="PRO_0000425464"
FT   CHAIN           47..129
FT                   /note="Omega-scoloptoxin(05)-Ssm1a"
FT                   /evidence="ECO:0000269|PubMed:22595790"
FT                   /id="PRO_0000425465"
SQ   SEQUENCE   129 AA;  13873 MW;  A3BC40DF1196962D CRC64;
     MPSLCIIALF GTLTFYTLIP SIHTLKCVRC DGPMSNYDCK TTYPAAEECP SLSGGSSNYC
     SKKETFTSNG NLEQTRRYCN SVAAPSTACT DLKTGGKLCE YSCNTDGCNS VAGMEPTRAV
     YFIAILMLA