ID   TXF2A_SCOMO             Reviewed;          73 AA.
AC   P0DPT5;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=U-scoloptoxin(15)-Sm2a {ECO:0000303|PubMed:30554841};
DE            Short=U-SLPTX(15)-Sm2a {ECO:0000303|PubMed:30554841};
DE   Flags: Precursor;
OS   Scolopendra morsitans (Tanzanian blue ringleg centipede).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=943129;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
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).
RN   [2]
RP   STRUCTURE BY NMR OF 21-73, SYNTHESIS OF 21-73, IDENTIFICATION BY MASS
RP   SPECTROMETRY, DISULFIDE BOND, BIOASSAY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=30554841; DOI=10.1016/j.str.2018.10.022;
RA   Dash T.S., Shafee T., Harvey P.J., Zhang C., Peigneur S., Deuis J.R.,
RA   Vetter I., Tytgat J., Anderson M.A., Craik D.J., Durek T., Undheim E.A.B.;
RT   "A centipede toxin family defines an ancient class of CSalphabeta
RT   defensins.";
RL   Structure 0:0-0(2018).
CC   -!- FUNCTION: Activity unknown, even that a lot of targets (Kv, Nav, Cav)
CC       have been tested and activities on insects and mice have been tested.
CC       {ECO:0000305|PubMed:30554841}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30554841}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24847043}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CS-alpha/beta). Since the toxin contains
CC       only 2 disulfide bonds, it is called 2ds-CSalpha/beta.
CC       {ECO:0000269|PubMed:30554841}.
CC   -!- MISCELLANEOUS: Does not show antimicrobial and ion channel inhbibitory
CC       activities. Antimicrobial activity was tested against five bacteria and
CC       two fungi, including four Gram-negative bactersoia (E.coli,
CC       P.aeruginosa, A.baumannii, and K.pneumoniae), one Gram-positive
CC       bacterium (S.aureus), and the fungi C.albicans and C.neoformans (tested
CC       at 32 mg/mL). Ion channel inhibitory activity was tested against 16
CC       voltage-gated potassium channels (Kv) (Kv1.1- Kv1.6, Kv2.1, Kv3.1,
CC       Kv4.2, Kv7.1-7.2, Kv7.4-7.5, Kv10.1, Kv11.1, and Shaker IR), 9 voltage-
CC       gated sodium channels (Nav) (Nav1.1-Nav1.8, BgNav1, and VdNav1), two
CC       voltage-gated calcium channels (Cav) (Cav1, Cav2.2), and two nicotinic
CC       acetylcholine receptors (nAChR) (alpha-7 nAChR, alpha-3-beta-2/alpha-3-
CC       beta-4 nAChR) (tested at 10 uM). In addition, the toxin does not show
CC       activity on trigeminal ganglia (500 ug tested) as well as on insects
CC       and on mice (absence of flinching or licking).
CC       {ECO:0000269|PubMed:30554841}.
CC   -!- SIMILARITY: Belongs to the scoloptoxin-15 family. {ECO:0000305}.
CC   -!- CAUTION: All S.morsitans family members described in 'Undeheim et al.,
CC       2014' have not been imported into UniProtKB. Please, refer to this
CC       paper to access them. {ECO:0000305|PubMed:24847043}.
CC   -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC       (NCBI);
CC       URL="https://www.ncbi.nlm.nih.gov/nuccore/GASH01000152";
CC   -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC       URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=30372";
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DR   PDB; 6BL9; NMR; -; A=1-53.
DR   PDBsum; 6BL9; -.
DR   AlphaFoldDB; P0DPT5; -.
DR   SMR; P0DPT5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..73
FT                   /note="U-scoloptoxin(15)-Sm2a"
FT                   /evidence="ECO:0000305|PubMed:30554841"
FT                   /id="PRO_0000446794"
FT   DISULFID        39..66
FT                   /evidence="ECO:0000269|PubMed:30554841,
FT                   ECO:0000312|PDB:6BL9"
FT   DISULFID        43..68
FT                   /evidence="ECO:0000269|PubMed:30554841,
FT                   ECO:0000312|PDB:6BL9"
SQ   SEQUENCE   73 AA;  8302 MW;  1F18CCE1296DABFF CRC64;
     MKFYIVFCLF VVLLINFAAA EETEEPIRHA KKNPSEGECK KACADAFANG DQSKIAKAEN
     FKDYYCNCHI IIH