ID   U51A_SCYTH              Reviewed;          71 AA.
AC   A0A0A0V633;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=U5-scytotoxin-Sth1a {ECO:0000303|PubMed:24303891, ECO:0000303|PubMed:27227898};
DE            Short=U5-SYTX-Sth1a {ECO:0000303|PubMed:24303891};
DE            Short=U5-Sth1a {ECO:0000303|PubMed:27227898};
DE   Flags: Precursor;
OS   Scytodes thoracica (Spitting spider) (Aranea thoracica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Scytodidae; Scytodes.
OX   NCBI_TaxID=1112478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24303891; DOI=10.1021/pr400875s;
RA   Zobel-Thropp P.A., Correa S.M., Garb J.E., Binford G.J.;
RT   "Spit and venom from scytodes spiders: a diverse and distinct cocktail.";
RL   J. Proteome Res. 13:817-835(2014).
RN   [2] {ECO:0007744|PDB:5FZX}
RP   STRUCTURE BY NMR OF 36-71, FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=27227898; DOI=10.1371/journal.pone.0156291;
RA   Ariki N.K., Munoz L.E., Armitage E.L., Goodstein F.R., George K.G.,
RA   Smith V.L., Vetter I., Herzig V., King G.F., Loening N.M.;
RT   "Characterization of three venom peptides from the spitting spider Scytodes
RT   thoracica.";
RL   PLoS ONE 11:E0156291-E0156291(2016).
CC   -!- FUNCTION: Probable insect neurotoxin with ion channel impairing
CC       activity (Probable). Does not show activity on 45 human receptors from
CC       9 families (5-hydroxytryptamine, adrenergic, dopamine, muscarinic,
CC       histamine, neurotransmitter, opioid, sigma, and gaba(A) receptors)
CC       (PubMed:27227898). In vivo, does not cause paralytic or lethal activity
CC       when injected into sheep blowflies or crickets (PubMed:27227898). It is
CC       noteworthy that both sheep blowflies and crickets are evolutionarily
CC       distant from prey species (PubMed:27227898).
CC       {ECO:0000269|PubMed:27227898}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24303891}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24303891}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:27227898}.
CC   -!- MISCELLANEOUS: Does not show activity on 45 human receptors from 9
CC       families (5-hydroxytryptamine, adrenergic, dopamine, muscarinic,
CC       histamine, neurotransmitter, opioid, sigma, and gaba(A) receptors).
CC       {ECO:0000269|PubMed:27227898}.
CC   -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC       URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26004";
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; KF860361; AIW62384.1; -; mRNA.
DR   PDB; 5FZX; NMR; -; A=36-71.
DR   PDBsum; 5FZX; -.
DR   AlphaFoldDB; A0A0A0V633; -.
DR   SMR; A0A0A0V633; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..35
FT                   /evidence="ECO:0000269|PubMed:24303891"
FT                   /id="PRO_0000448641"
FT   CHAIN           36..71
FT                   /note="U5-scytotoxin-Sth1a"
FT                   /evidence="ECO:0000269|PubMed:24303891"
FT                   /id="PRO_5001978113"
FT   DISULFID        42..60
FT                   /evidence="ECO:0000269|PubMed:27227898,
FT                   ECO:0007744|PDB:5FZX"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000269|PubMed:27227898,
FT                   ECO:0007744|PDB:5FZX"
FT   DISULFID        59..70
FT                   /evidence="ECO:0000269|PubMed:27227898,
FT                   ECO:0007744|PDB:5FZX"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:5FZX"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:5FZX"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:5FZX"
SQ   SEQUENCE   71 AA;  7837 MW;  3F1237937ECA763D CRC64;
     MKLFVCFLLL AVVVVSAVNA SEEMRLKNLL KAVERDETPD ECVTRGNFCA TPEVHGDWCC
     GSLKCVSNSC R