U31H_SCYTH
ID U31H_SCYTH Reviewed; 71 AA.
AC A0A0A0VBR5;
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=U3-scytotoxin-Sth1h {ECO:0000303|PubMed:24303891, ECO:0000303|PubMed:27227898};
DE Short=U3-SYTX-Sth1h {ECO:0000303|PubMed:24303891};
DE Short=U3-Sth1h {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].
RC TISSUE=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:5FZW}
RP STRUCTURE BY NMR OF 40-71, 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, when mixed with U3-SYTX-Sth1a does not
CC cause paralytic or lethal activity when injected into crickets
CC (PubMed:27227898). It is noteworthy that 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 -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26003";
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DR EMBL; KF860358; AIW62383.1; -; mRNA.
DR PDB; 5FZW; NMR; -; A=40-71.
DR PDBsum; 5FZW; -.
DR AlphaFoldDB; A0A0A0VBR5; -.
DR SMR; A0A0A0VBR5; -.
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..33
FT /evidence="ECO:0000255"
FT PROPEP 34..39
FT /evidence="ECO:0000305"
FT /id="PRO_0000448640"
FT CHAIN 40..71
FT /note="U3-scytotoxin-Sth1h"
FT /id="PRO_5001970751"
FT DISULFID 46..60
FT /evidence="ECO:0000269|PubMed:27227898,
FT ECO:0007744|PDB:5FZW"
FT DISULFID 53..64
FT /evidence="ECO:0000269|PubMed:27227898,
FT ECO:0007744|PDB:5FZW"
FT DISULFID 59..69
FT /evidence="ECO:0000269|PubMed:27227898,
FT ECO:0007744|PDB:5FZW"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5FZW"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5FZW"
SQ SEQUENCE 71 AA; 7934 MW; A0E3F197E173838E CRC64;
MSQNSITSYK MGFAKHFFLF AVLLCATAMY SVAEPAQERL IESIACMQKG LPCMEHVDCC
HGVCDSLFCL Y
