VSTX1_ACAGO
ID VSTX1_ACAGO Reviewed; 60 AA.
AC P0DQJ5;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=U1-theraphotoxin-Agm3a {ECO:0000303|PubMed:27436114};
DE Short=U1-TRTX-Agm3a {ECO:0000303|PubMed:27436114};
DE Flags: Precursor;
OS Acanthoscurria gomesiana (Tarantula spider) (Phormictopus pheopygus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Acanthoscurria.
OX NCBI_TaxID=115339;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=27436114; DOI=10.1016/j.jprot.2016.07.012;
RA Abreu T.F., Sumitomo B.N., Nishiyama M.Y. Jr., Oliveira U.C., Souza G.H.,
RA Kitano E.S., Zelanis A., Serrano S.M., Junqueira-de-Azevedo I.,
RA Silva P.I. Jr., Tashima A.K.;
RT "Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins
RT with potential antimicrobial activity.";
RL J. Proteomics 151:232-242(2017).
CC -!- FUNCTION: Inhibits sodium channels Nav1.7/SCN9A and potassium channels
CC Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium
CC channel KvAP (from the archaeon Aeropyrum pernix) with very slow
CC apparent binding kinetics and affects channel gating. Reaches its
CC target by dynamically partitioning into anionic or zwitterionic
CC headgroup lipid membranes. May bind to the open state of KvAP.
CC {ECO:0000250|UniProtKB:P60980}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27436114}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27436114}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P60980}.
CC -!- MASS SPECTROMETRY: Mass=3690.5; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:27436114};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 63 (VsTx1)
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DQJ5; -.
DR SMR; P0DQJ5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR InterPro; IPR013140; Huwentoxin_CS1.
DR Pfam; PF07740; Toxin_12; 1.
DR PROSITE; PS60021; HWTX_1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..29
FT /evidence="ECO:0000250|UniProtKB:P60980"
FT /id="PRO_0000448549"
FT CHAIN 30..60
FT /note="U1-theraphotoxin-Agm3a"
FT /evidence="ECO:0000269|PubMed:27436114"
FT /id="PRO_0000448550"
FT DISULFID 31..45
FT /evidence="ECO:0000250|UniProtKB:P60980"
FT DISULFID 38..50
FT /evidence="ECO:0000250|UniProtKB:P60980"
FT DISULFID 44..57
FT /evidence="ECO:0000250|UniProtKB:P60980"
SQ SEQUENCE 60 AA; 6877 MW; 0B5A4468D1C8B507 CRC64;
MKFSVLVFIL GLVLLLALSS ATEMEENARA CGSFMWKCSE RLPCCQEYVC SPQWKWCQNP
