ID   PME1A_POEME             Reviewed;          35 AA.
AC   P0DQO0;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Mu-theraphotoxin-Pm1a {ECO:0000303|PubMed:32092883};
DE            Short=Mu-TRTX-Pm1a {ECO:0000303|PubMed:32092883};
OS   Poecilotheria metallica (Metallic blue ornamental tree spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Poecilotheria.
OX   NCBI_TaxID=1956341;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AMIDATION AT PHE-35, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=32092883; DOI=10.3390/biomedicines8020037;
RA   Yin K., Deuis J.R., Dekan Z., Jin A.H., Alewood P.F., King G.F., Herzig V.,
RA   Vetter I.;
RT   "Addition of K22 converts spider venom peptide Pme2a from an activator to
RT   an inhibitor of Nav1.7.";
RL   Biomedicines 8:0-0(2020).
CC   -!- FUNCTION: Gating-modifier toxin with weak activity on Nav1.7/SCN9A and
CC       Nav1.8/SCN10A (PubMed:32092883). Inhibits Nav1.7/SCN9A peak current
CC       (IC(50)=334 nM) and shifts the voltage dependence of activation to more
CC       depolarised membrane potentials (PubMed:32092883). Shows 21% peak
CC       current inhibition (at 10 uM) on Nav1.8/SCN10A sodium channels
CC       (PubMed:32092883). {ECO:0000269|PubMed:32092883}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32092883}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:32092883}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60992}.
CC   -!- MASS SPECTROMETRY: Mass=3910.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:32092883};
CC   -!- MISCELLANEOUS: Does not show activity on TRPV1.
CC       {ECO:0000269|PubMed:32092883}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 62 (Vatx)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DQO0; -.
DR   SMR; P0DQO0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..35
FT                   /note="Mu-theraphotoxin-Pm1a"
FT                   /evidence="ECO:0000269|PubMed:32092883"
FT                   /id="PRO_0000451632"
FT   MOD_RES         35
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:32092883"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
FT   DISULFID        16..29
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
SQ   SEQUENCE   35 AA;  3920 MW;  117E132170611C6C CRC64;
     GGCRYFLGGC SEHSDCCEHL RCKMGLNYCA WDGTF