ID   PM1A_HOMSP              Reviewed;          28 AA.
AC   P0DQO2;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Mu-theraphotoxin-Hsp1a {ECO:0000305};
DE            Short=Hsp1a {ECO:0000303|PubMed:31647222};
DE            Short=Mu-TRTX-Hsp1a {ECO:0000305};
OS   Homoeomma sp. (Peruvian tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Homoeomma.
OX   NCBI_TaxID=2774376;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, SYNTHESIS, AMIDATION AT ASN-28, AND
RP   BIOTECHNOLOGY.
RC   TISSUE=Venom;
RX   PubMed=31647222; DOI=10.1021/acs.bioconjchem.9b00612;
RA   Gonzales J., Demetrio de Souza Franca P., Jiang Y., Pirovano G.,
RA   Kossatz S., Guru N., Yarilin D., Agwa A.J., Schroeder C.I., Patel S.G.,
RA   Ganly I., King G.F., Reiner T.;
RT   "Fluorescence imaging of peripheral nerves by a Nav1.7-targeted inhibitor
RT   cystine knot peptide.";
RL   Bioconj. Chem. 30:2879-2888(2019).
CC   -!- FUNCTION: Potent and selective inhibitor of Nav1.7/SCN9A sodium
CC       channels. Inhibits Nav1.7/SCN9A peak current (IC(50)=13 nM)
CC       (PubMed:31647222). In vivo, does not induce visible signs of toxicity
CC       when intravenously injected into mice (PubMed:31647222).
CC       {ECO:0000269|PubMed:31647222}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31647222,
CC       ECO:0000305|PubMed:31647222}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31647222}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60273}.
CC   -!- BIOTECHNOLOGY: When conjugated with a fluorophore, could be used as a
CC       tracer in surgery to discriminate nerves from their surrounding
CC       tissues, particularly during tumor resections or after traumatic
CC       injuries. The dye is conjugated to Lys-4 residue and this synthetic
CC       peptide shows only a small decrease in ability to inhibit Nav1.7/SCN9A
CC       compared to native peptide. {ECO:0000305|PubMed:31647222}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 30 (phrixotoxin) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DQO2; -.
DR   SMR; P0DQO2; -.
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   PEPTIDE         1..28
FT                   /note="Mu-theraphotoxin-Hsp1a"
FT                   /id="PRO_0000451989"
FT   MOD_RES         28
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:31647222"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:P60273"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P60273"
FT   DISULFID        15..25
FT                   /evidence="ECO:0000250|UniProtKB:P60273"
SQ   SEQUENCE   28 AA;  3398 MW;  13B5168C1B9B2A11 CRC64;
     YCQKFLWTCD SERPCCEGLV CRLWCKIN