ID   H7A01_CYRHA             Reviewed;          85 AA.
AC   D2Y2C3;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=U5-theraphotoxin-Hhn1a {ECO:0000305};
DE            Short=U5-TRTX-Hhn1a {ECO:0000305};
DE   AltName: Full=Hainantoxin-VII {ECO:0000303|PubMed:20192277, ECO:0000312|EMBL:ADB56816.1};
DE            Short=HNTX-VII {ECO:0000303|PubMed:20192277, ECO:0000312|EMBL:ADB56816.1};
DE   AltName: Full=Peptide F4-32.71 {ECO:0000303|PubMed:20192277};
DE   Flags: Precursor;
OS   Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Haplopelma.
OX   NCBI_TaxID=209901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], PROTEIN SEQUENCE OF 50-82,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20192277; DOI=10.1021/pr1000016;
RA   Tang X., Zhang Y., Hu W., Xu D., Tao H., Yang X., Li Y., Jiang L.,
RA   Liang S.;
RT   "Molecular diversification of peptide toxins from the tarantula Haplopelma
RT   hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic,
RT   and genomic analyses.";
RL   J. Proteome Res. 9:2550-2564(2010).
CC   -!- FUNCTION: Ion channel impairing toxin that inhibits voltage-gated
CC       sodium channels. The recombinantly expressed toxin shows a weak
CC       activity against Nav1.7/SCN9A, and shifts the voltage dependence of
CC       channel activation to more depolarized potentials.
CC       {ECO:0000250|UniProtKB:P0DQN1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20192277}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20192277}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P83480}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 18 (Hntx-VII)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GU293000; ADB56816.1; -; mRNA.
DR   AlphaFoldDB; D2Y2C3; -.
DR   SMR; D2Y2C3; -.
DR   ArachnoServer; AS001873; U5-theraphotoxin-Hhn1a.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..49
FT                   /evidence="ECO:0000305|PubMed:20192277"
FT                   /id="PRO_0000400577"
FT   PEPTIDE         50..85
FT                   /note="U5-theraphotoxin-Hhn1a"
FT                   /evidence="ECO:0000305|PubMed:20192277"
FT                   /id="PRO_0000400578"
FT   DISULFID        51..65
FT                   /evidence="ECO:0000250|UniProtKB:P83480"
FT   DISULFID        58..70
FT                   /evidence="ECO:0000250|UniProtKB:P83480"
FT   DISULFID        64..77
FT                   /evidence="ECO:0000250|UniProtKB:P83480"
SQ   SEQUENCE   85 AA;  9849 MW;  7CC6B84F9050AB91 CRC64;
     MKSQIFFAVA ALFLLTVRTY ASKSKEQDLR DALFSAMFSA DNQLNPQERE CRYWLGTCSK
     TGDCCSHLSC SPKHGWCVWD WTFRK