HN324_CYRHA
ID HN324_CYRHA Reviewed; 35 AA.
AC P0CH70; P0CH69;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=U1-theraphotoxin-Hhn1a;
DE Short=U1-TRTX-Hhn1a;
DE AltName: Full=Hainantoxin F3-24.71 {ECO:0000303|PubMed:20192277};
DE Contains:
DE RecName: Full=Hainantoxin-VI {ECO:0000303|Ref.2};
DE Short=HNTX-VI {ECO:0000303|Ref.2};
DE AltName: Full=Peptide F6-25.12 {ECO:0000303|PubMed:20192277};
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 PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
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).
RN [2]
RP PROTEIN SEQUENCE OF 1-34, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RA Pan J.Y., Hu W.J., Liang S.P.;
RT "Purification, sequencing and characterization of hainantoxin-VI, a
RT neurotoxin from the Chinese bird spider Selenocosmia hainana.";
RL Dong Wu Xue Yan Jiu 23:280-283(2002).
RN [3]
RP FUNCTION.
RX PubMed=20506577; DOI=10.1631/jzus.b0900393;
RA Wang R.L., Yi S., Liang S.P.;
RT "Mechanism of action of two insect toxins huwentoxin-III and hainantoxin-VI
RT on voltage-gated sodium channels.";
RL J. Zhejiang Univ. Sci. B 11:451-457(2010).
CC -!- FUNCTION: [Hainantoxin-VI]: Gating-modifier toxin that dose-dependently
CC inhibits inactivation of voltage-gated sodium channels and reduces the
CC peak of sodium current in cockroach DUM neurons (PubMed:20506577). In
CC vivo, reversibly paralyzes cockroaches for several hours, paralyzes rat
CC after intracerebroventricular injection and blocks the neuromuscular
CC transmission of the isolated rat phrenic nerve-diaphragm preparation
CC (Ref.2). {ECO:0000269|PubMed:20506577, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20192277}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [U1-theraphotoxin-Hhn1a]: Mass=4057.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20192277};
CC -!- MASS SPECTROMETRY: [Hainantoxin-VI]: Mass=3998.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20192277};
CC -!- MASS SPECTROMETRY: [Hainantoxin-VI]: Mass=3998.49; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 24 (Hwtx-6)
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CH70; -.
DR SMR; P0CH70; -.
DR ArachnoServer; AS002021; U1-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: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; Toxin.
FT PEPTIDE 1..35
FT /note="U1-theraphotoxin-Hhn1a"
FT /evidence="ECO:0000269|PubMed:20192277"
FT /id="PRO_0000400718"
FT PEPTIDE 1..34
FT /note="Hainantoxin-VI"
FT /evidence="ECO:0000269|PubMed:20192277, ECO:0000269|Ref.2"
FT /id="PRO_0000434820"
FT DISULFID 2..16
FT /evidence="ECO:0000250"
FT DISULFID 9..21
FT /evidence="ECO:0000250"
FT DISULFID 15..28
FT /evidence="ECO:0000250"
SQ SEQUENCE 35 AA; 4062 MW; 0BD5FE6489533182 CRC64;
ECKYLWGTCE KDEHCCEHLG CNKKHGWCGW DGTFG