ID   TXMO_HADIN              Reviewed;          83 AA.
AC   P60272; A0A1D0BPQ6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=U2-hexatoxin-Hi1a {ECO:0000305};
DE            Short=U2-HXTX-Hi1a {ECO:0000305};
DE   AltName: Full=Toxin AcTx-Hi:OB4219 {ECO:0000303|PubMed:11876637};
DE   Flags: Precursor;
OS   Hadronyche infensa (Fraser island funnel-web spider) (Atrax infensus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=153481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Pineda S.S.;
RT   "Probing the chemical diversity of venom from the Australian Funnel-web
RT   spider Hadronyche infensa.";
RL   Thesis (2012), The University of Queensland, Australia.
RN   [3]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND STRUCTURE BY NMR OF CIS- AND
RP   TRANS-PRO-30 ISOMERS.
RC   TISSUE=Venom;
RX   PubMed=11876637; DOI=10.1021/bi011932y;
RA   Rosengren K.J., Wilson D., Daly N.L., Alewood P.F., Craik D.J.;
RT   "Solution structures of the cis- and trans-Pro30 isomers of a novel 38-
RT   residue toxin from the venom of Hadronyche infensa sp. that contains a
RT   cystine-knot motif within its four disulfide bonds.";
RL   Biochemistry 41:3294-3301(2002).
CC   -!- FUNCTION: Inhibits sodium channels (Nav) of insects. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11876637}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11876637}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:11876637}.
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       Pro-75. {ECO:0000269|PubMed:11876637}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family.
CC       {ECO:0000305}.
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DR   EMBL; HACE01000038; CDZ18822.1; -; mRNA.
DR   EMBL; HACE01000101; CDZ18885.1; -; mRNA.
DR   PDB; 1KQH; NMR; -; A=46-83.
DR   PDB; 1KQI; NMR; -; A=46-83.
DR   PDBsum; 1KQH; -.
DR   PDBsum; 1KQI; -.
DR   AlphaFoldDB; P60272; -.
DR   SMR; P60272; -.
DR   ArachnoServer; AS000390; U2-hexatoxin-Hi1a.
DR   EvolutionaryTrace; P60272; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016328; Beta/delta-agatoxin_fam.
DR   PROSITE; PS60015; MU_AGATOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..45
FT                   /evidence="ECO:0000269|PubMed:11876637"
FT                   /id="PRO_0000444422"
FT   PEPTIDE         46..83
FT                   /note="U2-hexatoxin-Hi1a"
FT                   /evidence="ECO:0000269|PubMed:11876637"
FT                   /id="PRO_0000044966"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000269|PubMed:11876637,
FT                   ECO:0000312|PDB:1KQH, ECO:0000312|PDB:1KQI"
FT   DISULFID        54..68
FT                   /evidence="ECO:0000269|PubMed:11876637,
FT                   ECO:0000312|PDB:1KQH, ECO:0000312|PDB:1KQI"
FT   DISULFID        62..78
FT                   /evidence="ECO:0000269|PubMed:11876637,
FT                   ECO:0000312|PDB:1KQH, ECO:0000312|PDB:1KQI"
FT   DISULFID        70..76
FT                   /evidence="ECO:0000269|PubMed:11876637,
FT                   ECO:0000312|PDB:1KQH, ECO:0000312|PDB:1KQI"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:1KQH"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:1KQH"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1KQH"
FT   STRAND          72..79
FT                   /evidence="ECO:0007829|PDB:1KQH"
SQ   SEQUENCE   83 AA;  9241 MW;  FFCC80427B5CC0D8 CRC64;
     MRNTTFLVLN VMLLVSVALF CAADPEMEKS SFAEILDTGN PEQERKCLAE AADCSPWSGD
     SCCKPYLCSC IFFYPCSCRP KGW