ID   TZ72_HADIN              Reviewed;          96 AA.
AC   A0A1D0C027; A0A1D5B342;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=U4-hexatoxin-Hi1a;
DE            Short=U4-HXTX-Hi1a;
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   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   [2]
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   [3]
RP   STRUCTURE BY NMR OF 19-94.
RA   Pineda S.S., Chin Y.K.Y., Senff S., Mobli M., Escoubas P., Nicholson G.,
RA   Kass Q., Fry B.G., Mattick J.S., King G.F.;
RT   "Single-gene recruitment underlies venom complexity in the Australian
RT   funnel-web spider Hadronyche infensa.";
RL   Submitted (AUG-2015) to the PDB data bank.
CC   -!- FUNCTION: Probable neurotoxin with ion channel impairing activity.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305|Ref.3}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 27 (Jztx-72) family. ICK-72
CC       subfamily. {ECO:0000305}.
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DR   EMBL; HACE01000019; CDZ18803.1; -; Transcribed_RNA.
DR   EMBL; HACE01000039; CDZ18823.1; -; Transcribed_RNA.
DR   EMBL; HACE01000076; CDZ18860.1; -; Transcribed_RNA.
DR   PDB; 2N6R; NMR; -; A=20-94.
DR   PDBsum; 2N6R; -.
DR   AlphaFoldDB; A0A1D0C027; -.
DR   SMR; A0A1D0C027; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR035311; Cys_Knot_tox.
DR   Pfam; PF17486; Cys_Knot_tox; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000305"
FT   CHAIN           20..94
FT                   /note="U4-hexatoxin-Hi1a"
FT                   /evidence="ECO:0000305|Ref.3"
FT                   /id="PRO_5014266694"
FT   MOD_RES         94
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000305"
FT   DISULFID        39..80
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2N6R"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2N6R"
FT   DISULFID        52..65
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2N6R"
FT   DISULFID        83..90
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2N6R"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:2N6R"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:2N6R"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:2N6R"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:2N6R"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:2N6R"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:2N6R"
SQ   SEQUENCE   96 AA;  10919 MW;  B1651D76DDD7F558 CRC64;
     MKLILLIAIF SALAVVNLGT PSADQVRYNY TELPNGEYCY TPRRRCTSAD QCCRPYDTTA
     AFHGCGRIWP KDKREKVDRC YICNNEKTLC TSVMGK