ID   H16V1_CYRHA             Reviewed;         113 AA.
AC   D2Y2H9;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=U11-theraphotoxin-Hhn1v;
DE            Short=U11-TRTX-Hhn1v;
DE   AltName: Full=Hainantoxin-XVI-22;
DE            Short=HNTX-XVI-22;
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].
RC   TISSUE=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).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 75-113.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Weakly inhibits Kv1.2/KCNA2, Kv1.3/KCNA3, Kv2.1/KCNB1
CC       voltage-gated potassium channels, and Nav1.5/SCN5A voltage-gated sodium
CC       channels (PubMed:29483648). {ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 01 (HNTX-16)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GU293056; ADB56872.1; -; mRNA.
DR   AlphaFoldDB; D2Y2H9; -.
DR   ArachnoServer; AS001651; U11-theraphotoxin-Hhn1v.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012627; Toxin_22.
DR   Pfam; PF08092; Toxin_22; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000400959"
FT   PEPTIDE         75..113
FT                   /note="U11-theraphotoxin-Hhn1v"
FT                   /id="PRO_0000400960"
FT   REGION          61..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        75..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..110
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  13149 MW;  6B30276741932CE7 CRC64;
     MNTVRVTFLL VFVLAVSLGQ ADKDENRMEM QEKTEQGKSY LDFAENLLLQ KLEELEAKLL
     EEDSEESRNS RQKRCIGEGV PCDENDPRCC FGLVCLKPTL HGIWYKSYYC YKK