ID   THNB_HORVU              Reviewed;         136 AA.
AC   P21742;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Beta-hordothionin;
DE   Contains:
DE     RecName: Full=Beta-hordothionin;
DE   Contains:
DE     RecName: Full=Acidic protein;
DE   Flags: Precursor;
GN   Name=THI1.2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bomi; TISSUE=Endosperm;
RA   Rasmussen S.K., Rasmussen C.E.;
RT   "Full-length cDNA clone encoding barley toxin beta-hordothionin.";
RL   Plant Mol. Biol. 21:579-579(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-136.
RA   Hernandez-Lucas C., Royo J., Paz-Ares J., Ponz F., Garcia-Olmedo F.,
RA   Carbonero P.;
RT   "Polyadenylation site heterogeneity in mRNA encoding the precursor of the
RT   barley toxin beta-hordothionin.";
RL   FEBS Lett. 200:103-106(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-72, DISULFIDE BOND, AND
RP   SUBUNIT.
RX   PubMed=15848162; DOI=10.1016/j.febslet.2004.12.100;
RA   Johnson K.A., Kim E., Teeter M.M., Suh S.W., Stec B.;
RT   "Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution.";
RL   FEBS Lett. 579:2301-2306(2005).
CC   -!- FUNCTION: Thionins are small plant proteins which are toxic to animal
CC       cells. They seem to exert their toxic effect at the level of the cell
CC       membrane. Their precise function is not known.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15848162}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the plant thionin (TC 1.C.44) family.
CC       {ECO:0000305}.
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DR   EMBL; Z13008; CAA78352.1; -; mRNA.
DR   PIR; S22977; S22977.
DR   PDB; 1WUW; X-ray; 1.90 A; A/B=28-72.
DR   PDBsum; 1WUW; -.
DR   AlphaFoldDB; P21742; -.
DR   SMR; P21742; -.
DR   EnsemblPlants; HORVU.MOREX.r2.1HG0072510.1.mrna1; HORVU.MOREX.r2.1HG0072510.1.mrna1; HORVU.MOREX.r2.1HG0072510.1.
DR   Gramene; HORVU.MOREX.r2.1HG0072510.1.mrna1; HORVU.MOREX.r2.1HG0072510.1.mrna1; HORVU.MOREX.r2.1HG0072510.1.
DR   EvolutionaryTrace; P21742; -.
DR   ExpressionAtlas; P21742; baseline.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1350.10; -; 1.
DR   InterPro; IPR001010; Thionin.
DR   InterPro; IPR036391; Thionin-like_sf.
DR   PANTHER; PTHR33920; PTHR33920; 1.
DR   Pfam; PF00321; Thionin; 1.
DR   PRINTS; PR00287; THIONIN.
DR   SUPFAM; SSF57429; SSF57429; 1.
DR   PROSITE; PS00271; THIONIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Plant defense; Secreted; Signal; Toxin.
FT   SIGNAL          1..27
FT   CHAIN           28..72
FT                   /note="Beta-hordothionin"
FT                   /id="PRO_0000034114"
FT   CHAIN           73..136
FT                   /note="Acidic protein"
FT                   /id="PRO_0000034115"
FT   DISULFID        30..66
FT                   /evidence="ECO:0000269|PubMed:15848162"
FT   DISULFID        31..58
FT                   /evidence="ECO:0000269|PubMed:15848162"
FT   DISULFID        39..56
FT                   /evidence="ECO:0000269|PubMed:15848162"
FT   DISULFID        43..52
FT                   /evidence="ECO:0000269|PubMed:15848162"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:1WUW"
FT   HELIX           34..43
FT                   /evidence="ECO:0007829|PDB:1WUW"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:1WUW"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:1WUW"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1WUW"
SQ   SEQUENCE   136 AA;  14603 MW;  F9E04874D44CF831 CRC64;
     MGSKGLKGVM VCLLILGLVL EHVQVEGKSC CRSTLGRNCY NLCRVRGAQK LCANACRCKL
     TSGLKCPSSF PKLALVSNSD EPDTIDYCNL GCRASMCDYM VNAAADDEEM KLYVEHCSDA
     CVNFCNGDVG LTSLTA