THNA_HORVU
ID THNA_HORVU Reviewed; 127 AA.
AC P01545;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Alpha-hordothionin;
DE AltName: Full=Purothionin II;
DE Contains:
DE RecName: Full=Alpha-hordothionin;
DE Contains:
DE RecName: Full=Acidic protein;
DE Flags: Precursor;
GN Name=THI1.1;
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].
RX PubMed=3082629; DOI=10.1111/j.1432-1033.1986.tb09557.x;
RA Ponz F., Paz-Ares J., Hernandez-Lucas C., Garcia-Olmedo F., Carbonero P.;
RT "Cloning and nucleotide sequence of a cDNA encoding the precursor of the
RT barley toxin alpha-hordothionin.";
RL Eur. J. Biochem. 156:131-135(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2850969; DOI=10.1016/0378-1119(88)90199-0;
RA Rodriguez-Palenzuela P., Pintor-Toro J.A., Carbonero P., Garcia-Olmedo F.;
RT "Nucleotide sequence and endosperm-specific expression of the structural
RT gene for the toxin alpha-hordothionin in barley (Hordeum vulgare L.).";
RL Gene 70:271-281(1988).
RN [3]
RP PROTEIN SEQUENCE OF 19-63.
RX PubMed=6987216; DOI=10.1093/oxfordjournals.jbchem.a132777;
RA Ozaki Y., Wada K., Hase T., Matsubara H., Nakanishi T., Yoshizumi H.;
RT "Amino acid sequence of a purothionin homolog from barley flour.";
RL J. Biochem. 87:549-555(1980).
RN [4]
RP PROTEIN SEQUENCE OF 19-27.
RC STRAIN=cv. Bomi; TISSUE=Starchy endosperm;
RX PubMed=11271488;
RX DOI=10.1002/1522-2683(200011)21:17<3693::aid-elps3693>3.0.co;2-i;
RA Kristoffersen H.E., Flengsrud R.;
RT "Separation and characterization of basic barley seed proteins.";
RL Electrophoresis 21:3693-3700(2000).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the plant thionin (TC 1.C.44) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32966.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X05901; CAA29330.1; -; mRNA.
DR EMBL; M23080; AAA32966.1; ALT_INIT; Genomic_DNA.
DR PIR; JA0087; VSBH2.
DR AlphaFoldDB; P01545; -.
DR SMR; P01545; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0072570.1; HORVU.MOREX.r2.1HG0072570.1; HORVU.MOREX.r2.1HG0072570.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0072590.1.mrna1; HORVU.MOREX.r2.1HG0072590.1.mrna1; HORVU.MOREX.r2.1HG0072590.1.
DR Gramene; HORVU.MOREX.r2.1HG0072570.1; HORVU.MOREX.r2.1HG0072570.1; HORVU.MOREX.r2.1HG0072570.
DR Gramene; HORVU.MOREX.r2.1HG0072590.1.mrna1; HORVU.MOREX.r2.1HG0072590.1.mrna1; HORVU.MOREX.r2.1HG0072590.1.
DR ExpressionAtlas; P01545; 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 Direct protein sequencing; Disulfide bond; Plant defense; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:11271488,
FT ECO:0000269|PubMed:6987216"
FT CHAIN 19..63
FT /note="Alpha-hordothionin"
FT /id="PRO_0000034112"
FT CHAIN 64..127
FT /note="Acidic protein"
FT /id="PRO_0000034113"
FT DISULFID 21..57
FT DISULFID 22..49
FT DISULFID 30..47
FT DISULFID 34..43
SQ SEQUENCE 127 AA; 13597 MW; 70C1BD787A9D1C46 CRC64;
MVCLLILGLV LEQVQVEGKS CCRSTLGRNC YNLCRVRGAQ KLCAGVCRCK LTSSGKCPTG
FPKLALVSNS DEPDTVKYCN LGCRASMCDY MVNAAADDEE MKLYLENCGD ACVNFCNGDA
GLTSLTA