THNB_WHEAT
ID THNB_WHEAT Reviewed; 136 AA.
AC P01543;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Purothionin A-1;
DE AltName: Full=Beta-purothionin;
DE AltName: Full=Purothionin A-I;
DE Contains:
DE RecName: Full=Purothionin A-1;
DE Contains:
DE RecName: Full=Acidic protein;
DE Flags: Precursor;
GN Name=THI1.3;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rosella;
RA Hughes P.A., Llewellyn D.L., Whitecross M.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 28-72.
RC STRAIN=cv. Manitoba 3;
RX PubMed=914810; DOI=10.1093/oxfordjournals.jbchem.a131752;
RA Ohtani S., Okada T., Yoshizumi H., Kagamiyama H.;
RT "Complete primary structures of two subunits of purothionin A, a lethal
RT protein for brewer's yeast from wheat flour.";
RL J. Biochem. 82:753-767(1977).
RN [3]
RP PROTEIN SEQUENCE OF 28-72.
RA Ohtani S., Okada T., Kagamiyama H., Yoshizumi H.;
RT "The amino acid sequence of purothionin A, a lethal toxic protein to
RT brewer's yeast from wheat.";
RL Agric. Biol. Chem. 39:2269-2270(1975).
RN [4]
RP PROTEIN SEQUENCE OF 28-72.
RX PubMed=990986; DOI=10.1139/o76-120;
RA Mak A.S., Jones B.L.;
RT "The amino acid sequence of wheat beta-purothionin.";
RL Can. J. Biochem. 54:835-842(1976).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=15299761; DOI=10.1107/s0907444995002976;
RA Stec B., Rao U., Teeter M.M.;
RT "Refinement of purothionins reveals solute particles important for lattice
RT formation and toxicity. Part 2: structure of beta-purothionin at 1.7-A
RT resolution.";
RL Acta Crystallogr. D 51:914-924(1995).
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}.
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DR EMBL; AF004018; AAB71137.1; -; mRNA.
DR PDB; 1BHP; X-ray; 1.70 A; A=28-72.
DR PDBsum; 1BHP; -.
DR AlphaFoldDB; P01543; -.
DR SMR; P01543; -.
DR Allergome; 9834; Tri a 37.
DR TCDB; 1.C.44.1.1; the plant thionine (pt) family.
DR PRIDE; P01543; -.
DR EvolutionaryTrace; P01543; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P01543; 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; Direct protein sequencing; Disulfide bond; Plant defense;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:914810,
FT ECO:0000269|PubMed:990986, ECO:0000269|Ref.3"
FT CHAIN 28..72
FT /note="Purothionin A-1"
FT /id="PRO_0000034130"
FT CHAIN 73..136
FT /note="Acidic protein"
FT /id="PRO_0000034131"
FT DISULFID 30..66
FT DISULFID 31..58
FT DISULFID 39..56
FT DISULFID 43..52
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1BHP"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1BHP"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1BHP"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1BHP"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1BHP"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1BHP"
SQ SEQUENCE 136 AA; 14625 MW; A855C815519EDA24 CRC64;
MGSKGLKGVM VCLLILGLVL EQVQVEGKSC CKSTLGRNCY NLCRARGAQK LCANVCRCKL
TSGLSCPKDF PKLVLESNSD EPDTMEYCNL GCRSSLCDYI VNAAADDEEM KLYVEQCGDA
CVNFCNADAG LTSLDA