ID   THN3_VISAL              Reviewed;         111 AA.
AC   P01538;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Viscotoxin-A3;
DE   Contains:
DE     RecName: Full=Viscotoxin-A3;
DE   Contains:
DE     RecName: Full=Acidic protein;
DE   Flags: Precursor;
GN   Name=THI2.1;
OS   Viscum album (European mistletoe).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Santalales; Viscaceae; Viscum.
OX   NCBI_TaxID=3972;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1710983; DOI=10.1111/j.1432-1033.1991.tb16049.x;
RA   Schrader G., Apel K.;
RT   "Isolation and characterization of cDNAs encoding viscotoxins of mistletoe
RT   (Viscum album).";
RL   Eur. J. Biochem. 198:549-553(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-72.
RX   PubMed=5719166; DOI=10.3891/acta.chem.scand.22-2624;
RA   Samuelsson G., Seger L., Olson T.;
RT   "The amino acid sequence of oxidized viscotoxin A3 from the European
RT   mistletoe (Viscum album L, Loranthaceae).";
RL   Acta Chem. Scand. 22:2624-2642(1968).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=4941626; DOI=10.3891/acta.chem.scand.25-2048;
RA   Samuelsson G., Pettersson B.;
RT   "The disulfide bonds of viscotoxin A3 from the European mistletoe (Viscum
RT   album L., Loranthaceae).";
RL   Acta Chem. Scand. 25:2048-2054(1971).
RN   [4]
RP   STRUCTURE BY NMR OF 73-111.
RX   PubMed=10947973; DOI=10.1042/bj3500569;
RA   Romagnoli S., Ugolini R., Fogolari F., Schaller G., Urech K.,
RA   Giannattasio M., Ragona L., Molinari H.;
RT   "NMR structural determination of viscotoxin A3 from Viscum album L.";
RL   Biochem. J. 350:569-577(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; S16099; S16099.
DR   PDB; 1ED0; NMR; -; A=27-72.
DR   PDB; 1OKH; X-ray; 1.75 A; A/B=27-72.
DR   PDB; 7PVB; NMR; -; A=27-72.
DR   PDBsum; 1ED0; -.
DR   PDBsum; 1OKH; -.
DR   PDBsum; 7PVB; -.
DR   AlphaFoldDB; P01538; -.
DR   SMR; P01538; -.
DR   EvolutionaryTrace; P01538; -.
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   Secreted; Signal; Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:5719166"
FT   CHAIN           27..72
FT                   /note="Viscotoxin-A3"
FT                   /id="PRO_0000034137"
FT   CHAIN           73..111
FT                   /note="Acidic protein"
FT                   /id="PRO_0000034138"
FT   DISULFID        29..66
FT                   /evidence="ECO:0000269|PubMed:4941626"
FT   DISULFID        30..58
FT                   /evidence="ECO:0000269|PubMed:4941626"
FT   DISULFID        42..52
FT                   /evidence="ECO:0000269|PubMed:4941626"
FT   CONFLICT        69..71
FT                   /note="DYP -> YPD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:1OKH"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:1OKH"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:1OKH"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1OKH"
SQ   SEQUENCE   111 AA;  11620 MW;  749F7D70CA0BDF96 CRC64;
     MEVVRGSSLV LLVLLLGALL VSQVESKSCC PNTTGRNIYN ACRLTGAPRP TCAKLSGCKI
     ISGSTCPSDY PKFYCTLGCE SSQCATNSNG DAEAVRCKTA CSDLCQDVDD A