THNB_VISAL
ID THNB_VISAL Reviewed; 103 AA.
AC P08943; P01536; P84186;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Viscotoxin-B;
DE Contains:
DE RecName: Full=Viscotoxin-B;
DE AltName: Full=Viscotoxin-B2;
DE Contains:
DE RecName: Full=Acidic protein;
DE Flags: Precursor; Fragment;
GN Name=THI2.2;
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 7-52.
RX PubMed=5568678; DOI=10.1111/j.1432-1033.1971.tb01443.x;
RA Samuelsson G., Pettersson B.M.;
RT "The amino acid sequence of viscotoxin B from the European mistletoe
RT (Viscum album L, loranthaceae).";
RL Eur. J. Biochem. 21:86-89(1971).
RN [3]
RP PROTEIN SEQUENCE OF 7-52, FUNCTION, AND MASS SPECTROMETRY.
RA Kahle B., Debreczeni J.E., Sheldrick G.M., Zeeck A.;
RL Submitted (SEP-2004) to UniProtKB.
RN [4]
RP STRUCTURE BY NMR OF 7-52.
RX PubMed=12733989; DOI=10.1042/bj20030488;
RA Coulon A., Mosbah A., Lopez A., Sautereau A.-M., Schaller G., Urech K.,
RA Rouge P., Darbon H.;
RT "Comparative membrane interaction study of viscotoxins A3, A2 and B from
RT mistletoe (Viscum album) and connections with their structures.";
RL Biochem. J. 374:71-78(2003).
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. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: [Viscotoxin-B]: Mass=4852.5; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the plant thionin (TC 1.C.44) family.
CC {ECO:0000305}.
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DR PIR; A91187; VTVAB.
DR PDB; 1JMP; NMR; -; A=7-52.
DR PDB; 2V9B; X-ray; 1.05 A; A/B=7-52.
DR PDBsum; 1JMP; -.
DR PDBsum; 2V9B; -.
DR AlphaFoldDB; P08943; -.
DR SMR; P08943; -.
DR TCDB; 1.C.44.1.2; the plant thionine (pt) family.
DR EvolutionaryTrace; P08943; -.
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..6
FT /evidence="ECO:0000269|PubMed:5568678, ECO:0000269|Ref.3"
FT CHAIN 7..52
FT /note="Viscotoxin-B"
FT /id="PRO_0000034134"
FT PROPEP 53..72
FT /id="PRO_0000034135"
FT CHAIN 73..103
FT /note="Acidic protein"
FT /id="PRO_0000034136"
FT DISULFID 9..46
FT DISULFID 10..38
FT DISULFID 22..32
FT CONFLICT 17
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..51
FT /note="DYP -> YPD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2V9B"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2V9B"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:2V9B"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2V9B"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1JMP"
SQ SEQUENCE 103 AA; 11008 MW; 99E3DD135FEE0846 CRC64;
FRNVESKSCC PNTTGRNIYN TCRLGGGSRE RCASLSGCKI ISASTCPSDY PKFYCTLGCQ
SSKCASITTP PNSEVDAEAV RCKAACSNLC DFGVTTNQEI QDD