TRIC_VIOAR
ID TRIC_VIOAR Reviewed; 204 AA.
AC P0C589;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Pro-tricyclons;
DE Contains:
DE RecName: Full=Tricyclon-A;
DE Contains:
DE RecName: Full=Tricyclon-B;
DE Flags: Precursor;
OS Viola arvensis (European field pansy) (Field violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=97415;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, FUNCTION, STRUCTURE BY
RP NMR OF 73-105, DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15893660; DOI=10.1016/j.str.2005.02.013;
RA Mulvenna J.P., Sando L., Craik D.J.;
RT "Processing of a 22 kDa precursor protein to produce the circular protein
RT tricyclon A.";
RL Structure 13:691-701(2005).
CC -!- FUNCTION: Probably participates in a plant defense mechanism. Has a
CC weak hemolytic activity. {ECO:0000269|PubMed:15893660}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines those proteins as knottins.
CC -!- PTM: Proteolytically processed in two steps to yield first two linear
CC precursors, and then two cyclic peptides after removal of the N-
CC terminal repeats (NTR) and short tails.
CC -!- MISCELLANEOUS: Tricyclon-A and tricyclon-B are hybrids of the Bracelet
CC and Moebius subfamilies.
CC -!- SIMILARITY: Belongs to the cyclotide family. {ECO:0000305}.
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DR PDB; 1YP8; NMR; -; A=79-105.
DR PDBsum; 1YP8; -.
DR AlphaFoldDB; P0C589; -.
DR SMR; P0C589; -.
DR EvolutionaryTrace; P0C589; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 2.
DR SUPFAM; SSF57038; SSF57038; 2.
DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Knottin; Plant defense; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..204
FT /note="Pro-tricyclons"
FT /id="PRO_0000295770"
FT PROPEP 23..72
FT /note="NTR"
FT /id="PRO_0000295771"
FT PEPTIDE 73..105
FT /note="Tricyclon-A"
FT /id="PRO_0000295772"
FT PROPEP 106..118
FT /id="PRO_0000295773"
FT PROPEP 119..167
FT /note="NTR"
FT /id="PRO_0000295774"
FT PEPTIDE 168..200
FT /note="Tricyclon-B"
FT /id="PRO_0000295775"
FT PROPEP 201..204
FT /id="PRO_0000295776"
FT DISULFID 79..93
FT /evidence="ECO:0000269|PubMed:15893660"
FT DISULFID 83..95
FT /evidence="ECO:0000269|PubMed:15893660"
FT DISULFID 88..101
FT /evidence="ECO:0000269|PubMed:15893660"
FT DISULFID 174..188
FT /evidence="ECO:0000250"
FT DISULFID 178..190
FT /evidence="ECO:0000250"
FT DISULFID 183..196
FT /evidence="ECO:0000250"
FT CROSSLNK 73..105
FT /note="Cyclopeptide (Gly-Asn)"
FT CROSSLNK 168..200
FT /note="Cyclopeptide (Gly-Asn)"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1YP8"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1YP8"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1YP8"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1YP8"
SQ SEQUENCE 204 AA; 21820 MW; 76EAFD7DB07329C4 CRC64;
MKTMASFVLV LVAAFALPAA FASLETKDVI TRAAYEKLVE SGAIQGITMT KTIISNPILE
EALVAHFNRK LGGGTIFDCG ESCFLGTCYT KGCSCGEWKL CYGTNSLPES NNEKAMVASL
EKDVITRAAY ENLVNSGAIQ GITMTKTIIS NPILEEALVS HFNRKLGGGT IFDCGESCFL
GTCYTKGCSC GEWKLCYGEN SLAI