CYV3_VIOOD
ID CYV3_VIOOD Reviewed; 28 AA.
AC C0HL16;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Cyclotide vodo I3 {ECO:0000303|PubMed:28621949};
OS Viola odorata (Sweet violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=97441 {ECO:0000303|PubMed:28621949};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY,
RP PRESENCE OF DISULFIDE BONDS, AND CYCLIZATION.
RX PubMed=28621949; DOI=10.1021/acs.jnatprod.6b01004;
RA Narayani M., Chadha A., Srivastava S.;
RT "Cyclotides from the Indian Medicinal Plant Viola odorata (Banafsha):
RT Identification and Characterization.";
RL J. Nat. Prod. 80:1972-1980(2017).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:28621949}.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:28621949}.
CC -!- MASS SPECTROMETRY: Mass=2840.19; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:28621949};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000305|PubMed:28621949}.
CC -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC similarity to Oak1 (kalata B1) for which the DNA sequence is known.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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 AlphaFoldDB; C0HL16; -.
DR SMR; C0HL16; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT PEPTIDE 1..28
FT /note="Cyclotide vodo I3"
FT /evidence="ECO:0000269|PubMed:28621949"
FT /id="PRO_0000441791"
FT DISULFID 4..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 8..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 13..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
SQ SEQUENCE 28 AA; 2866 MW; B539C1E5937F9D44 CRC64;
GVFCGEPCIK ASCSIPGCEC IAGLCYKN