CYO9_VIOBI
ID CYO9_VIOBI Reviewed; 103 AA.
AC B1NRR2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Cycloviolacin-O9;
DE AltName: Full=Vbc5;
DE Flags: Precursor; Fragment;
OS Viola biflora (Yellow wood violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=214529;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABW08094.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-99, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000269|PubMed:18191970};
RX PubMed=18191970; DOI=10.1016/j.phytochem.2007.10.023;
RA Herrmann A., Burman R., Mylne J.S., Karlsson G., Gullbo J., Craik D.J.,
RA Clark R.J., Goeransson U.;
RT "The alpine violet, Viola biflora, is a rich source of cyclotides with
RT potent cytotoxicity.";
RL Phytochemistry 69:939-952(2008).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P56871}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:18191970}.
CC -!- MASS SPECTROMETRY: Mass=3140; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18191970};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
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 EMBL; EU046622; ABW08094.1; -; mRNA.
DR AlphaFoldDB; B1NRR2; -.
DR SMR; B1NRR2; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012323; Cyclotide_bracelet_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT SIGNAL <1..9
FT /evidence="ECO:0000250|UniProtKB:Q5USN8"
FT PROPEP 10..69
FT /evidence="ECO:0000269|PubMed:18191970"
FT /id="PRO_0000341442"
FT PEPTIDE 70..99
FT /note="Cycloviolacin-O9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:18191970"
FT /id="PRO_0000341443"
FT PROPEP 100..103
FT /evidence="ECO:0000269|PubMed:18191970"
FT /id="PRO_0000341444"
FT DISULFID 73..89
FT /evidence="ECO:0000250|UniProtKB:P56871,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 77..91
FT /evidence="ECO:0000250|UniProtKB:P56871,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 82..96
FT /evidence="ECO:0000250|UniProtKB:P56871,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 70..99
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:18191970"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABW08094.1"
SQ SEQUENCE 103 AA; 10997 MW; DCA727577637AC9B CRC64;
AAFALPAFAS FEKDVITPAA LEAVLNRKAP LYNIMMENDA ILNVIANVKT VISNPVLEEA
LLKTNHGVNG IPCGESCVWI PCLTSAVGCS CKSKVCYRNS LDN