CYO23_VIOOD
ID CYO23_VIOOD Reviewed; 31 AA.
AC P85186;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Cycloviolacin-O23;
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;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX PubMed=16872274; DOI=10.1042/bj20060627;
RA Ireland D.C., Colgrave M.L., Craik D.J.;
RT "A novel suite of cyclotides from Viola odorata: sequence variation and the
RT implications for structure, function and stability.";
RL Biochem. J. 400:1-12(2006).
RN [2]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves but not in petals, petioles,
CC roots and runners (at protein level). {ECO:0000269|PubMed:28621949}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P58453}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:16872274}.
CC -!- MASS SPECTROMETRY: Mass=3137.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16872274};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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:0000269|PubMed:16872274}.
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DR AlphaFoldDB; P85186; -.
DR SMR; P85186; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT PEPTIDE 1..31
FT /note="Cycloviolacin-O23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294952"
FT DISULFID 5..19
FT /evidence="ECO:0000250|UniProtKB:P58453,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 9..21
FT /evidence="ECO:0000250|UniProtKB:P58453,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 14..28
FT /evidence="ECO:0000250|UniProtKB:P58453,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..31
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:16872274"
SQ SEQUENCE 31 AA; 3164 MW; 59B1ACD6EA385930 CRC64;
GLPTCGETCF GGTCNTPGCT CDSSWPICTH N