CYO2_VIOOD
ID CYO2_VIOOD Reviewed; 30 AA.
AC P58434;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Cycloviolacin-O2;
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]
RP PROTEIN SEQUENCE.
RX PubMed=10600388; DOI=10.1006/jmbi.1999.3383;
RA Craik D.J., Daly N.L., Bond T., Waine C.;
RT "Plant cyclotides: a unique family of cyclic and knotted proteins that
RT defines the cyclic cystine knot structural motif.";
RL J. Mol. Biol. 294:1327-1336(1999).
RN [2]
RP PROTEIN SEQUENCE, FUNCTION, 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 [3]
RP FUNCTION.
RX PubMed=12477048;
RA Lindholm P., Goransson U., Johansson S., Claeson P., Gullbo J., Larsson R.,
RA Bohlin L., Backlund A.;
RT "Cyclotides: a novel type of cytotoxic agents.";
RL Mol. Cancer Ther. 1:365-369(2002).
RN [4]
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. Has
CC strong cytotoxic activity against a variety of drug-resistant and drug-
CC sensitive human tumor cell lines, and against primary chronic
CC lymphocytic leukemia and ovarian carcinoma cells. Has weaker cytotoxic
CC activity against normal lymphocytes. Has hemolytic activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00395, ECO:0000269|PubMed:12477048,
CC ECO:0000269|PubMed:16872274}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, petals, petioles, roots and
CC 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 -!- PTM: This is a cyclic peptide.
CC -!- MASS SPECTROMETRY: Mass=3138.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16872274};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet 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:0000305}.
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DR PDB; 2KCG; NMR; -; A=1-30.
DR PDB; 2KNM; NMR; -; A=1-30.
DR PDB; 2KNN; NMR; -; A=1-30.
DR PDB; 7RMQ; X-ray; 1.17 A; A/B=2-30.
DR PDB; 7RMR; X-ray; 1.04 A; A/B=2-30.
DR PDB; 7RMS; X-ray; 1.10 A; A/B=2-30.
DR PDBsum; 2KCG; -.
DR PDBsum; 2KNM; -.
DR PDBsum; 2KNN; -.
DR PDBsum; 7RMQ; -.
DR PDBsum; 7RMR; -.
DR PDBsum; 7RMS; -.
DR AlphaFoldDB; P58434; -.
DR BMRB; P58434; -.
DR SMR; P58434; -.
DR EvolutionaryTrace; P58434; -.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012323; Cyclotide_bracelet_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR PIRSF; PIRSF037891; Cycloviolacin; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Knottin; Plant defense.
FT PEPTIDE 1..30
FT /note="Cycloviolacin-O2"
FT /id="PRO_0000043610"
FT DISULFID 4..20
FT DISULFID 8..22
FT DISULFID 13..27
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:7RMR"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7RMR"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:7RMR"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7RMR"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7RMR"
SQ SEQUENCE 30 AA; 3165 MW; 19D19A52EACD5FE5 CRC64;
GIPCGESCVW IPCISSAIGC SCKSKVCYRN
