CYH1_VIOHE
ID CYH1_VIOHE Reviewed; 30 AA.
AC P58433;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Cycloviolacin-H1;
OS Viola hederacea (Australian violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=180952;
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).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
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 -!- 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 AlphaFoldDB; P58433; -.
DR SMR; P58433; -.
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 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 Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT PEPTIDE 1..30
FT /note="Cycloviolacin-H1"
FT /id="PRO_0000043607"
FT DISULFID 4..20
FT DISULFID 8..22
FT DISULFID 13..27
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
SQ SEQUENCE 30 AA; 3156 MW; BF372A52E0CDFFE3 CRC64;
GIPCGESCVY IPCLTSAIGC SCKSKVCYRN