CYC7_CHACT
ID CYC7_CHACT Reviewed; 64 AA.
AC I0B6F4;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Chassatide C7 {ECO:0000312|EMBL:AFH57354.1};
DE AltName: Full=Cyclotide chaC7 {ECO:0000303|PubMed:22467870};
DE Flags: Precursor; Fragment;
OS Chassalia chartacea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Palicoureeae;
OC Chassalia.
OX NCBI_TaxID=510798;
RN [1] {ECO:0000312|EMBL:AFH57354.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-64, FUNCTION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22467870; DOI=10.1074/jbc.m111.338970;
RA Nguyen G.K., Lim W.H., Nguyen P.Q., Tam J.P.;
RT "Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from
RT Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities.";
RL J. Biol. Chem. 287:17598-17607(2012).
CC -!- FUNCTION: Probably participates in a plant defense mechanism
CC (Probable). Active against E.coli ATTC25922 but not against S.aureus
CC ATCC 12600 or S.epidermidis ATCC 14990 (PubMed:22467870). Has cytotoxic
CC and hemolytic activity (PubMed:22467870). {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU00395, ECO:0000269|PubMed:22467870}.
CC -!- TISSUE SPECIFICITY: Expressed in fruit, pedicel, root and stem but not
CC in leaf (at protein level). {ECO:0000269|PubMed:22467870}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2955; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- CAUTION: The mature peptide is linear as it lacks the C-terminal
CC Asp/Asn residue required for cyclization.
CC {ECO:0000269|PubMed:22467870}.
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; JQ309964; AFH57354.1; -; mRNA.
DR AlphaFoldDB; I0B6F4; -.
DR SMR; I0B6F4; -.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; 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 SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Knottin; Plant defense.
FT PROPEP <1..35
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22467870"
FT /id="PRO_0000440229"
FT PEPTIDE 36..64
FT /note="Chassatide C7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:22467870"
FT /id="PRO_0000440230"
FT DISULFID 39..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 43..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 48..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AFH57354.1"
SQ SEQUENCE 64 AA; 6926 MW; FD3228BEDB9B2894 CRC64;
VLVASLVMLE AQSSDTIQVP DWGKRLLMNH DSNRVGIPCG ESCVWIPCLT AIAGCSCKNK
VCYT
