CYC8_CHACT
ID CYC8_CHACT Reviewed; 75 AA.
AC I0B6F5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Chassatide C8 {ECO:0000303|PubMed:22467870};
DE AltName: Full=Cyclotide chaC8 {ECO:0000303|PubMed:22467870};
DE Flags: Precursor;
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:AFH57355.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-75, 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=3084; 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}.
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DR EMBL; JQ309965; AFH57355.1; -; mRNA.
DR AlphaFoldDB; I0B6F5; -.
DR SMR; I0B6F5; -.
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; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..45
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22467870"
FT /id="PRO_0000440231"
FT PEPTIDE 46..75
FT /note="Chassatide C8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:22467870"
FT /id="PRO_0000440232"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 54..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 59..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
SQ SEQUENCE 75 AA; 8231 MW; 7276042F4768258C CRC64;
MAKFANYLML FLLVASLVML EAQSSDTIKA PDWGKRLLMN HDSDLGAIPC GESCVWIPCI
STVIGCSCSN KVCYR
