CYC2_CHACT
ID CYC2_CHACT Reviewed; 77 AA.
AC I0B6F2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Chassatide C2 {ECO:0000303|PubMed:22467870};
DE AltName: Full=Cyclotide chaC2 {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:AFH57352.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-75, FUNCTION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP OXIDATION AT MET-63.
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: Chassatide C2: Probably participates in a plant defense
CC mechanism (Probable). Has no activity against bacteria up to a
CC concentration of 80 uM (PubMed:22467870). Has cytotoxic but no
CC hemolytic activity (PubMed:22467870). {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU00395, ECO:0000269|PubMed:22467870}.
CC -!- FUNCTION: Chassatide C2A: Probably participates in a plant defense
CC mechanism (Probable). Has no activity against bacteria up to a
CC concentration of 80 uM (PubMed:22467870). Has no cytotoxic and no
CC hemolytic activity (PubMed:22467870). {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU00395, ECO:0000269|PubMed:22467870}.
CC -!- TISSUE SPECIFICITY: Expressed in fruit, pedicel and stem but not in
CC leaf and root (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 -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- MASS SPECTROMETRY: Mass=3282; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- MASS SPECTROMETRY: Mass=3298; Method=MALDI; Note=Chassatide chaC2A.;
CC Evidence={ECO:0000269|PubMed:22467870};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR EMBL; JQ309962; AFH57352.1; -; mRNA.
DR AlphaFoldDB; I0B6F2; -.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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 SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Disulfide bond; Knottin; Oxidation;
KW Plant defense; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..44
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22467870"
FT /id="PRO_0000440220"
FT PEPTIDE 45..75
FT /note="Chassatide C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:22467870"
FT /id="PRO_0000440221"
FT PROPEP 76..77
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22467870"
FT /id="PRO_0000440222"
FT MOD_RES 63
FT /note="Methionine sulfoxide; in form chassatide chaC2A"
FT /evidence="ECO:0000269|PubMed:22467870"
FT DISULFID 48..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 52..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 57..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 45..75
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:22467870"
SQ SEQUENCE 77 AA; 8502 MW; 741A6D0BB71DB796 CRC64;
MAKFANYLML FLLVASLVML EAQSSDTIKV PDLGKRLLMN RDPNGIPCAE SCVWIPCTIT
ALMGCSCKNN VCYNNEL
