CYCM_PETHY
ID CYCM_PETHY Reviewed; 32 AA.
AC B3EWH7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Acyclotide phyb-M {ECO:0000303|PubMed:22700981};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, DISULFIDE BONDS, PYROGLUTAMATE
RP FORMATION AT GLN-1, AND MASS SPECTROMETRY.
RC TISSUE=Root {ECO:0000269|PubMed:22700981};
RX PubMed=22700981; DOI=10.1074/jbc.m112.370841;
RA Poth A.G., Mylne J.S., Grassl J., Lyons R.E., Millar A.H., Colgrave M.L.,
RA Craik D.J.;
RT "Cyclotides associate with leaf vasculature and are the products of a novel
RT precursor in Petunia (Solanaceae).";
RL J. Biol. Chem. 287:27033-27046(2012).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000250, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in midvein, lamina and periphery of
CC leaves (at protein level). {ECO:0000269|PubMed:22700981}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:22700981}.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:22700981}.
CC -!- MASS SPECTROMETRY: Mass=3387.47; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22700981};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255}.
CC -!- CAUTION: This peptide is linear but closely related to cyclotides.
CC Since in UniProtKB the primary structure is preferred to classify
CC proteins, the sequence is assigned to the cyclotide family.
CC {ECO:0000305}.
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DR AlphaFoldDB; B3EWH7; -.
DR SMR; B3EWH7; -.
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; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense;
KW Pyrrolidone carboxylic acid.
FT PEPTIDE 1..32
FT /note="Acyclotide phyb-M"
FT /evidence="ECO:0000269|PubMed:22700981"
FT /id="PRO_0000419341"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:22700981"
FT DISULFID 5..21
FT /evidence="ECO:0000250|UniProtKB:P56254"
FT DISULFID 9..23
FT /evidence="ECO:0000250|UniProtKB:P56254"
FT DISULFID 14..28
FT /evidence="ECO:0000250|UniProtKB:P56254"
FT UNSURE 3
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:22700981"
FT UNSURE 12
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:22700981"
FT UNSURE 18
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22700981"
FT UNSURE 19
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:22700981"
FT UNSURE 29
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:22700981"
SQ SEQUENCE 32 AA; 3413 MW; 0DD2133137DC33A2 CRC64;
QSISCAESCV WIPCATSLIG CSCVNSRCIY SK
