CYM45_MELRA
ID CYM45_MELRA Reviewed; 198 AA.
AC A9P3S1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Cyclotides mra4/mra5 {ECO:0000305};
DE Contains:
DE RecName: Full=Cyclotide mra4 {ECO:0000303|PubMed:19462049};
DE Contains:
DE RecName: Full=Cyclotide mra5 {ECO:0000303|PubMed:19462049};
DE Flags: Precursor;
OS Melicytus ramiflorus (Whitey wood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Melicytus.
OX NCBI_TaxID=316498 {ECO:0000303|PubMed:19462049};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-110 AND 164-193, MASS
RP SPECTROMETRY, AND PRESENCE OF DISULFIDE BONDS.
RC TISSUE=Leaf {ECO:0000303|PubMed:19462049};
RX PubMed=19462049; DOI=10.1039/b823020j;
RA Trabi M., Mylne J.S., Sando L., Craik D.J.;
RT "Circular proteins from Melicytus (Violaceae) refine the conserved protein
RT and gene architecture of cyclotides.";
RL Org. Biomol. Chem. 7:2378-2388(2009).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC {ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: These are cyclic peptides. {ECO:0000269|PubMed:19462049}.
CC -!- PTM: The mature peptides contain 3 disulfide bonds each.
CC {ECO:0000269|PubMed:19462049}.
CC -!- MASS SPECTROMETRY: [Cyclotide mra4]: Mass=3219; Method=Electrospray;
CC Note=Cyclotide mra4.; Evidence={ECO:0000269|PubMed:19462049};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR EMBL; EF103478; ABO21629.1; -; mRNA.
DR AlphaFoldDB; A9P3S1; -.
DR SMR; A9P3S1; -.
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; 2.
DR SUPFAM; SSF57038; SSF57038; 2.
DR PROSITE; PS51052; CYCLOTIDE; 2.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..79
FT /evidence="ECO:0000305"
FT /id="PRO_0000441833"
FT PEPTIDE 80..110
FT /note="Cyclotide mra4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:19462049"
FT /id="PRO_0000441834"
FT PROPEP 111..163
FT /evidence="ECO:0000305"
FT /id="PRO_0000441835"
FT PEPTIDE 164..193
FT /note="Cyclotide mra5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:19462049"
FT /id="PRO_0000441836"
FT PROPEP 194..198
FT /evidence="ECO:0000305"
FT /id="PRO_0000441837"
FT DISULFID 84..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 88..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 93..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 167..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 171..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 176..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
SQ SEQUENCE 198 AA; 20895 MW; CB13444F7D614916 CRC64;
MESNKMVVGV LLIAAFALPA LALFERDVIT HETIEAVLKK STPNSNTMLQ EDAINALTGK
TLISQTILEE TLLKNGVVGG SIPCGESCVY IPCISSLLGC SCKSKVCYKN SLALPTLEKD
VITPEALEAV LKSNGGAIVN TKTIISNAIF EETLLNNANH VLGGIPCAES CVYIPCLTSA
IGCSCKSKVC YRNSLALN
