CYVE_VIOBI
ID CYVE_VIOBI Reviewed; 105 AA.
AC B1NRQ8; P85243;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Cyclotide vibi-E;
DE AltName: Full=Vbc1;
DE Flags: Precursor; Fragment;
OS Viola biflora (Yellow wood violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=214529;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABW08090.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-99, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000269|PubMed:18191970};
RX PubMed=18191970; DOI=10.1016/j.phytochem.2007.10.023;
RA Herrmann A., Burman R., Mylne J.S., Karlsson G., Gullbo J., Craik D.J.,
RA Clark R.J., Goeransson U.;
RT "The alpine violet, Viola biflora, is a rich source of cyclotides with
RT potent cytotoxicity.";
RL Phytochemistry 69:939-952(2008).
CC -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC cytotoxic activity, active against a human lymphoma cell line with an
CC IC(50) of 3.2 uM. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:18191970, ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P82230}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:18191970}.
CC -!- MASS SPECTROMETRY: Mass=3081; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18191970};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR EMBL; EU046618; ABW08090.1; -; mRNA.
DR AlphaFoldDB; B1NRQ8; -.
DR SMR; B1NRQ8; -.
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 Direct protein sequencing; Disulfide bond; Knottin; Plant defense; Signal.
FT SIGNAL <1..9
FT /evidence="ECO:0000250|UniProtKB:P58443"
FT PROPEP 10..69
FT /evidence="ECO:0000269|PubMed:18191970"
FT /id="PRO_0000341425"
FT PEPTIDE 70..99
FT /note="Cyclotide vibi-E"
FT /id="PRO_0000341426"
FT PROPEP 100..105
FT /evidence="ECO:0000269|PubMed:18191970"
FT /id="PRO_0000341427"
FT DISULFID 73..90
FT /evidence="ECO:0000250|UniProtKB:P82230,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 77..92
FT /evidence="ECO:0000250|UniProtKB:P82230,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 82..97
FT /evidence="ECO:0000250|UniProtKB:P82230,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 70..99
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:18191970"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABW08090.1"
SQ SEQUENCE 105 AA; 11068 MW; 3A680C6294765BE5 CRC64;
AAFALPALAS SFEKDVISFR AIQAVLEKRG LSKLEDDPVL SALAHTKTII SNPVIEEALL
NGANLKAGNG IPCAESCVWI PCTVTALIGC GCSNKVCYNS LQTKY