VHL2_VIOHE
ID VHL2_VIOHE Reviewed; 30 AA.
AC P85231;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Leaf cyclotide 2;
DE AltName: Full=Vhl-2;
OS Viola hederacea (Australian violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=180952;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000269|PubMed:15824119};
RX PubMed=15824119; DOI=10.1074/jbc.m501737200;
RA Chen B., Colgrave M.L., Daly N.L., Rosengren K.J., Gustafson K.R.,
RA Craik D.J.;
RT "Isolation and characterization of novel cyclotides from Viola hederaceae:
RT solution structure and anti-HIV activity of vhl-1, a leaf-specific
RT expressed cyclotide.";
RL J. Biol. Chem. 280:22395-22405(2005).
RN [2]
RP FUNCTION, DISULFIDE BONDS, AND STRUCTURE BY NMR.
RX DOI=10.1071/CH10007;
RA Daly N.L., Chen B., Nguyencong P., Craik D.J.;
RT "Structure and activity of the leaf-specific cyclotide vhl-2.";
RL Aust. J. Chem. 63:771-778(2010).
CC -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC hemolytic activity. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|Ref.2, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15824119}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P56254}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:15824119}.
CC -!- MASS SPECTROMETRY: Mass=3172.58; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15824119};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC similarity to OAK1 (kalata-B1) for which the DNA sequence is known.
CC {ECO:0000305}.
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DR PDB; 2KUK; NMR; -; A=5-30.
DR PDBsum; 2KUK; -.
DR AlphaFoldDB; P85231; -.
DR SMR; P85231; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 1.
DR PIRSF; PIRSF037891; Cycloviolacin; 1.
DR SUPFAM; SSF57038; SSF57038; 1.
DR PROSITE; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Knottin; Plant defense.
FT PEPTIDE 1..30
FT /note="Leaf cyclotide 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:15824119"
FT /id="PRO_0000302129"
FT DISULFID 5..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|Ref.2"
FT DISULFID 9..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|Ref.2"
FT DISULFID 14..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|Ref.2"
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:15824119, ECO:0000269|Ref.2"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2KUK"
SQ SEQUENCE 30 AA; 3200 MW; AC596BCB2574C0FC CRC64;
GLPVCGETCF TGTCYTNGCT CDPWPVCTRN
