CYVA_LEOCM
ID CYVA_LEOCM Reviewed; 31 AA.
AC P84637;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Cycloviolin-A;
OS Leonia cymosa (Sacha uba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Leonia.
OX NCBI_TaxID=341676;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC STRAIN=Q65T-5650 {ECO:0000269|PubMed:10813905};
RC TISSUE=Bark {ECO:0000269|PubMed:10813905};
RX PubMed=10813905; DOI=10.1021/jo990952r;
RA Hallock Y.F., Sowder R.C. II, Pannell L.K., Hughes C.B., Johnson D.G.,
RA Gulakowski R., Cardellina J.H. Jr., Boyd M.R.;
RT "Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa.";
RL J. Org. Chem. 65:124-128(2000).
CC -!- FUNCTION: Probably participates in a plant defense mechanism. Has anti-
CC HIV activity. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:10813905, ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P56879}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:10813905}.
CC -!- MASS SPECTROMETRY: Mass=3213.4; Method=FAB;
CC Evidence={ECO:0000269|PubMed:10813905};
CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet 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 AlphaFoldDB; P84637; -.
DR SMR; P84637; -.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; 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; PS51052; CYCLOTIDE; 1.
DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE 1: Evidence at protein level;
KW Antiviral protein; Direct protein sequencing; Disulfide bond; Knottin;
KW Plant defense.
FT PEPTIDE 1..31
FT /note="Cycloviolin-A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:10813905"
FT /id="PRO_0000044697"
FT DISULFID 5..21
FT /evidence="ECO:0000250|UniProtKB:P56879,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 9..23
FT /evidence="ECO:0000250|UniProtKB:P56879,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 14..28
FT /evidence="ECO:0000250|UniProtKB:P56879,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 1..31
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:10813905"
SQ SEQUENCE 31 AA; 3236 MW; 30C19A52F6B17ABA CRC64;
GVIPCGESCV FIPCISAAIG CSCKNKVCYR N