CYHEE_AFREN
ID CYHEE_AFREN Reviewed; 30 AA.
AC C0HLN9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=Cyclotide hyen-E {ECO:0000303|PubMed:32414842};
OS Afrohybanthus enneaspermus (Spade flower) (Viola enneasperma).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Afrohybanthus.
OX NCBI_TaxID=212266 {ECO:0000303|PubMed:32414842};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY, DOMAIN,
RP AND DISULFIDE BONDS.
RX PubMed=32414842; DOI=10.1074/jbc.ra120.012627;
RA Du Q., Chan L.Y., Gilding E.K., Henriques S.T., Condon N.D., Ravipati A.S.,
RA Kaas Q., Huang Y.H., Craik D.J.;
RT "Discovery and mechanistic studies of cytotoxic cyclotides from the
RT medicinal herb Hybanthus enneaspermus.";
RL J. Biol. Chem. 295:10911-10925(2020).
CC -!- FUNCTION: Probably participates in a plant defense mechanism (By
CC similarity). Has cytotoxic activity against HUVEC cells (LC(50)= 2.17
CC uM) and various cancer cells including HeLa (LC(50)= 3.05 uM), MCF-7
CC and K562 (PubMed:32414842). Displays very weak hemolytic activity
CC (PubMed:32414842). Binds to and induces leakage in phospholipd
CC membranes, particularly ones containing 1-palmitoyl-2-
CC oleophosphatidylethanolamine (POPE) (PubMed:32414842).
CC {ECO:0000255|PROSITE-ProRule:PRU00395, ECO:0000269|PubMed:32414842}.
CC -!- TISSUE SPECIFICITY: Detected in stems (at protein level).
CC {ECO:0000269|PubMed:32414842}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- MASS SPECTROMETRY: Mass=3232.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:32414842};
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:0000255|PROSITE-ProRule:PRU00395}.
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DR AlphaFoldDB; C0HLN9; -.
DR SMR; C0HLN9; -.
DR GO; GO:0051715; P:cytolysis in another organism; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT PEPTIDE 1..30
FT /note="Cyclotide hyen-E"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT /id="PRO_0000450761"
FT DISULFID 4..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:32414842"
FT DISULFID 8..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:32414842"
FT DISULFID 13..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:32414842"
FT CROSSLNK 1..30
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000250|UniProtKB:C0HKH0"
SQ SEQUENCE 30 AA; 3259 MW; 9F4A0A59933636A0 CRC64;
GVPCGESCVY IPCFTGIINC SCRDKVCYNN
