VARA_VIOOD
ID VARA_VIOOD Reviewed; 207 AA.
AC Q5USN7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Varv peptide A/Kalata-B1;
DE AltName: Full=Cyclotide k1;
DE Contains:
DE RecName: Full=Varv peptide A;
DE Contains:
DE RecName: Full=Kalata-B1;
DE Flags: Precursor;
GN Name=Vok1 {ECO:0000303|PubMed:15328347};
OS Viola odorata (Sweet violet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Violaceae; Viola.
OX NCBI_TaxID=97441;
RN [1] {ECO:0000312|EMBL:AAU04395.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf {ECO:0000312|EMBL:AAU04395.1};
RX PubMed=15328347; DOI=10.1074/jbc.m407421200;
RA Dutton J.L., Renda R.F., Waine C., Clark R.J., Daly N.L., Jennings C.V.,
RA Anderson M.A., Craik D.J.;
RT "Conserved structural and sequence elements implicated in the processing of
RT gene-encoded circular proteins.";
RL J. Biol. Chem. 279:46858-46867(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203, FUNCTION, AND MASS
RP SPECTROMETRY.
RX PubMed=16872274; DOI=10.1042/bj20060627;
RA Ireland D.C., Colgrave M.L., Craik D.J.;
RT "A novel suite of cyclotides from Viola odorata: sequence variation and the
RT implications for structure, function and stability.";
RL Biochem. J. 400:1-12(2006).
CC -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC hemolytic activity. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC ECO:0000269|PubMed:16872274, ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P58446}.
CC -!- PTM: Varv peptide A and kalata-B1 are cyclic peptides.
CC {ECO:0000269|PubMed:16872274}.
CC -!- MASS SPECTROMETRY: [Varv peptide A]: Mass=2878.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16872274};
CC -!- MASS SPECTROMETRY: [Kalata-B1]: Mass=2890.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16872274};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR EMBL; AY630566; AAU04395.1; -; mRNA.
DR PDB; 1WN4; NMR; -; A=150-177.
DR PDBsum; 1WN4; -.
DR AlphaFoldDB; Q5USN7; -.
DR SMR; Q5USN7; -.
DR TCDB; 1.A.118.1.3; the plant cycltide (cyclotide) family.
DR EvolutionaryTrace; Q5USN7; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 3.
DR SUPFAM; SSF57038; SSF57038; 3.
DR PROSITE; PS51052; CYCLOTIDE; 3.
DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Knottin; Plant defense; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..66
FT /evidence="ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294967"
FT PEPTIDE 67..95
FT /note="Varv peptide A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294968"
FT PROPEP 96..120
FT /evidence="ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294969"
FT PEPTIDE 121..149
FT /note="Kalata-B1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294970"
FT PROPEP 150..174
FT /evidence="ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294971"
FT PEPTIDE 175..203
FT /note="Varv peptide A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294972"
FT PROPEP 204..207
FT /evidence="ECO:0000269|PubMed:16872274"
FT /id="PRO_0000294973"
FT DISULFID 71..85
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 75..87
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 80..92
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 125..139
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 129..141
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 134..146
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 179..193
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 183..195
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT DISULFID 188..200
FT /evidence="ECO:0000250|UniProtKB:P58446,
FT ECO:0000255|PROSITE-ProRule:PRU00395"
FT CROSSLNK 67..95
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:16872274"
FT CROSSLNK 121..149
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:16872274"
FT CROSSLNK 175..203
FT /note="Cyclopeptide (Gly-Asn)"
FT /evidence="ECO:0000269|PubMed:16872274"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:1WN4"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1WN4"
SQ SEQUENCE 207 AA; 21334 MW; 960241C55F696F72 CRC64;
MKMFIVLVLS AAFALPAAFA TEQDVITLQA YEELLKNGAA NGMTKTVISS PVLEEALVSY
SKNKLGGLPV CGETCVGGTC NTPGCSCSWP VCTRNSLEST KSANPLLEEA LTAFAKKGLG
GLPVCGETCV GGTCNTPGCT CSWPVCTRNA LETQKPNHLL EEALVAFAKK GNLGGLPVCG
ETCVGGTCNT PGCSCSWPVC TRNALAM
