ID   KAB4_OLDAF              Reviewed;          29 AA.
AC   P83938;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Kalata-B4;
OS   Oldenlandia affinis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Spermacoceae;
OC   Hedyotis-Oldenlandia complex; Oldenlandia.
OX   NCBI_TaxID=60225;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RX   PubMed=10600388; DOI=10.1006/jmbi.1999.3383;
RA   Craik D.J., Daly N.L., Bond T., Waine C.;
RT   "Plant cyclotides: a unique family of cyclic and knotted proteins that
RT   defines the cyclic cystine knot structural motif.";
RL   J. Mol. Biol. 294:1327-1336(1999).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=17534989; DOI=10.1002/cbic.200700097;
RA   Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L.,
RA   Craik D.J.;
RT   "The cyclotide fingerprint in Oldenlandia affinis: elucidation of
RT   chemically modified, linear and novel macrocyclic peptides.";
RL   ChemBioChem 8:1001-1011(2007).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P83836}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:10600388}.
CC   -!- MASS SPECTROMETRY: Mass=2893.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17534989};
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; 1ZNU; NMR; -; A=1-29.
DR   PDB; 7RFA; NMR; -; A=1-28.
DR   PDBsum; 1ZNU; -.
DR   PDBsum; 7RFA; -.
DR   AlphaFoldDB; P83938; -.
DR   BMRB; P83938; -.
DR   SMR; P83938; -.
DR   EvolutionaryTrace; P83938; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..29
FT                   /note="Kalata-B4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:10600388"
FT                   /id="PRO_0000043629"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:P83836,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P83836,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250|UniProtKB:P83836,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..29
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000269|PubMed:10600388,
FT                   ECO:0000269|PubMed:17534989"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:7RFA"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:7RFA"
SQ   SEQUENCE   29 AA;  2917 MW;  3CCE6BEE3F82FA18 CRC64;
     GLPVCGETCV GGTCNTPGCT CSWPVCTRD