ID   KAB12_OLDAF             Reviewed;          28 AA.
AC   P85130;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Kalata-B12;
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, 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:0000269|PubMed:17534989}.
CC   -!- MASS SPECTROMETRY: Mass=2880.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255}.
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:0000269|PubMed:17534989}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PDB; 2KVX; NMR; -; A=1-28.
DR   PDBsum; 2KVX; -.
DR   AlphaFoldDB; P85130; -.
DR   SMR; P85130; -.
DR   EvolutionaryTrace; P85130; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..28
FT                   /note="Kalata-B12"
FT                   /evidence="ECO:0000269|PubMed:17534989"
FT                   /id="PRO_0000294959"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000250|UniProtKB:P83836"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000250|UniProtKB:P83836"
FT   DISULFID        13..25
FT                   /evidence="ECO:0000250|UniProtKB:P83836"
FT   CROSSLNK        1..28
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000269|PubMed:17534989"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2KVX"
FT   TURN            8..11
FT                   /evidence="ECO:0007829|PDB:2KVX"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:2KVX"
SQ   SEQUENCE   28 AA;  2904 MW;  FB121B7F6D0694F2 CRC64;
     GSLCGDTCFV LGCNDSSCSC NYPICVKD