ID   KAB10_OLDAF             Reviewed;          30 AA.
AC   P85128;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Kalata-B10;
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, MASS SPECTROMETRY, AND MODIFICATION AT TRP-24.
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 peptide occurs in both cyclic and linear forms. The linear
CC       form contains unmodified Trp-24, the cyclic peptide occurs in two forms
CC       with unmodified Trp-24, and with Trp-24 oxidized to form
CC       oxindolylalanine. Oxidation is enhanced by exposure to sunlight.
CC       {ECO:0000269|PubMed:17534989}.
CC   -!- MASS SPECTROMETRY: Mass=3030.5; Method=Electrospray; Note=Cyclic form.;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- MASS SPECTROMETRY: Mass=3048.5; Method=Electrospray; Note=Linear form.;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- MASS SPECTROMETRY: Mass=3046.5; Method=Electrospray; Note=With
CC       oxindolylalanine.; Evidence={ECO:0000269|PubMed:17534989};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- CAUTION: The oxidation form of Trp-24 is subject of controversy and
CC       could be the artifactual result of sample handling.
CC       {ECO:0000305|PubMed:17534989}.
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DR   AlphaFoldDB; P85128; -.
DR   SMR; P85128; -.
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   Direct protein sequencing; Disulfide bond; Knottin; Plant defense.
FT   PEPTIDE         1..30
FT                   /note="Kalata-B10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:17534989"
FT                   /id="PRO_0000294957"
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..27
FT                   /evidence="ECO:0000250|UniProtKB:P83836,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..30
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000269|PubMed:17534989"
SQ   SEQUENCE   30 AA;  3054 MW;  C8626F2FCF6D26EC CRC64;
     GLPTCGETCF GGTCNTPGCS CSSWPICTRD