ID   PABR1_PALRI             Reviewed;          32 AA.
AC   B3EWF1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Parigidin-br1 {ECO:0000303|PubMed:22074926};
OS   Palicourea rigida.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Palicoureeae;
OC   Palicourea.
OX   NCBI_TaxID=96266;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, CYCLIZATION, AND MASS
RP   SPECTROMETRY.
RX   PubMed=22074926; DOI=10.1074/jbc.m111.294009;
RA   Pinto M.F., Fensterseifer I.C., Migliolo L., Sousa D.A., de Capdville G.,
RA   Arboleda-Valencia J.W., Colgrave M.L., Craik D.J., Magalhaes B.S.,
RA   Dias S.C., Franco O.L.;
RT   "Identification and structural characterization of novel cyclotide with
RT   activity against an insect pest of sugar cane.";
RL   J. Biol. Chem. 287:134-147(2012).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Reduces
CC       growth of and increases mortality in larvae of D.saccharalis. Kills
CC       cultured SF-9 cells of S.frugiperda probably by disrupting plasma
CC       membranes. Has hemolytic activity against human erythrocytes. Has no
CC       antibacterial activity against E.coli strain ATCC 8739 and S.aureus
CC       strain ATCC 25923. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:22074926}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, peduncles and seeds
CC       (at protein level). {ECO:0000269|PubMed:22074926}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P56879}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:22074926}.
CC   -!- MASS SPECTROMETRY: Mass=3278.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22074926};
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:0000305}.
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DR   AlphaFoldDB; B3EWF1; -.
DR   SMR; B3EWF1; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   CHAIN           1..32
FT                   /note="Parigidin-br1"
FT                   /id="PRO_0000415953"
FT   DISULFID        6..22
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        10..24
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        15..29
FT                   /evidence="ECO:0000250|UniProtKB:P56879,
FT                   ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        1..32
FT                   /note="Cyclopeptide (Gly-Asp)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   32 AA;  3305 MW;  D997DA52E263AA70 CRC64;
     GGSVPCGESC VFIPCITSLA GCSCKNKVCY YD