ID   PALIC_PALCO             Reviewed;          37 AA.
AC   P84645;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Palicourein;
OS   Palicourea condensata (Cappel).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Palicoureeae;
OC   Palicourea.
OX   NCBI_TaxID=272141;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Bark {ECO:0000269|PubMed:11430013};
RX   PubMed=11430013; DOI=10.1021/np000372l;
RA   Bokesch H.R., Pannell L.K., Cochran P.K., Sowder R.C. II, McKee T.C.,
RA   Boyd M.R.;
RT   "A novel anti-HIV macrocyclic peptide from Palicourea condensata.";
RL   J. Nat. Prod. 64:249-250(2001).
RN   [2] {ECO:0000305}
RP   STRUCTURE BY NMR.
RX   PubMed=14725768; DOI=10.1016/j.str.2003.11.019;
RA   Barry D.G., Daly N.L., Bokesch H.R., Gustafson K.R., Craik D.J.;
RT   "Solution structure of the cyclotide palicourein: implications for the
RT   development of a pharmaceutical framework.";
RL   Structure 12:85-94(2004).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Inhibits
CC       the cytopathic effects of the human immunodeficiency virus.
CC       {ECO:0000269|PubMed:11430013, ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:14725768}.
CC   -!- PTM: This is a cyclic peptide. {ECO:0000269|PubMed:11430013,
CC       ECO:0000269|PubMed:14725768}.
CC   -!- SIMILARITY: Belongs to the cyclotide family. {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:0000305}.
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DR   PDB; 1R1F; NMR; -; A=4-37.
DR   PDBsum; 1R1F; -.
DR   AlphaFoldDB; P84645; -.
DR   SMR; P84645; -.
DR   EvolutionaryTrace; P84645; -.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
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..37
FT                   /note="Palicourein"
FT                   /evidence="ECO:0000269|PubMed:11430013"
FT                   /id="PRO_0000044701"
FT   DISULFID        6..24
FT                   /evidence="ECO:0000269|PubMed:14725768"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000269|PubMed:14725768"
FT   DISULFID        16..34
FT                   /evidence="ECO:0000269|PubMed:14725768"
FT   CROSSLNK        1..37
FT                   /note="Cyclopeptide (Gly-Asn)"
FT                   /evidence="ECO:0000269|PubMed:11430013,
FT                   ECO:0000269|PubMed:14725768"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1R1F"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:1R1F"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1R1F"
SQ   SEQUENCE   37 AA;  3928 MW;  F2E47EA83BDA960D CRC64;
     GDPTFCGETC RVIPVCTYSA ALGCTCDDRS DGLCKRN