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Gene Review

FPR2  -  peptidylprolyl isomerase family protein FPR2

Saccharomyces cerevisiae S288c

Synonyms: D9719.24, FK506-binding protein 2, FKB2, FKBP proline rotamase 2, FKBP-13, ...
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Disease relevance of FPR2

  • When expressed in and purified from Escherichia coli, both full-length Fpr3 and its isolated COOH-terminal domain exhibit readily detectable PPIase activity [1].

High impact information on FPR2

  • In S. cerevisiae, the gene for a 112-residue cytosolic FKBP (FPR1) and the gene for a 135-residue ER-associated FKBP (FPR2) have been described before [1].
  • The core region of VfFKBP15 is most similar to yeast and mammalian FKBP13 localized in the endoplasmic reticulum (ER) [2].
  • As with KAR2, FKB2 mRNA levels are also elevated by heat shock [3].
  • The similarities in the regulation of FKB2 and other ER chaperone genes suggest that FKBP-13 may play a role in protein trafficking in the ER [3].
  • FKB2 mRNA levels are elevated in cells blocked in N-glycosylation--i.e., in wild-type cells treated with tunicamycin and in the sec53-6 mutant grown at the nonpermissive temperature [3].

Biological context of FPR2

  • FKB2 is located on the right arm of chromosome IV and contains an open reading frame of 135 amino acids, of which the first 17 residues comprise a putative hydrophobic leader peptide [4].
  • FKB2 encodes a homolog of human FKBP-13, a membrane-associated binding protein for the immunosuppressants FK506 and rapamycin [4].
  • Recombinant Cyp40 produced in bacteria has a peptidyl-prolyl cis-trans isomerase activity with a catalytic efficiency (k[cat]/K[m]) of 0.5 x 10(6)M(-1)s(-1), which can be inhibited by cyclosporin A with an IC50 value of 60nM [5].

Anatomical context of FPR2


Associations of FPR2 with chemical compounds

  • This protein, a peptidyl-prolyl cis-trans isomerase, is the yeast homologue of the protein that mediates the immunosuppressant effects of the drug cyclosporin A (CsA) [6].
  • Furthermore, deletion of the entire PPIase domain did not significantly affect growth or Hsp90-mediated steroid receptor activity [7].
  • The whole process of reactivation is catalysed by peptidyl prolyl cis-trans isomerase and thus suggests that one or more proline residues stereochemically control the rate limiting step of reactivation [8].

Other interactions of FPR2


  1. A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus. Benton, B.M., Zang, J.H., Thorner, J. J. Cell Biol. (1994) [Pubmed]
  2. Molecular characterization of a FKBP-type immunophilin from higher plants. Luan, S., Kudla, J., Gruissem, W., Schreiber, S.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. The FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulum. Partaledis, J.A., Berlin, V. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Saccharomyces cerevisiae contains a homolog of human FKBP-13, a membrane-associated FK506/rapamycin binding protein. Partaledis, J.A., Fleming, M.A., Harding, M.W., Berlin, V. Yeast (1992) [Pubmed]
  5. Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Warth, R., Briand, P.A., Picard, D. Biol. Chem. (1997) [Pubmed]
  6. Specific cross-linking of the proline isomerase cyclophilin to a non-proline-containing peptide. McNew, J.A., Sykes, K., Goodman, J.M. Mol. Biol. Cell (1993) [Pubmed]
  7. The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. Duina, A.A., Marsh, J.A., Kurtz, R.B., Chang, H.C., Lindquist, S., Gaber, R.F. J. Biol. Chem. (1998) [Pubmed]
  8. Multiple unfolded states of UDP-galactose 4-epimerase from yeast Kluyveromyces fragilis. Involvement of proline cis-trans isomerization in reactivation. Dutta, S., Maity, N.R., Bhattacharyya, D. Biochim. Biophys. Acta (1997) [Pubmed]
  9. Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae. Kern, G., Kern, D., Jaenicke, R., Seckler, R. Protein Sci. (1993) [Pubmed]
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