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InterPro: IPR002130 Peptidyl-prolyl cis-trans isomerase, cyclophilin-type
Protein matches
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UniProtKB Matches: 5698 proteins |
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Accession
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IPR002130 PPIase_cyclophilin |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Parent
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IPR015891 Cyclophilin-like
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Found in
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IPR016304 Peptidyl-prolyl cis-trans isomerase E
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Contains
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IPR020892 Peptidyl-prolyl cis-trans isomerase, cyclophilin-type, conserved site
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GO Term annotation
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Process
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GO:0006457 protein folding
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Function
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GO:0003755 peptidyl-prolyl cis-trans isomerase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Cyclophilin [1] is the major high-affinity binding protein in vertebrates for the immunosuppressive drug cyclosporin A (CSA), but is also found in other organisms. It exhibits a peptidyl-prolyl cis-trans isomerase activity (EC:5.2.1.8) (PPIase or rotamase). PPIase is an enzyme that accelerates protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [2]. It is probable that CSA mediates some of its effects via an forming a tight complex with cyclophilin that inhibits the phosphatase activity of calcineurin [3], [4]. Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B and C, and natural killer cell cyclophilin-related protein [5, 6, 7]. Major isoforms have been found throughout the cell, including the ER, and some are even secreted. The sequences of the different forms of cyclophilin-type PPIases are well conserved.
Note: FKBP's, a family of proteins that bind the immunosuppressive drug FK506, are also PPIases, but their sequence is not at all related to that of cyclophilin (see IPR001179).
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Structural links
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Database links
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Publications
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1.
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Stamnes MA, Rutherford SL, Zuker CS.
Cyclophilins: a new family of proteins involved in intracellular folding.
Trends Cell Biol. 2 272-6 1992
[PubMed: 14731520]
http://dx.doi.org/10.1016/0962-8924(92)90200-7
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2.
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Fischer G, Schmid FX.
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.
Biochemistry 29 2205-12 1990
[PubMed: 2186809]
http://dx.doi.org/10.1021/bi00461a001
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3.
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Husi H, Luyten MA, Zurini MG.
Mapping of the immunophilin-immunosuppressant site of interaction on calcineurin.
J. Biol. Chem. 269 14199-204 1994
[PubMed: 7514602]
http://intl.jbc.org/cgi/reprint/269/19/14199.pdf
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4.
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Etzkorn FA, Chang ZY, Stolz LA, Walsh CT.
Cyclophilin residues that affect noncompetitive inhibition of the protein serine phosphatase activity of calcineurin by the cyclophilin.cyclosporin A complex.
Biochemistry 33 2380-8 1994
[PubMed: 8117697]
http://dx.doi.org/10.1021/bi00175a005
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5.
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Trandinh CC, Pao GM, Saier MH Jr.
Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases.
FASEB J. 6 3410-20 1992
[PubMed: 1464374]
http://www.fasebj.org/cgi/content/abstract/6/15/3410
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6.
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Galat A.
Peptidylproline cis-trans-isomerases: immunophilins.
Eur. J. Biochem. 216 689-707 1993
[PubMed: 8404888]
http://dx.doi.org/10.1111/j.1432-1033.1993.tb18189.x
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7.
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Hacker J, Fischer G.
Immunophilins: structure-function relationship and possible role in microbial pathogenicity.
Mol. Microbiol. 10 445-56 1993
[PubMed: 7526121]
http://dx.doi.org/10.1111/j.1365-2958.1993.tb00917.x
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Additional Reading
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Wear MA, Kan D, Rabu A, Walkinshaw MD.
Experimental determination of van der waals energies in a biological system.
Angew. Chem. Int. Ed. Engl. 46 2007 6453-6
[PubMed: 17654646]
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Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E.
Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region.
J. Biol. Chem. 270 1995 14209-13
[PubMed: 7775481]
http://dx.doi.org/10.1074/jbc.270.23.14209
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Wang P, Heitman J.
The cyclophilins.
Genome Biol. 6 2005 226
[PubMed: 15998457]
http://dx.doi.org/10.1186/gb-2005-6-7-226
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Kajitani K, Fujihashi M, Kobayashi Y, Shimizu S, Tsujimoto Y, Miki K.
Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 0.96-A resolution.
Proteins 70 2008 1635-9
[PubMed: 18076075]
http://dx.doi.org/10.1002/prot.21855
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Davis TL, Walker JR, Ouyang H, MacKenzie F, Butler-Cole C, Newman EM, Eisenmesser EZ, Dhe-Paganon S.
The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1).
FEBS J. 275 2008 2283-95
[PubMed: 18397323]
http://dx.doi.org/10.1111/j.1742-4658.2008.06381.x
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Xu C, Zhang J, Huang X, Sun J, Xu Y, Tang Y, Wu J, Shi Y, Huang Q, Zhang Q.
Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP.
J. Biol. Chem. 281 2006 15900-8
[PubMed: 16595688]
http://dx.doi.org/10.1074/jbc.M511155200
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Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol. Biochem. Parasitol. 151 2007 100-10
[PubMed: 17125854]
http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
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