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InterPro: IPR001179 Peptidyl-prolyl cis-trans isomerase, FKBP-type

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6838 proteins

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Architectures
Accession List
Matches in BioMart

Accession

IPR001179 PPIase_FKBP

Secondary

IPR015478

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00254	FKBP_C	6574
PROSITE profile	PS50059	FKBP_PPIASE	6360
PANTHER	PTHR10516	PPIase_FKBP	5333
Signatures in BioMart

InterPro Relationships Help

Children

IPR019869 Gliding motility-associated, peptidyl-prolyl isomerase, GldI

Found in

IPR005215 Trigger factor

GO Term annotation Help

Process

GO:0006457 protein folding

InterPro annotation

Entry Details in BioMart

Abstract

Synonym(s): Peptidylprolyl cis-trans isomerase

FKBP-type peptidylprolyl isomerases (EC:5.2.1.8) in vertebrates, are receptors for the two immunosuppressants, FK506 and rapamycin. The drugs inhibit T cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. Peptidylprolyl isomerases accelerate protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides. These proteins are found in a variety of organisms.

Structural links Help

PDB - click here

SCOP: a.118.8.1 , d.26.1.1

CATH: 1.25.40.10 , 3.10.50.40

Database links Help

PROSITE doc: PDOC00426

PANDIT: PF00254

Blocks: IPB001179

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001179

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O08915 AH receptor-interacting protein

O75344 FK506-binding protein 6

P20081 FK506-binding protein 1

P48375 12 kDa FK506-binding protein

Q9LDC0 42 kDa peptidyl-prolyl isomerase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001179	Peptidyl-prolyl cis-trans isomerase, FKBP-type
IPR011990	Tetratricopeptide-like helical
IPR013026	Tetratricopeptide repeat-containing
IPR019734	Tetratricopeptide repeat
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	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 1992 3410-20 [PubMed: 1464374] http://www.fasebj.org/cgi/content/abstract/6/15/3410
	Saul FA, Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335 2004 595-608 [PubMed: 14672666] http://dx.doi.org/10.1016/j.jmb.2003.10.056
	Gopalan G, He Z, Balmer Y, Romano P, Gupta R, Heroux A, Buchanan BB, Swaminathan K, Luan S. Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Proc. Natl. Acad. Sci. U.S.A. 101 2004 13945-50 [PubMed: 15356344] http://dx.doi.org/10.1073/pnas.0405240101
	Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z. 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex. Proc. Natl. Acad. Sci. U.S.A. 101 2004 8348-53 [PubMed: 15159550] http://dx.doi.org/10.1073/pnas.0305969101
	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 1990 2205-12 [PubMed: 2186809] http://dx.doi.org/10.1021/bi00461a001
	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
	Siekierka JJ, Wiederrecht G, Greulich H, Boulton D, Hung SH, Cryan J, Hodges PJ, Sigal NH. The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. J. Biol. Chem. 265 1990 21011-5 [PubMed: 1701173] http://intl.jbc.org/cgi/content/abstract/265/34/21011
	Stein RL. Exploring the catalytic activity of immunophilins. Curr. Biol. 1 1991 234-6 [PubMed: 15336129] http://dx.doi.org/10.1016/0960-9822(91)90067-7
	Tropschug M, Wachter E, Mayer S, Schonbrunner ER, Schmid FX. Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Nature 346 1990 674-7 [PubMed: 1696687] http://dx.doi.org/10.1038/346674a0
	Ludlam AV, Moore BA, Xu Z. The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae. Proc. Natl. Acad. Sci. U.S.A. 101 2004 13436-41 [PubMed: 15353602] http://dx.doi.org/10.1073/pnas.0405868101
	Galat A. Peptidylproline cis-trans-isomerases: immunophilins. Eur. J. Biochem. 216 1993 689-707 [PubMed: 8404888] http://dx.doi.org/10.1111/j.1432-1033.1993.tb18189.x
	Hacker J, Fischer G. Immunophilins: structure-function relationship and possible role in microbial pathogenicity. Mol. Microbiol. 10 1993 445-56 [PubMed: 7526121] http://dx.doi.org/10.1111/j.1365-2958.1993.tb00917.x

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