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FK506-binding protein 1A (12 kD FK506-binding protein, immunophilin FKBP12, FKBP1A)
Function:
- may play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the Ca+2 release channel of skeletal muscle sarcoplasmic reticulum
- there are 4 molecules of FKBP12 per skeletal muscle RYR.
- PPIases accelerate the folding of proteins
- catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
- inhibited by both FK506 & rapamycin
peptidylproline (omega=180) peptidylproline (omega=0)
Structure:
- belongs to the FKBP-type PPIase family, FKBP1 subfamily
- contains 1 PPIase FKBP-type domain
Compartment: cytoplasm
Interactions
molecular events
Related
FKBP12-rapamycin complex-associated protein; FK506-binding protein 12-rapamycin complex-associated protein 1; rapamycin target protein; RAPT1; mammalian target of rapamycin; mTOR (FRAP1, FRAP, FRAP2)
General
FK506 binding protein (FKBP)
Properties
SIZE: MW = 12 kD
entity length = 107 aa
COMPARTMENT: cytoplasm
MOTIF: active site
binding site
FOR-BINDING-OF: sirolimus
Database Correlations
OMIM 186945
UniProt P62942
Pfam PF00254
ENZYME 5.2.1.8
References
- Martinus RD et al
Role of chaperones in the biogenesis and maintenance of the
mitochondrion.
FASEB J. 1995 Mar;9(5):371-8. Review.
PMID: 7896006
- UniProt :accession P62942