Peptidyl-prolyl cis-trans isomerase FKBP14 (FKBP14)

Peptidyl-prolyl cis-trans isomerase FKBP14 (FKBP14) is an enzyme localized to the endoplasmic reticulum, classified as a member of the FK506-binding protein family with peptidyl-prolyl cis-trans isomerase (PPIase) activity[1][4][3]. It assists protein folding by catalyzing the cis-trans isomerization of proline residues, with a particular role in folding procollagen, crucial for proper collagen biosynthesis and organization of the extracellular matrix[1][2][5]. The protein contains EF-hand motifs and forms a dimer, contributing to the processing of multiple collagen types, especially those with 4-hydroxyproline modifications[3][5]. Genetic mutations resulting in FKBP14 deficiency cause the kyphoscoliotic type of Ehlers-Danlos syndrome, marked by joint hypermobility, kyphoscoliosis, vascular fragility, muscle atrophy, and congenital hearing loss[1][2]. Increased FKBP14 expression is observed in some cancers, such as ovarian carcinoma, where it may support cell proliferation[2]. FKBP14 can bind immunosuppressive drugs like tacrolimus, which inhibit its isomerase activity[3].

Other names

FKBP prolyl isomerase 1422 kDa FK506-binding proteinFK506 binding protein 14FKBP22FKBP-22FKBP-14FLJ20731EDSKMHEDSKSCL2IPBP12PPIase FKBP14rotamase

Inhibition of peptidyl-prolyl cis-trans isomerase activity (for FK506/tacrolimus)