Peptidyl-prolyl cis-trans isomerase FKBP1C (FKBP1C)

Peptidyl-prolyl cis-trans isomerase FKBP1C (FKBP1C) is a member of the FKBP (FK506 binding protein) family of immunophilins, functioning as a peptidyl-prolyl cis-trans isomerase (PPIase) that catalyzes the cis-trans isomerization of proline bonds in oligopeptides[4][5]. This activity assists proper protein folding and may be involved in chaperone-mediated biological processes. FKBP1C shares overall mechanistic similarities with other FKBPs but, unlike some family members (such as FKBP1A/FKBP12), there is no evidence it binds immunosuppressive drugs or is targeted therapeutically. Functional predictions suggest involvement in regulation of signaling pathways (such as the activin receptor pathway), but disease associations and pharmacological targeting remain uncharacterized as of now[5][6]. There are also published references to an "lncRNA-FKBP1C" (in chickens) that regulates muscle development, but this is not a protein-coding gene and is distinct from the human protein FKBP1C[1].

Other names

FKBP prolyl isomerase family member 1CFKBP1CFK506 binding protein 1CbA184C23.2peptidyl-prolyl cis-trans isomerase FKBP1CFKBP prolyl isomerase 1C

Not established for drugs targeting this molecule specifically. For the FKBP family, drug mechanisms (when present) often involve immunosuppression via calcineurin inhibition, but this has not been demonstrated for FKBP1C[2][3][4].