FKBP7
FKBP7 (FKBP prolyl isomerase 7, also known as FKBP23 and FK506-binding protein 7) is a peptidyl-prolyl cis-trans isomerase of the FKBP family. It accelerates protein folding during synthesis and acts as a molecular chaperone in the endoplasmic reticulum lumen. Browse Assay Genie's current range of FKBP7 research reagents below, or read on for the biology behind the target.
FKBP7 is a peptidyl-prolyl cis-trans isomerase (PPIase), an enzyme class that accelerates the folding of proteins during protein synthesis. The isomerase reaction, assigned EC 5.2.1.8, interconverts the cis and trans forms of peptide bonds preceding proline residues, a step that can limit the rate at which a nascent polypeptide reaches its native fold. According to the NCBI Gene summary, members of this family show PPIase activity and also function as molecular chaperones.
The FKBP7 gene encodes a protein that belongs to the FKBP-type PPIase family. UniProt records its subcellular location as the endoplasmic reticulum lumen, where newly synthesised secretory and membrane proteins are folded. The NCBI Gene summary notes that a similar protein in mouse, encoded by Fkbp7, is located in the endoplasmic reticulum and binds calcium. HGNC places the gene in two groups: the EF-hand domain containing group, a family of calcium-binding motifs, and the FKBP prolyl isomerase family.
The protein is known by the alias FKBP23, and earlier names include FK506-binding protein 7. These names refer to the FKBP family's namesake property of binding the immunosuppressant FK506. Researchers studying FKBP7 are typically interested in endoplasmic reticulum protein folding, chaperone function and calcium-linked regulation of folding enzymes, and in how it compares with other FKBP proteins.
FKBP7 is a PPIase that accelerates protein folding during synthesis, making it a subject for studies of proline isomerisation in the secretory pathway.
Located in the endoplasmic reticulum lumen, FKBP7 is relevant to work on luminal chaperones and the folding environment of this compartment.
FKBP family members combine PPIase activity with molecular chaperone function, and FKBP7 offers a model for how these roles are coupled.
The mouse counterpart binds calcium and the human gene is in the EF-hand domain group, linking FKBP7 to calcium-dependent regulation in the endoplasmic reticulum.
FKBP7 is a peptidyl-prolyl cis-trans isomerase that accelerates the folding of proteins during protein synthesis. Like other members of the FKBP-type PPIase family, it also functions as a molecular chaperone. UniProt places it in the lumen of the endoplasmic reticulum.
The HGNC name is FKBP prolyl isomerase 7. The protein is also called FKBP23, and earlier names are FK506-binding protein 7 and FK506 binding protein 7. UniProt lists it as peptidyl-prolyl cis-trans isomerase FKBP7.
A mouse ortholog, Fkbp7, exists. The NCBI Gene summary reports that a similar mouse protein is located in the endoplasmic reticulum and binds calcium. Check the datasheet of any product for its validated reactivity.
Other FKBP prolyl isomerase family members and related chaperone targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y680; product specifications from Assay Genie datasheets.