| First Author | Shadidy M | Year | 1999 |
| Journal | Biochim Biophys Acta | Volume | 1446 |
| Issue | 3 | Pages | 295-307 |
| PubMed ID | 10524204 | Mgi Jnum | J:57457 |
| Mgi Id | MGI:1344831 | Doi | 10.1016/s0167-4781(99)00080-9 |
| Citation | Shadidy M, et al. (1999) Biochemical analysis of mouse FKBP60, a novel member of the FKPB family. Biochim Biophys Acta 1446(3):295-307 |
| abstractText | We have identified mouse and human FKBP60, a new member of the FKBP gene family. FKBP60 shares strongest homology with FKBP65 and SMAP. FKBP60 contains a hydrophobic signal peptide at the N-terminus, 4 peptidyl-prolyl cis/trans isomerase (PPIase) domains and an endoplasmic reticulum retention motif (HDEL) at the C-terminus. Immunodetection of HA-tagged FKBP60 in NIH-3T3 cells suggests that FKBP60 is segregated to the endoplasmic reticulum. Northern blot analysis shows that FKBP60 is predominantly expressed in heart, skeletal muscle, lung, liver and kidney. With N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as a substrate, recombinant GST-FKBP60 is shown to accelerate effectively the isomerization of the peptidyl-prolyl bond. This isomerization activity is inhibited by FK506. mFKBP60 binds Ca2+ in vitro, presumably by its C-terminal EF-hand Ca2+ binding motif, and is phosphorylated in vivo. hFKBP60 has been mapped to 7p12 and/or 7p14 by fluorescence in situ hybridization (FISH). |
