Q3B7U9
SS
Gene name |
Fkbp8 |
Protein name |
Peptidyl-prolyl cis-trans isomerase FKBP8 |
Names |
PPIase FKBP8, FK506-binding protein 8, FKBP-8, Rotamase |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:290652 |
EC number |
5.2.1.8: Cis-trans isomerases |
Protein Class |
|
Descriptions
FK506 binding protein 38 (FKBP38) is a multi-domain protein containing PPlase domain followed by TPR, CaM-binding domain and transmembrane domain. FKBP38 regulates apoptosis through unique interactions with multiple regulators including Bcl-2. the N-terminal extension (residues 1-32) preceding the catalytic domain of FKBP38 has an autoinhibitory activity. The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain.
Autoinhibitory domains (AIDs)
Target domain |
106-195 (Peptidyl-prolyl cis-trans isomerase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q3B7U9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3B7U9-F1 | Predicted | AlphaFoldDB |
No variants for Q3B7U9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3B7U9 | |||||
No associated diseases with Q3B7U9
4 regional properties for Q3B7U9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FKBP-type peptidyl-prolyl cis-trans isomerase domain | 106 - 195 | IPR001179 |
| repeat | Tetratricopeptide repeat | 212 - 245 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 263 - 296 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 297 - 330 | IPR019734-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| mitochondrial envelope | The double lipid bilayer enclosing the mitochondrion and separating its contents from the cell cytoplasm; includes the intermembrane space. |
| mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| disordered domain specific binding | Binding to a disordered domain of a protein. |
| identical protein binding | Binding to an identical protein or proteins. |
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
14 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| camera-type eye development | The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field. |
| cell fate specification | The process involved in the specification of cell identity. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. |
| dorsal/ventral neural tube patterning | The process in which the neural tube is regionalized in the dorsoventral axis. |
| dorsal/ventral pattern formation | The regionalization process in which the areas along the dorsal/ventral axis are established that will lead to differences in cell differentiation. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism. |
| multicellular organism growth | The increase in size or mass of an entire multicellular organism, as opposed to cell growth. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| negative regulation of protein phosphorylation | Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein. |
| neural tube development | The process whose specific outcome is the progression of the neural tube over time, from its formation to the mature structure. The mature structure of the neural tube exists when the tube has been segmented into the forebrain, midbrain, hindbrain and spinal cord regions. In addition neural crest has budded away from the epithelium. |
| positive regulation of BMP signaling pathway | Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| regulation of BMP signaling pathway | Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway. |
| regulation of gene expression | Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
| smoothened signaling pathway | The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A6QQ71 | FKBP6 | Inactive peptidyl-prolyl cis-trans isomerase FKBP6 | Bos taurus (Bovine) | PR |
| Q9W1I9 | shu | Inactive peptidyl-prolyl cis-trans isomerase shutdown | Drosophila melanogaster (Fruit fly) | PR |
| Q02790 | FKBP4 | Peptidyl-prolyl cis-trans isomerase FKBP4 | Homo sapiens (Human) | PR |
| Q14318 | FKBP8 | Peptidyl-prolyl cis-trans isomerase FKBP8 | Homo sapiens (Human) | EV |
| O35465 | Fkbp8 | Peptidyl-prolyl cis-trans isomerase FKBP8 | Mus musculus (Mouse) | SS |
| Q7DMA9 | PAS1 | Peptidyl-prolyl cis-trans isomerase PASTICCINO1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASWAEPSEP | AAQLLCGAPL | LEGFEVLDGV | DDAEEEDDLS | GLPPLEDMGQ | PTVEEAEQPG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALAREFLAAT | EPEPAPAPAP | EEWLDILGNG | LLRKKTLVPG | PTGSSRPLKG | QVVTVHLQMS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LENGTRVQEE | PELAFTLGDC | DVIQALDLSV | PLMHVGETAM | VTADSKYCYG | PQGSRSPYIP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PHAALCLEVT | LKTAEDGPDL | EMLSGQERVA | LANRKRECGN | AHYQRADFVL | AANSYDLAIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AITSNAKVDM | TCEEEEELLQ | LKVKCLNNLA | ASQLKLDHYR | AALRSCSQVL | EHQPDNIKAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FRKGKVLAQQ | GEYSEAIPIL | RAALKLEPSN | KTIHAELSKL | VKKRAAQRST | ETALYRKMLG |
| 370 | 380 | 390 | 400 | ||
| NPSRLPAKCP | GKGAWSIPWK | WLFGATAVAL | GGVALSVVIA | ARN |