O35465 · FKBP8_MOUSE
- ProteinPeptidyl-prolyl cis-trans isomerase FKBP8
- GeneFkbp8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids402 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity).
Required for normal embryonic development
Required for normal embryonic development
Miscellaneous
Binds the immunosuppressant FK506 only in its calmodulin/calcium activated form.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Cofactor
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase FKBP8
- EC number
- Short namesPPIase FKBP8
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO35465
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 380-400 | Helical | ||||
Sequence: WLFGATAVALGGVALSVVIAA |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice die shortly after birth. They display neural tube and skeletal defects. The neuroepithelium is disorganized and the formation of dorsal root ganglia is defective, likely as a result of an increased frequency of apoptosis and aberrant migration of neuronal cells. The extension of nerve fibers in the spinal cord is also abnormal.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000075332 | 1-402 | Peptidyl-prolyl cis-trans isomerase FKBP8 | |||
Sequence: MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN | ||||||
Cross-link | 239 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 261 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 263 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 274 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 286 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 297 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 304 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 324 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 330 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 338 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 341 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 342 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected throughout the embryonic body, in caudal neural tube, limbs and head. Detected in adult retina, brain, heart, kidney, liver, pancreas, lung, testis and urinary bladder (at protein level). Detected in adult brain, kidney, liver, testis and trigeminal nerve, and in embryo. Detected at lower levels in lung, spleen, heart and ovary. Widely expressed in forebrain. Detected in the Purkinje cell layer in the cerebellum and in hippocampus neurons.
Gene expression databases
Interaction
Subunit
Homomultimers or heteromultimers (Potential). Forms heterodimer with calmodulin. When activated by calmodulin and calcium, interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin (By similarity).
Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By similarity).
Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-42 | Acidic residues | ||||
Sequence: DGVDDAEEEDDLSGL | ||||||
Region | 28-54 | Disordered | ||||
Sequence: DGVDDAEEEDDLSGLPPLEDMGQPTVE | ||||||
Domain | 110-194 | PPIase FKBP-type | ||||
Sequence: GQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAE | ||||||
Repeat | 211-244 | TPR 1 | ||||
Sequence: ANRKRECGNAHYQRADFVLAANSYDLAIKAITSN | ||||||
Repeat | 262-295 | TPR 2 | ||||
Sequence: VKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDN | ||||||
Repeat | 296-329 | TPR 3 | ||||
Sequence: IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O35465-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length402
- Mass (Da)43,529
- Last updated2008-07-01 v2
- Checksum609A954FAD3A76F8
O35465-2
- Name2
- Differences from canonical
- 173-173: G → GS
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-42 | Acidic residues | ||||
Sequence: DGVDDAEEEDDLSGL | ||||||
Sequence conflict | 100 | in Ref. 1; AAO39021, 2; AAQ84562, 4; AAH03739 and 5; AAB86422 | ||||
Sequence: G → C | ||||||
Sequence conflict | 163 | in Ref. 3; BAE26916 | ||||
Sequence: A → T | ||||||
Sequence conflict | 170 | in Ref. 3; BAC40541 | ||||
Sequence: G → A | ||||||
Alternative sequence | VSP_034487 | 173 | in isoform 2 | |||
Sequence: G → GS | ||||||
Sequence conflict | 400 | in Ref. 1; AAO39021, 2; AAQ84562, 4; AAH03739 and 5; AAB86422 | ||||
Sequence: A → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY225340 EMBL· GenBank· DDBJ | AAO39021.1 EMBL· GenBank· DDBJ | mRNA | ||
AY278608 EMBL· GenBank· DDBJ | AAQ84562.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088739 EMBL· GenBank· DDBJ | BAC40541.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK146122 EMBL· GenBank· DDBJ | BAE26916.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK152198 EMBL· GenBank· DDBJ | BAE31027.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK165281 EMBL· GenBank· DDBJ | BAE38118.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK167663 EMBL· GenBank· DDBJ | BAE39713.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC003739 EMBL· GenBank· DDBJ | AAH03739.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC027808 EMBL· GenBank· DDBJ | AAH27808.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF030635 EMBL· GenBank· DDBJ | AAB86422.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY187231 EMBL· GenBank· DDBJ | AAO27795.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |