Q9D0W5 · PPIL1_MOUSE
- ProteinPeptidyl-prolyl cis-trans isomerase-like 1
- GenePpil1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids166 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in pre-mRNA splicing as component of the spliceosome (PubMed:33220177).
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (By similarity).
Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed:33220177).
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (By similarity).
Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed:33220177).
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Inhibited by Cyclosporin A.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 54-65 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: HRIIKDFMIQGG | ||||||
Binding site | 70-71 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 99-104 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: AMANAG | ||||||
Binding site | 109-113 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: GSQFF | ||||||
Binding site | 119 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 125 | cyclosporin A (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | catalytic step 2 spliceosome | |
Cellular Component | nucleus | |
Cellular Component | U2-type catalytic step 2 spliceosome | |
Molecular Function | cyclosporin A binding | |
Molecular Function | disordered domain specific binding | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | embryonic brain development | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | protein folding | |
Biological Process | protein peptidyl-prolyl isomerization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase-like 1
- EC number
- Short namesPPIase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D0W5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mutant mice, in which PPIL1 is truncated at position 102, die before 12.5 dpc.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 55 | Loss of isomerase activity. No phenotype when introduced in mice, animals are viable and fertile with no microcephaly or defective cortical lamination; no splicing defect. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064165 | 1-166 | Peptidyl-prolyl cis-trans isomerase-like 1 | |||
Sequence: MAAIPPDTWQPPNVYLETSMGVIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKILKAYPSG | ||||||
Modified residue | 149 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Widely expressed in the developing cortex at 14.5 dpc.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-164 | PPIase cyclophilin-type | ||||
Sequence: QPPNVYLETSMGVIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKILKAYP |
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length166
- Mass (Da)18,237
- Last updated2001-06-01 v1
- ChecksumA5C5B04FE29C52C9
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6SSV9 | F6SSV9_MOUSE | Ppil1 | 64 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK004331 EMBL· GenBank· DDBJ | BAB23265.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150643 EMBL· GenBank· DDBJ | BAE29731.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151572 EMBL· GenBank· DDBJ | BAE30513.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058369 EMBL· GenBank· DDBJ | AAH58369.1 EMBL· GenBank· DDBJ | mRNA |