A0A087RGC0 · A0A087RGC0_APTFO
- ProteinCAAX prenyl protease
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids427 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | CAAX-box protein processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCAAX prenyl protease
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Aequornithes > Sphenisciformes > Spheniscidae > Aptenodytes
Accessions
- Primary accessionA0A087RGC0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 80-104 | Helical | ||||
Sequence: IVQSLVFLLLATLFSAVTGLPWSLY | ||||||
Transmembrane | 131-149 | Helical | ||||
Sequence: FIVTQCILLPVTSLLLYII | ||||||
Transmembrane | 155-176 | Helical | ||||
Sequence: YFFIYAWLFTLVVSLVLVTIYA | ||||||
Transmembrane | 309-331 | Helical | ||||
Sequence: FLCFFLFAVLIGRKELFAAFGFY | ||||||
Transmembrane | 337-362 | Helical | ||||
Sequence: LIGLMIIFQFIFSPYNEVLSFCLTVL |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-185 | CAAX prenyl protease 1 N-terminal | ||||
Sequence: QRRVYRTTTHVPRELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSEVEGTMILLCGGIPFLWNLSGQISGRAGFGPEYEIVQSLVFLLLATLFSAVTGLPWSLYNTFVIEEKHGFNQQTLGFFFKDAIKKFIVTQCILLPVTSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDK | ||||||
Domain | 188-423 | Peptidase M48 | ||||
Sequence: PLPEGELKQQIETMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEDYSALNKEPAEGEDGENEETKSKTKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDTQPTLIGLMIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKELGKAKDLYSALIKLNKDNLGFPVSDWIFSMWHYSHPPLLERLQALKD | ||||||
Region | 253-273 | Disordered | ||||
Sequence: EPAEGEDGENEETKSKTKNKK |
Sequence similarities
Belongs to the peptidase M48A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length427
- Mass (Da)48,961
- Last updated2014-10-29 v1
- Checksum7170162821E9445C
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: Q | ||||||
Non-terminal residue | 427 | |||||
Sequence: E |
Keywords
- Technical term