Detail Information for IndEnz0002004618
IED ID IndEnz0002004618
Enzyme Type ID protease004618
Protein Name CAAX prenyl protease 2
EC 3.4.-.-
Farnesylated proteins-converting enzyme 2
FACE-2
Prenyl protein-specific endoprotease 2
RCE1 homolog
Gene Name RCE1
Organism Bos taurus (Bovine)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MAALGGDGFRLLSVSRPERQPESAALGGPGPGLCCWVSVFSCLSLACSYVGSLYVWKSELPRDHPAVIKRRFTSVLVVSSLSPLCVLLWRELTGIQPGTSLLTLMGFRLEGIFPAALLPLLLTMILFLGPLMQLSMDCPCDLADGLKVVLAPRSWARCLTDMRWLRNQVIAPLTEELVFRACMLPMLAPCTGLGPAVFTCPLFFGVAHFHHIFEQLRFRQSSVGSIFLSAGHLIGPVLCHSFCNYMGFPAVCAALEHPQRRPLLAGYALGVGLFLLLLQPLTDPKLYGSLPLCVLLERAGDSEAPLCS
Enzyme Length 308
Uniprot Accession Number A6H7A0
Absorption
Active Site ACT_SITE 175; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q6LZY8; ACT_SITE 208; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q6LZY8
Activity Regulation ACTIVITY REGULATION: Deubiquitination by USP17L2/USP17 negatively regulates the proteolytic activity toward Ras GTPases. {ECO:0000250|UniProtKB:Q9Y256}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (By similarity). {ECO:0000250|UniProtKB:Q9Y256}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Initiator methionine (1); Modified residue (1); Site (2); Transmembrane (6)
Keywords Acetylation;Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y256}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q9Y256
Post Translational Modification PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. 'Lys-48' ubiquitination induces its degradation. Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q9Y256}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,455
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda