Detail Information for IndEnz0002013453
IED ID IndEnz0002013453
Enzyme Type ID protease013453
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L1
UCH-L1
EC 3.4.19.12
Neuron cytoplasmic protein 9.5
PGP 9.5
PGP9.5
Ubiquitin thioesterase L1
Gene Name Uchl1
Organism Rattus norvegicus (Rat)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MQLKPMEINPEMLNKVLAKLGVAGQWRFADVLGLEEETLGSVPSPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLEFEDGSVLKQFLSETEKLSPEDRAKCFEKNEAIQAAHDSVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAAKVCREFTEREQGEVRFSAVALCKAA
Enzyme Length 223
Uniprot Accession Number Q00981
Absorption
Active Site ACT_SITE 90; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10091; ACT_SITE 161; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10091
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:P09936};
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (By similarity). This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin (By similarity). Also binds to free monoubiquitin and may prevent its degradation in lysosomes (By similarity). The homodimer may have ATP-independent ubiquitin ligase activity (By similarity). {ECO:0000250|UniProtKB:P09936, ECO:0000250|UniProtKB:Q9R0P9}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Lipidation (1); Modified residue (1); Propeptide (1); Region (2); Sequence conflict (3); Site (1)
Keywords Cytoplasm;Direct protein sequencing;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Phosphoprotein;Prenylation;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Modified Residue MOD_RES 125; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903
Post Translational Modification PTM: O-glycosylated. {ECO:0000269|PubMed:11739622}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11850463; 17011532; 17599367; 17690318; 18616865; 18836575; 19267071; 20231490; 20387083; 20933087; 21069350; 23599427; 24090154; 24687852; 25326379; 25638021; 25763798; 29964011; 30305579; 30551363; 31041655; 34130526;
Motif
Gene Encoded By
Mass 24,838
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.19.12;