| IED ID | IndEnz0002001673 |
| Enzyme Type ID | protease001673 |
| Protein Name |
Sentrin-specific protease 3 EC 3.4.22.- SUMO-1-specific protease 3 Sentrin/SUMO-specific protease SENP3 Smt3-specific isopeptidase 1 Smt3ip1 |
| Gene Name | Senp3 Smt3ip Smt3ip1 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MKETIQGTGSWGPEPPGPGTTYSNPRRERLRWPLPPKPRLKSGGGFGPDPGSGTTVPTRRLPAPRPSFDASASEEEEEEEEEDEEEVAAWRLPPRWGQLGASQRSRALRPSHRKTCSQRRRRAMRAFQMLLYSKSTSLTFHWKLWGRHRGRRRNLAHPKNHLSPQEGGATPQVPSPCCRFDSPRGLPPPRLGLLGALMAEDGMRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGLSGPEGERSLAPPDASILISNVCSIGDHVAQELFQSSDLGIAEEADRTGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKSLVLQLIQSYQRMPGNAMVRGFRVSYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV |
| Enzyme Length | 568 |
| Uniprot Accession Number | Q9EP97 |
| Absorption | |
| Active Site | ACT_SITE 459; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 476; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 526; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q9HC62 |
| Activity Regulation | ACTIVITY REGULATION: On oxidative stress, SENP3 degradation is blocked by inhibition of its ubiquitination, which stabilizes it as it accumulates in the nucleoplasm. {ECO:0000250|UniProtKB:Q9H4L4}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:11029585). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (By similarity). Deconjugates SUMO2 and SUMO3 from CDCA8 (By similarity). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (By similarity). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (By similarity). Plays a role in the regulation of sumoylation status of ZNF148 (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (By similarity). {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:11029585, ECO:0000269|PubMed:22872859}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Modified residue (9); Motif (2); Region (3); Sequence conflict (2) |
| Keywords | Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11029585}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (By similarity). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (PubMed:22872859). {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}. |
| Modified Residue | MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9H4L4"; MOD_RES 71; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 73; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 170; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 182; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 206; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 226; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 12520002; 12904583; 18799693; 18948745; 19680224; 21677750; 23524851; 25772139; 29277914; 29352108; 29576508; 29771430; 30992372; 31373534; 32049023; 32237051; 33211757; 33434504; 34000626; |
| Motif | MOTIF 119..122; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 147..153; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 64,403 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B72; |