| IED ID | IndEnz0002009484 |
| Enzyme Type ID | protease009484 |
| Protein Name |
Sentrin-specific protease 2 EC 3.4.22.- Axin-associating molecule Axam Sentrin/SUMO-specific protease SENP2 |
| Gene Name | Senp2 |
| 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 | MYRWLTKVLGTILRLCERPAPGARALLKRRRSSSSLFSTAVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVSSACNGTRNVAPSGEVFSNSPSCELTTSGSCSSMLKLGNKSPNGISDYPKIRVTVARDQPRRVLPSFGFTLKSEGYNRRPSGRRHSKSNPESSLPWKPQEQGVTEMISEEGGKGARRPHCTVEEGVQKDEREKYLKLLERLKEGAHGSTFPPAVSHHSSQRTQMDTLKTKGWMEEQNHGVRTTHLVPKQYRVVETRGPLCSVRSEKRYSKGKADTEKVVGLRFEKDGTRGHQLEPDLSEEVSARLRLGSGSNGLLRRKISVLEAKEKNFPSKEKDRRTEDLFELTEDMEKEISNALGHGPPDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERSKKQGYPALHALSTFFYPKLKSGGYQAVKRWTKGVNLFDQELVLVPIHRKVHWSLVVMDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNTDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL |
| Enzyme Length | 588 |
| Uniprot Accession Number | Q9EQE1 |
| Absorption | |
| Active Site | ACT_SITE 477; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 494; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 547; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q9HC62 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway (By similarity). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (By similarity). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (By similarity). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (PubMed:10944533, PubMed:11997515). Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (By similarity). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:10944533, ECO:0000269|PubMed:11997515}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Modified residue (3); Motif (3); Mutagenesis (1); Region (3) |
| Keywords | Cytoplasm;Hydrolase;Membrane;Nuclear pore complex;Nucleus;Phosphoprotein;Protease;Protein transport;Reference proteome;Thiol protease;Translocation;Transport;Ubl conjugation;Ubl conjugation pathway;Wnt signaling pathway;mRNA transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}. |
| Modified Residue | MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62; MOD_RES 332; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62; MOD_RES 343; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62 |
| Post Translational Modification | PTM: Polyubiquitinated; which leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q9HC62}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 28..31; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 47..52; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 316..331; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:Q9HC62 |
| Gene Encoded By | |
| Mass | 67,252 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |