| IED ID | IndEnz0002010072 |
| Enzyme Type ID | protease010072 |
| Protein Name |
Ufm1-specific protease 2 UfSP2 EC 3.4.22.- |
| Gene Name | UFSP2 C4orf20 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVISESMDILFRIRGGLDLAFQLATPNEIFLKKALKHVLSDLSTKLSSNALVFRICHSSVYIWPSSDINTIPGELTDASACKNILRFIQFEPEEDIKRKFMRKKDKKLSDMHQIVNIDLMLEMSTSLAAVTPIIERESGGHHYVNMTLPVDAVISVAPEETWGKVRKLLVDAIHNQLTDMEKCILKYMKGTSIVVPEPLHFLLPGKKNLVTISYPSGIPDGQLQAYRKELHDLFNLPHDRPYFKRSNAYHFPDEPYKDGYIRNPHTYLNPPNMETGMIYVVQGIYGYHHYMQDRIDDNGWGCAYRSLQTICSWFKHQGYTERSIPTHREIQQALVDAGDKPATFVGSRQWIGSIEVQLVLNQLIGITSKILFVSQGSEIASQGRELANHFQSEGTPVMIGGGVLAHTILGVAWNEITGQIKFLILDPHYTGAEDLQVILEKGWCGWKGPDFWNKDAYYNLCLPQRPNMI |
| Enzyme Length | 469 |
| Uniprot Accession Number | Q9NUQ7 |
| Absorption | |
| Active Site | ACT_SITE 302; /evidence=ECO:0000305|PubMed:25219498; ACT_SITE 426; /evidence=ECO:0000250|UniProtKB:Q99K23; ACT_SITE 428; /evidence=ECO:0000250|UniProtKB:Q99K23 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins (PubMed:25219498, PubMed:32160526). Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins (PubMed:25219498). Through TRIP4 deufmylation may regulate intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation (PubMed:25219498). {ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:32160526}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Modified residue (1); Mutagenesis (1); Natural variant (3); Sequence conflict (2) |
| Keywords | Acetylation;Cytoplasm;Disease variant;Dwarfism;Endoplasmic reticulum;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | P41238; P25800 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99K23}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99K23}. Nucleus {ECO:0000250|UniProtKB:Q99K23}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:25732826 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 26496610; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,261 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |