| IED ID | IndEnz0002012827 |
| Enzyme Type ID | protease012827 |
| Protein Name |
Ufm1-specific protease 2 UfSP2 EC 3.4.22.- |
| Gene Name | ufsp2 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MVVITSACIIFRIRGGLNLSFPLTATDETSAKKALFRAVCDLSSKLLSESLVLNICNSVLYIWPNTGTCTHPTELSDDTPCKDILRFIQVDDERKVSKKKEKKSQDLQQMVNIKLLFERSTSSEAVSPVIHQDISSQQLVNMVLPIDTVVSVSPDEAWGKVRQLLVNGLTHQLSEMEKCLLKYMKGTSFYVAEPNHFLLPDQGLATVIYPAGVADVQLEDCRQALHEQFNLPLDRPYFRRANAFHFPDEPYKDGYIRNPHLQLGTPPLEGATVSLVQGLYSYHHYMQDRMDDNGWGCAYRSLQTICSWFKYQGYTDKPIPTHKEIQQALVDVGDKPASFVGSRQWIGSIEVQLVLDHLLGITSKIMFVSQGTELASRGRELVHHFTSEGTPVMIGGGVLAHTILGVAWSELTGDIRFLILDPHYKGGEDLHVILEKGWCGWKGPEFWDATAYYNLCLPQRPTAI |
| Enzyme Length | 464 |
| Uniprot Accession Number | Q3B8N0 |
| Absorption | |
| Active Site | ACT_SITE 297; /evidence=ECO:0000250|UniProtKB:Q99K23; ACT_SITE 421; /evidence=ECO:0000250|UniProtKB:Q99K23; ACT_SITE 423; /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. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. {ECO:0000250|UniProtKB:Q99K23, ECO:0000250|UniProtKB:Q9NUQ7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Erroneous initiation (1) |
| Keywords | Cytoplasm;Endoplasmic reticulum;Hydrolase;Nucleus;Protease;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99K23}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99K23}. Nucleus {ECO:0000250|UniProtKB:Q99K23}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,113 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |