| IED ID | IndEnz0002012860 |
| Enzyme Type ID | protease012860 |
| Protein Name |
Proteasome subunit beta type-10 EC 3.4.25.1 Low molecular mass protein 10 Macropain subunit MECl-1 Multicatalytic endopeptidase complex subunit MECl-1 Proteasome MECl-1 Proteasome subunit beta-2i |
| Gene Name | Psmb10 Lmp10 Mecl1 |
| 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 | MLKQAVEPTGGFSFENCQRNASLEHVLPGLRVPHARKTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAITAGILSDLGSGGNVDACVITAGGAKLQRALSTPTEPVQRAGRYRFAPGTTPVLTREVRPLTLELLEETVQAMEVE |
| Enzyme Length | 273 |
| Uniprot Accession Number | O35955 |
| Absorption | |
| Active Site | ACT_SITE 40; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; |
| DNA Binding | |
| EC Number | 3.4.25.1 |
| Enzyme Function | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response. {ECO:0000269|PubMed:22341445}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (1); Helix (4); Modified residue (1); Mutagenesis (1); Propeptide (1); Sequence conflict (3); Site (1); Turn (1) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. {ECO:0000269|PubMed:15907481}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P40306 |
| Post Translational Modification | PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000305|PubMed:10413086}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3UNF; 3UNH; |
| Mapped Pubmed ID | 10047537; 10047538; 12220526; 14610273; 14645204; 14681479; 15199151; 15537664; 16141072; 16547243; 16615898; 16857963; 17114438; 17540904; 17548590; 18160473; 18799693; 20228196; 20345760; 20525886; 20881186; 20881299; 21108466; 21267068; 21360704; 21455681; 21677750; 21862448; 21887316; 22013127; 22197977; 22398747; 22772448; 22984077; 23365662; 23709680; 25770130; 25978061; 26464284; 27294792; 27544233; 27875560; 28157553; 28478040; 29067678; 29186691; 29499566; 29507100; 29654304; 29950673; 31629736; 32160764; 32581853; 33195259; 34547302; 9131260; 9174609; |
| Motif | |
| Gene Encoded By | |
| Mass | 29,063 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |