| IED ID | IndEnz0002002260 |
| Enzyme Type ID | protease002260 |
| Protein Name |
Legumain EC 3.4.22.34 Asparaginyl endopeptidase Protease, cysteine 1 |
| Gene Name | Lgmn Prsc1 |
| 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 | MTWRVAVLLSLVLGAGAVHIGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANNEENPTPGVVINRPNGTDVYKGVPKDYTGEDVTPENFLAVLRGDEEAVKGKGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDIDVYATTAANPNESSYACYYDEERSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRKLLRTNNMKESQVLVGQIQHLLDARHIIEKSVQKIVSLLAGFGETAQKHLSERAMLTAHDCHQEAVTHFRTHCFNWHSVTYEHALRYLYVLANLCEKPYPIDRIKMAMDKVCLSHY |
| Enzyme Length | 435 |
| Uniprot Accession Number | Q9R0J8 |
| Absorption | |
| Active Site | ACT_SITE 150; /evidence=ECO:0000250; ACT_SITE 191; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; |
| DNA Binding | |
| EC Number | 3.4.22.34 |
| Enzyme Function | FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Glycosylation (5); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9742219}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by autocatalytic processing at pH 4. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20234379; 21610319; 30676070; 31521890; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,466 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |