| IED ID | IndEnz0002002258 |
| Enzyme Type ID | protease002258 |
| Protein Name |
Legumain EC 3.4.22.34 Asparaginyl endopeptidase Protease, cysteine 1 |
| Gene Name | Lgmn Prsc1 |
| 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 | MTWRVAVLLSLVLGAGAVPVGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDVTPENFLAVLRGDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPNDDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDINVYATTAANPKESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRTHCFNWHSVTYEHALRYLYVLANLCEAPYPIDRIEMAMDKVCLSHY |
| Enzyme Length | 435 |
| Uniprot Accession Number | O89017 |
| Absorption | |
| Active Site | ACT_SITE 150; /evidence=ECO:0000269|PubMed:9891971; ACT_SITE 191; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9891971 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cystatin-C. {ECO:0000269|PubMed:24407422}. |
| 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; Evidence={ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:9742219, ECO:0000269|PubMed:9891971}; |
| 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. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. 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. {ECO:0000269|PubMed:17350006, ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:9742219}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:9742219}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Disulfide bond (2); Glycosylation (4); Helix (20); Mutagenesis (9); Propeptide (1); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:9742219}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000305|PubMed:24407422}.; PTM: Activated by autocatalytic processing at pH 4. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4NOJ; 4NOK; 4NOL; 4NOM; |
| Mapped Pubmed ID | 10725249; 12775715; 12904583; 14610273; 15044380; 15905550; 16141072; 18374643; 18799693; 19106291; 19879164; 20164435; 20234379; 20495178; 21267068; 21308776; 21606482; 22718532; 22916010; 23237799; 24952961; 25326800; 26462467; 26549211; 27514475; 27626380; 28162997; 29414692; 29769405; 29934589; 30030107; 30135302; 30373880; 30530690; 30559339; 30676070; 33172978; 33219900; 33383559; 33677035; 34260075; 34509465; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,373 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.34; |