Detail Information for IndEnz0002002258
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;