| IED ID | IndEnz0002019264 |
| Enzyme Type ID | protease019264 |
| Protein Name |
ER degradation-enhancing alpha-mannosidase-like protein 3 EC 3.2.1.113 Alpha-1,2-mannosidase EDEM3 |
| Gene Name | Edem3 |
| 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 | MSKAGGCRGCGCRVPQRASWSLVAATAALCLVLATSVCTAGAAPMSREEKQKLGNQVLEMFDHAYGNYMEHAYPADELMPLTCRGRVRGQEPSRGDVDDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDNDVVVSVFETNIRVLGGLLGGHSLAIMLKEKGEHMQWYNDELLHMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPEARTGTETDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSSNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSFLERFNTHYDAIMRYISQPPLLLDVHIHKPMLNARTWMDALLAFFPGLQVLKGDIRPAIETHEMLYQVIKKHNFLPEAFTTDFRVHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIENLNKYARVPCGFAAMKDVRTGSHEDRMDSFFLAEMFKYLYLLFADKEDIIFDIEDYIFTTEAHLLPLWLSTTNRSISKKNTTSEYTELDDSNFDWTCPNTQILFPNDPLYAQSIREPLKNVVDKSCPRGIIRVEESFRSGAKPPLRARDFMATNPEHLEILKKMGVSLIHLKDGRVQLVQHAIQAASSIDAEDGLRFMQEMIELSSQQQKEQQLPPRAVQIISHPFFGRVVLTAGPAQFGLDLSKHKETRGFVASSKPYNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREHEQVEVLLSDKARDRDPEMENEDQPSSENDSQNQSAEQMLSLSQTVDLADKESPEHPADSHSEASPSDSEEAAGFAPSEQISGSTENHETTSLDGECTDLDNQVQEQSETEEDSSPNVSWGTKAQPIDSILADWNEDIEAFEMMEKDEL |
| Enzyme Length | 931 |
| Uniprot Accession Number | Q2HXL6 |
| Absorption | |
| Active Site | ACT_SITE 147; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 294; /evidence=ECO:0000250; ACT_SITE 388; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P31723; ACT_SITE 406; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; |
| DNA Binding | |
| EC Number | 3.2.1.113 |
| Enzyme Function | FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity. {ECO:0000250|UniProtKB:Q9BZQ6, ECO:0000269|PubMed:16431915}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (1); Compositional bias (4); Domain (1); Glycosylation (7); Metal binding (1); Motif (1); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Endoplasmic reticulum;Glycoprotein;Hydrolase;Metal-binding;Reference proteome;Signal;Unfolded protein response |
| Interact With | |
| Induction | INDUCTION: Slightly increased by endoplasmic reticulum stress. {ECO:0000269|PubMed:16431915}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:16431915}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. |
| Signal Peptide | SIGNAL 1..42; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12520002; 14610273; 16141072; 21267068; 22665516; 32213464; 33671632; |
| Motif | MOTIF 928..931; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
| Gene Encoded By | |
| Mass | 104,200 |
| Kinetics | |
| Metal Binding | METAL 492; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P32906 |
| Rhea ID | RHEA:56008; RHEA:56028 |
| Cross Reference Brenda | 3.2.1.209; |