| IED ID | IndEnz0002019266 |
| Enzyme Type ID | protease019266 |
| Protein Name |
ER degradation-enhancing alpha-mannosidase-like protein 3 EC 3.2.1.113 Alpha-1,2-mannosidase EDEM3 |
| Gene Name | edem3 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MGCPAVEARRWGDMWLVVAFCLLGHGHAAVTKEEKAHLRSQVLEMFDHAYGNYMQHAYPADELMPLTCRGRIRGQEPSRGDVDDALGKFSLTLIDTLDTLVVLNKTKEFEDAVRKVITDVNLDNDIVVSVFETNIRVLGGLLGGHSVAIMLKENGDGMQWYNDELLHMAKELGYKLLPAFNTTSGLPYPRINLKFGIRRPEARTGTETDTCTACAGTMILEFAALSRFTGISVFEEHARKALDFLWDKRQRSSNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSYLERFNTHYDAIMRYISQPPLLLDVHIHKPMLTARTWMDSLLAFFPGLQVLKGDIRPAIETHEMLYQVIKKHNFLPEAFTTDFRVHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIDNLNKYARVPCGFAAVKDVRTGSHEDRMDSFFLAEMFKYLYLLFSEREDLIFDIEDYIFTTEAHLLPLSLSTANPSSTKKNTTTQYTELDDSNFDWSCPNTQILFRNDPMYAQNIREPLKNVVDKNCPRSPSRLDEISGSGKMPPLRARDFMASNSEHLEILKKMGVSLIHLKDGRVQLVQHANQAASSIDAEDGLRFMQEMIELSSQQQKEQQLPPRAVQIVSHPFYGRVVLTAGPAQFGMDLSKHLAGAQGLVARAEPYSGCSDITNGQAIQGKIALMQRGQCMFAEKARNVQKAGAIGGIVIDDNEGSSSDTAPLFQMAGDGKSTDDVTIPMLFLFSKEGNIILDAIREYQQVEVLLSDKAKDRDLESESGEQKPVENDSQKQALEDLFMTPEEIAELLIVHEEESPVSQPEVPSSDSPSGGDRTSERDITPESQEHKTEETEHSPKDNVQTPPENSEDSTEEKMDNKVQPMESILADWKEDIEAFEMMEKDEL |
| Enzyme Length | 913 |
| Uniprot Accession Number | Q6GQB9 |
| Absorption | |
| Active Site | ACT_SITE 132; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 279; /evidence=ECO:0000250; ACT_SITE 373; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P31723; ACT_SITE 391; /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: May be involved in endoplasmic reticulum-associated degradation (ERAD). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Glycosylation (4); Metal binding (1); Motif (1); Region (1); Signal peptide (1) |
| Keywords | Endoplasmic reticulum;Glycoprotein;Hydrolase;Metal-binding;Signal;Unfolded protein response |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 910..913; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
| Gene Encoded By | |
| Mass | 102,735 |
| Kinetics | |
| Metal Binding | METAL 477; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P32906 |
| Rhea ID | RHEA:56008; RHEA:56028 |
| Cross Reference Brenda |