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UniProt functional annotation for Q9UKM7 | ||
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| UniProt code: Q9UKM7. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2). {ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:18003979}. |
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| 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:0000269|PubMed:10409699, ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:15713668}; |
| 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:0000269|PubMed:10409699, ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:15713668}; |
| Cofactor: | |
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; |
| Activity regulation: | |
Inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine. {ECO:0000269|PubMed:10409699}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.4 mM for Man9GlcNAc2 {ECO:0000269|PubMed:10521544}; pH dependence: Optimum pH is between 6.5 and 6.9. {ECO:0000269|PubMed:10521544}; |
| Pathway: | |
Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. |
| Subcellular location: | |
Endoplasmic reticulum membrane {ECO:0000269|PubMed:10409699}; Single-pass type II membrane protein {ECO:0000269|PubMed:10409699}. |
| Tissue specificity: | |
Widely expressed. {ECO:0000269|PubMed:10409699, ECO:0000269|PubMed:10521544}. |
| Disease: | |
Rafiq syndrome (RAFQS) [MIM:614202]: An autosomal recessive disorder characterized by variably impaired intellectual and motor development, a characteristic facial dysmorphism, truncal obesity, and hypotonia. The facial dysmorphism comprises prominent eyebrows with lateral thinning, downward-slanting palpebral fissures, bulbous tip of the nose, large ears, and a thin upper lip. Behavioral problems, including overeating, verbal and physical aggression, have been reported in some cases. Serum transferrin isoelectric focusing shows a type 2 pattern. {ECO:0000269|PubMed:21763484}. Note=The disease is caused by variants affecting the gene represented in this entry. |
| Similarity: | |
Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.