LMPD Database

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LMP012938

UniProt Annotations

Entry Information
Gene NameUDP-glucose glycoprotein glucosyltransferase 1
Protein EntryUGGG1_RAT
UniProt IDQ9JLA3
SpeciesRat
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=44 uM for UDP-glucose (in the presence of 0.5 uM denatured acid phosphatase) {ECO:0000269|PubMed:10764828, ECO:0000269|PubMed:1533626}; Vmax=34 pmol/h/mg enzyme toward UDP-glucose (in the presence of 0.5 uM denatured acid phosphatase) {ECO:0000269|PubMed:10764828, ECO:0000269|PubMed:1533626}; pH dependence: Optimum pH is 7.6-8.0. {ECO:0000269|PubMed:10764828, ECO:0000269|PubMed:1533626};
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence= ;
DomainN-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects.
FunctionRecognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. {ECO:0000269|PubMed:10764828, ECO:0000269|PubMed:14730348, ECO:0000269|PubMed:15861139}.
PathwayProtein modification; protein glycosylation.
Sequence CautionSequence=AAF67072.1; Type=Erroneous initiation; Evidence= ;
SimilarityBelongs to the glycosyltransferase 8 family
Subcellular LocationEndoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:11535823}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:11535823}.
SubunitMonomer as well as in a tight complex with SEP15. Interacts with METTL23 (By similarity)