Mannosyl-oligosaccharide glucosidase (MOGS)
The protein contains 837 amino acids for an estimated molecular weight of 91918 Da.
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner. (updated: Oct. 17, 2006)
Protein identification was indicated in the following studies:
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs3213671 | |
| dbSNP:rs1063587 | |
| dbSNP:rs1063588 | |
| dbSNP:rs2268416 | |
| CDGIIb | |
| dbSNP:rs34075781 | |
| CDGIIb | |
| dbSNP:rs35533773 |
Biological Process
Oligosaccharide metabolic process
Protein folding
Protein N-linked glycosylation
Viral protein processing
The reference OMIM entry for this protein is 601336
Mannosyl-oligosaccharide glycosidase; mogs
Glucosidase i; gcs1
DESCRIPTION
The processing of N-linked glycoproteins is initiated by the action of glucosidase I, which cleaves specifically the distal alpha-1,2-linked glucose residue in the Glc(3)-Man(9)-GlcNAc(2) oligosaccharide precursor after its en bloc transfer from dolichyl diphosphate to the nascent polypeptide chain (Kornfeld and Kornfeld, 1985). The resulting Glc(2)-Man(9)-GlcNAc(2) intermediate is then further modified by glucosidase II and several ER- and Golgi-resident mannosidases and glycosyltransferases, finally yielding a complex array of glycan structures.CLONING
Kalz-Fuller et al. (1995) used the amino acid sequence of tryptic peptides of the pig liver glucosidase I enzyme to synthesize degenerate oligonucleotides that were used to amplify a specific cDNA probe by PCR with porcine cDNA. Screening of a human hippocampus cDNA library with this probe resulted in the isolation of several glucosidase I-specific clones, allowing the reconstruction of a full-length human cDNA of 2,881 bp. The oligonucleotide sequence showed no homology to other processing enzymes cloned to that time.MAPPING
By fluorescence in situ hybridization, Kalz-Fuller et al. (1996) mapped the GCS1 gene to chromosome 2p13-p12. They confirmed the localization with PCR-based analysis of somatic cell hybrids.MOLECULAR GENETICS
De Praeter et al. (2000) identified a glucosidase I defect in a neonate with severe generalized hypotonia and dysmorphic features consistent with congenital disorder of glycosylation type IIb (CDG2B; 606056). Molecular studies showed that the patient was a compound heterozygote for 2 missense mutations in the GCS1 gene (601336.0001-601336.0002). In 2 sibs with CDG2B, Sadat et al. (2014) identified compound heterozygous mutations in the MOGS gene (601336.0003 and 601336.0004). The mutations resulted in lack of detectable protein expression. Each unaffected parent was heterozygous for 1 of the mutant alleles. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 601336 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).