GCS1

MOGS
Identifiers
Aliases	MOGS , CDG2B, CWH41, DER7, GCS1, mannosyl-oligosaccharide glucosidase
External IDs	OMIM: 601336 MGI: 1929872 HomoloGene: 4593 GeneCards: MOGS
Gene location (Mouse) Chr. Chromosome 6 (mouse) [1] Band 6|6 C3 Start 83,092,477 bp [1] End 83,095,879 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas body of stomach stromal cell of endometrium right uterine tube right lobe of thyroid gland minor salivary gland right lobe of liver left lobe of thyroid gland anterior pituitary upper lobe of left lung Top expressed in primitive streak Paneth cell condyle cumulus cell somite fossa lacrimal gland abdominal wall crypt of lieberkuhn of small intestine dermis More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glucosidase activity catalytic activity hydrolase activity hydrolase activity, acting on glycosyl bonds Glc3Man9GlcNAc2 oligosaccharide glucosidase activity Cellular component integral component of membrane extracellular exosome membrane endoplasmic reticulum endoplasmic reticulum membrane Biological process metabolism protein N-linked glycosylation protein folding oligosaccharide metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7841 57377 Ensembl n/a ENSMUSG00000030036 UniProt Q13724 Q80UM7 RefSeq (mRNA) NM_006302 NM_001146158 NM_020619 RefSeq (protein) NP_001139630 NP_006293 NP_065644 Location (UCSC) n/a Chr 6: 83.09 – 83.1 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene. ^{[4] [5] [6]}

Glucosidase I is the first enzyme in the N-linked oligosaccharide processing pathway. GCS1 cleaves the distal alpha-1,2-linked glucose residue from the Glc(3)-Man(9)-GlcNAc(2) oligosaccharide precursor. GCS1 is located in the lumen of the endoplasmic reticulum. ^[6]

GCS1 may also refer to "generative cell specific 1", also called HAP2 (hapless2), a gene of lower eukaryotes which is thought to be responsible for gametes fusion . ^[7] .

References

1. GRCm38: Ensembl release 89: ENSMUSG00000030036 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Kalz-Fuller B, Bieberich E, Bause E (Sep 1995). "Sexualization and expression of glucosidase I from human hippocampus". Eur J Biochem. 231 (2): 344–51. doi:10.1111/j.1432-1033.1995.tb20706.x. PMID   7635146.
5. Kalz-Fuller B, Heidrich-Kaul C, Nothen M, Bause E, Schwanitz G (Sep 1996). "Localization of the human glucosidase I gene to chromosome 2p12-p13 by fluorescence in situ hybridization and PCR analysis of somatic cell hybrids". Genomics. 34 (3): 442–3. doi:10.1006/geno.1996.0313. PMID   8786151.
6. "Entrez Gene: GCS1 glucosidase I".
7. Goodman CD, McFadden GI (2008). "Gamete Fusion: Key Protein Identified". Current Biology. 18 (13): R571–R573. doi: 10.1016/j.cub.2008.05.007 . PMID   18606131. S2CID   14367758.

Further reading

• Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID   2136376.
• Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl: 1874/5091 . PMID   11530211. S2CID   13576808.
• Fenouillet E, Gluckman JC (1991). "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". J. Gen. Virol. 72 (8): 1919–26. doi: 10.1099/0022-1317-72-8-1919 . PMID   1678778.
• Ratner L, vander Heyden N, Dedera D (1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology. 181 (1): 180–92. doi:10.1016/0042-6822(91)90483-R. PMID   1704656.
• Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology. 187 (1): 377–82. doi:10.1016/0042-6822(92)90331-I. PMID   1736542.
• Murphy CI, Lennick M, Lehar SM, et al. (1991). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genet. Anal. Tech. Appl. 7 (6): 160–71. doi:10.1016/0735-0651(90)90030-J. PMID   2076345.
• Kalyanaraman VS, Rodriguez V, Veronese F, et al. (1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Res. Hum. Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID   2187500.
• Shimizu H, Tsuchie H, Honma H, et al. (1991). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Jpn. J. Med. Sci. Biol. 43 (3): 75–87. doi: 10.7883/yoken1952.43.75 . PMID   2283726.
• Leonard CK, Spellman MW, Riddle L, et al. (1990). "Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells". J. Biol. Chem. 265 (18): 10373–82. doi: 10.1016/S0021-9258(18)86956-3 . PMID   2355006.
• Pal R, Hoke GM, Sarngadharan MG (1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–8. Bibcode:1989PNAS...86.3384P. doi: 10.1073/pnas.86.9.3384 . PMC   287137 . PMID   2541446.
• Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". J. Virol. 63 (6): 2452–6. doi:10.1128/jvi.63.6.2452-2456.1989. PMC   250699 . PMID   2542563.
• Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID   2649653.
• Walker BD, Kowalski M, Goh WC, et al. (1987). "Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine". Proc. Natl. Acad. Sci. U.S.A. 84 (22): 8120–4. Bibcode:1987PNAS...84.8120W. doi: 10.1073/pnas.84.22.8120 . PMC   299490 . PMID   2825177.
• Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID   2829950.
• Gruters RA, Neefjes JJ, Tersmette M, et al. (1987). "Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase". Nature. 330 (6143): 74–7. Bibcode:1987Natur.330...74G. doi:10.1038/330074a0. PMID   2959866. S2CID   4270139.
• Blough HA, Pauwels R, De Clercq E, et al. (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID   3099781.
• Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. Bibcode:1988PNAS...85.9248M. doi: 10.1073/pnas.85.23.9248 . PMC   282716 . PMID   3264072.
• Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. doi:10.1128/jvi.67.1.150-160.1993. PMC   237347 . PMID   8093218.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview