GCS1

Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene.[5][6][7]

MOGS
Identifiers
Aliases	MOGS, CDG2B, CWH41, DER7, GCS1, mannosyl-oligosaccharide glucosidase
External IDs	OMIM: 601336 MGI: 1929872 HomoloGene: 4593 GeneCards: MOGS
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p13.1 Start 74,461,057 bp[1] End 74,465,410 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 C3 Start 83,115,496 bp[2] End 83,118,898 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • glucosidase activity • catalytic activity • hydrolase activity • hydrolase activity, acting on glycosyl bonds • mannosyl-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	ENSG00000115275	ENSMUSG00000030036
UniProt	Q13724	Q80UM7
RefSeq (mRNA)	NM_006302 NM_001146158	NM_020619
RefSeq (protein)	NP_001139630 NP_006293	NP_065644
Location (UCSC)	Chr 2: 74.46 – 74.47 Mb	Chr 6: 83.12 – 83.12 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

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 .[8] .

References

1. GRCh38: Ensembl release 89: ENSG00000115275 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030036 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: GCS1 glucosidase I".
8. Goodman CD, McFadden GI (2008). "Gamete Fusion: Key Protein Identified". Current Biology. 18 (13): R571–R573. doi:10.1016/j.cub.2008.05.007. Retrieved 06.05.09. Check date values in: |accessdate= (help)

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.
• 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. 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.
• 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