GCS1

MOGS
Identifiers
Aliases	MOGS,CDG2B, CWH41, DER7, GCS1, mannosyl-oligosaccharide glucosidase
External IDs	OMIM:601336;MGI:1929872;HomoloGene:4593;GeneCards:MOGS;OMA:MOGS - orthologs
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 C3 Start 83,092,477bp End 83,095,879bp
RNA expressionpattern 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 glands 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 fetal liver hematopoietic progenitor cell lacrimal gland epiblast abdominal wall 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 PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Mannosyl-oligosaccharide glucosidaseis anenzymethat in humans is encoded by theMOGSgene.

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.

GCS1 may also refer to "generative cell specific 1", also called HAP2 (hapless2), a gene of lowereukaryoteswhich is thought to be responsible forgametesfusion. .

Further reading

• Feizi T, Larkin M (1992). "AIDS and glycosylation".Glycobiology.1(1): 17–23.doi:10.1093/glycob/1.1.17.PMID2136376.
• 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.PMID11530211.S2CID13576808.
• 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.PMID1678778.
• 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.PMID1704656.
• 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.PMID1736542.
• 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.PMID2076345.
• 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.PMID2187500.
• 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.PMID2283726.
• 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.PMID2355006.
• 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.PMC287137.PMID2541446.
• 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.PMC250699.PMID2542563.
• 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.PMID2649653.
• 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.PMC299490.PMID2825177.
• 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.PMID2829950.
• 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.PMID2959866.S2CID4270139.
• 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.PMID3099781.
• 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.PMC282716.PMID3264072.
• 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.PMC237347.PMID8093218.

External links

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