ALG1

Chitobiosyldiphosphodolichol beta-mannosyltransferase is an enzyme that is encoded by ALG1[5] whose structure and function has been conserved from lower to higher organisms.[6][7]

ALG1
Identifiers
Aliases	ALG1, CDG1K, HMAT1, HMT-1, HMT1, MT-1, Mat-1, hMat-1, chitobiosyldiphosphodolichol beta-mannosyltransferase, ALG1 chitobiosyldiphosphodolichol beta-mannosyltransferase
External IDs	OMIM: 605907 MGI: 2384774 HomoloGene: 5387 GeneCards: ALG1
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 5,033,923 bp[1] End 5,087,379 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 A1 Start 5,233,621 bp[2] End 5,244,912 bp[2]
Gene ontology Molecular function • transferase activity • transferase activity, transferring glycosyl groups • mannosyltransferase activity • chitobiosyldiphosphodolichol beta-mannosyltransferase activity Cellular component • integral component of membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane Biological process • dolichol-linked oligosaccharide biosynthetic process • mannosylation • protein glycosylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	56052	208211
Ensembl	ENSG00000033011	ENSMUSG00000039427
UniProt	Q9BT22	Q921Q3
RefSeq (mRNA)	NM_019109 NM_001330504	NM_145362
RefSeq (protein)	NP_001317433 NP_061982	NP_663337
Location (UCSC)	Chr 16: 5.03 – 5.09 Mb	Chr 16: 5.23 – 5.24 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The biosynthesis of lipid-linked oligosaccharides is highly conserved among eukaryotes and is catalyzed by 14 glycosyltransferases in an ordered stepwise manner. The Alg1 mannosyltransferase I (MT I) catalyzes the first mannosylation step in this process.[6] Clinically, the deficiency of ALG1 in humans results in ALG1-CDG, a congenital disorder of glycosylation.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000033011 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039427 - 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. Couto JR, Huffaker TC, Robbins PW (1984). "Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway". J. Biol. Chem. 259 (1): 378–82. PMID 6368538.
6. "Entrez Gene: ALG1 asparagine-linked glycosylation 1 homolog (S. cerevisiae, beta-1,4-mannosyltransferase)".
7. Takahashi T, Honda R, Nishikawa Y (Mar 2000). "Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1". Glycobiology. 10 (3): 321–7. doi:10.1093/glycob/10.3.321. PMID 10704531.
8. "# 608540 CONGENITAL DISORDER OF GLYCOSYLATION, TYPE Ik; CDG1K". Johns Hopkins University. Retrieved 2019-05-01.

Further reading

• Couto JR, Huffaker TC, Robbins PW (January 1984). "Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway". J. Biol. Chem. 259 (1): 378–82. PMID 6368538.
• Gao XD, Nishikawa A, Dean N (June 2004). "Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum". Glycobiology. 14 (6): 559–70. doi:10.1093/glycob/cwh072. PMID 15044395.
• Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kranz C, Denecke J, Lehle L, et al. (2004). "Congenital Disorder of Glycosylation Type Ik (CDG-Ik): A Defect of Mannosyltransferase I". Am. J. Hum. Genet. 74 (3): 545–51. doi:10.1086/382493. PMC 1182267. PMID 14973782.
• Schwarz M, Thiel C, Lübbehusen J, et al. (2004). "Deficiency of GDP-Man:GlcNAc2-PP-Dolichol Mannosyltransferase Causes Congenital Disorder of Glycosylation Type Ik". Am. J. Hum. Genet. 74 (3): 472–81. doi:10.1086/382492. PMC 1182261. PMID 14973778.
• Grubenmann CE, Frank CG, Hülsmeier AJ, et al. (2004). "Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik". Hum. Mol. Genet. 13 (5): 535–42. doi:10.1093/hmg/ddh050. PMID 14709599.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
• Human ALG1 genome location and ALG1 gene details page in the UCSC Genome Browser.