ALG1

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; OMA:ALG1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 5,033,702 bp[1] End 5,087,379 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 A1 Start 5,051,485 bp[2] End 5,062,776 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium buccal mucosa cell body of pancreas left adrenal gland right adrenal cortex mucosa of transverse colon left adrenal cortex body of stomach islet of Langerhans right testis Top expressed in right kidney vestibular membrane of cochlear duct otic vesicle proximal tubule utricle stroma of bone marrow saccule lacrimal gland neural layer of retina molar More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity glycosyltransferase activity 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: 5.05 – 5.06 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

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. doi:10.1016/S0021-9258(17)43670-2. 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. doi:10.1016/S0021-9258(17)43670-2. 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. hdl:20.500.11850/51881. 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. Bibcode:2002PNAS...9916899M. 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.