Alpha-1,3/1,6-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene.[4] Mutations in the human gene are associated with congenital defects in glycosylation [5][6] The protein encoded by the ALG2 gene belongs to two classes of enzymes: GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase (EC 2.4.1.132) and GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase (EC 2.4.1.257).

ALG2
Identifiers
AliasesALG2, CDGIi, NET38, hALPG2, CMS14, CMSTA3, alpha-1,3/1,6-mannosyltransferase, CDG1I, ALG2 alpha-1,3/1,6-mannosyltransferase
External IDsOMIM: 607905; MGI: 1914731; HomoloGene: 5930; GeneCards: ALG2; OMA:ALG2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_033087
NM_197973

NM_019998
NM_001355496

RefSeq (protein)

NP_149078

NP_064382
NP_001342425

Location (UCSC)n/aChr 4: 47.47 – 47.47 Mb
PubMed search[2][3]
Wikidata
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Function

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This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).[6]

Interactions

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ALG2 has been shown to interact with ANXA7[7] and ANXA11.[7]

References

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  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039740Ensembl, 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. ^ Jackson BJ, Kukuruzinska MA, Robbins P (August 1993). "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation". Glycobiology. 3 (4): 357–64. doi:10.1093/glycob/3.4.357. PMID 8400550.
  5. ^ Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschütter A, von Figura K, Lehle L, Körner C (June 2003). "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis". The Journal of Biological Chemistry. 278 (25): 22498–505. doi:10.1074/jbc.M302850200. PMID 12684507.
  6. ^ a b "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)".
  7. ^ a b Satoh H, Nakano Y, Shibata H, Maki M (November 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.

Further reading

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