DPM2

Dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit
Identifiers
Symbols	DPM2 ; CDG1U
External IDs	OMIM: 603564 MGI: 1330238 HomoloGene: 99726 ChEMBL: 4479 GeneCards: DPM2 Gene
EC number	2.4.1.83
Gene ontology Molecular function • dolichyl-phosphate beta-D-mannosyltransferase activity • protein binding • enzyme regulator activity Cellular component • glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex • endoplasmic reticulum membrane • integral component of endoplasmic reticulum membrane • dolichol-phosphate-mannose synthase complex Biological process • dolichol-linked oligosaccharide biosynthetic process • C-terminal protein lipidation • GPI anchor biosynthetic process • preassembly of GPI anchor in ER membrane • protein N-linked glycosylation via asparagine • dolichol metabolic process • regulation of protein stability • protein O-linked mannosylation • post-translational protein modification • cellular protein metabolic process • regulation of catalytic activity Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8818	13481
Ensembl	ENSG00000136908	ENSMUSG00000026810
UniProt	O94777	Q9Z324
RefSeq (mRNA)	NM_003863	NM_010073
RefSeq (protein)	NP_003854	NP_034203
Location (UCSC)	Chr 9: 127.94 – 127.94 Mb	Chr 2: 32.57 – 32.57 Mb
PubMed search

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.^[1]

Function

Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins, defective N-linked glycosylation and deficient O-mannosylation of α-dystroglycan. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. The protein encoded by this gene is a hydrophobic protein that contains 2 predicted transmembrane domains and a putative ER localization signal near the C-terminus. This protein associates with DPM1 in vivo and is required for the ER localization and stable expression of DPM1 and also enhances the binding of dolichol-phosphate to DPM1.^[1]

Clinical significance

Mutations in this gene are associated with congenital disorder of glycosylation.

References

1. "Entrez Gene: dolichyl-phosphate mannosyltransferase polypeptide 2".

Further reading

• Suzuki H, Fukunishi Y, Kagawa I; et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs.". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
• Maeda Y, Tanaka S, Hino J; et al. (2000). "Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3.". EMBO J. 19 (11): 2475–82. doi:10.1093/emboj/19.11.2475. PMC 212771. PMID 10835346.
• Watanabe R, Murakami Y, Marmor MD; et al. (2000). "Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2.". EMBO J. 19 (16): 4402–11. doi:10.1093/emboj/19.16.4402. PMC 302040. PMID 10944123.
• Kinoshita T, Inoue N (2000). "Dissecting and manipulating the pathway for glycosylphos-phatidylinositol-anchor biosynthesis.". Curr Opin Chem Biol 4 (6): 632–8. doi:10.1016/s1367-5931(00)00151-4. PMID 11102867.
• Ashida H, Maeda Y, Kinoshita T (2006). "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3.". J. Biol. Chem. 281 (2): 896–904. doi:10.1074/jbc.M511311200. PMID 16280320.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2002). "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.
• Lennon G, Auffray C, Polymeropoulos M, Soares MB (1996). "The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression.". Genomics 33 (1): 151–2. doi:10.1006/geno.1996.0177. PMID 8617505.
• Maeda Y, Tomita S, Watanabe R; et al. (1998). "DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.". EMBO J. 17 (17): 4920–9. doi:10.1093/emboj/17.17.4920. PMC 1170821. PMID 9724629.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.