DPM2

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.[5]

DPM2
Identifiers
Aliases	DPM2, CDG1U, dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit, dolichyl-phosphate mannosyltransferase subunit 2, regulatory
External IDs	OMIM: 603564 MGI: 1330238 HomoloGene: 99726 GeneCards: DPM2
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q34.11 Start 127,935,099 bp[1] End 127,938,484 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 B Start 32,570,858 bp[2] End 32,573,579 bp[2]
Gene ontology Molecular function • dolichyl-phosphate beta-D-mannosyltransferase activity • GO:0001948 protein binding • GO:0010576 enzyme regulator activity Cellular component • integral component of membrane • endoplasmic reticulum membrane • membrane • integral component of endoplasmic reticulum membrane • endoplasmic reticulum • dolichol-phosphate-mannose synthase complex • glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Biological process • preassembly of GPI anchor in ER membrane • regulation of protein stability • protein O-linked mannosylation • protein glycosylation • GPI anchor biosynthetic process • GO:0048552 regulation of catalytic activity • dolichol metabolic process • protein N-linked glycosylation via asparagine Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8818	13481
Ensembl	ENSG00000136908	ENSMUSG00000026810
UniProt	O94777	Q9Z324
RefSeq (mRNA)	NM_152690 NM_003863	NM_010073
RefSeq (protein)	NP_003854 NP_001365365 NP_001365366	NP_034203
Location (UCSC)	Chr 9: 127.94 – 127.94 Mb	Chr 2: 32.57 – 32.57 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

Clinical significance

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

References

1. GRCh38: Ensembl release 89: ENSG00000136908 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026810 - 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. "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. Bibcode:2002PNAS...9916899M. 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.