DPM2

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; OMA:DPM2 - orthologs
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 32,460,870 bp [2] End 32,463,591 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas left lobe of thyroid gland right lobe of thyroid gland body of stomach right uterine tube mucosa of transverse colon islet of Langerhans stromal cell of endometrium right frontal lobe minor salivary glands Top expressed in yolk sac perirhinal cortex entorhinal cortex granulocyte superior frontal gyrus primary visual cortex neural tube CA3 field internal carotid artery lip More reference expression data BioGPS n/a
Gene ontology Molecular function dolichyl-phosphate beta-D-mannosyltransferase activity protein binding 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 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: 32.46 – 32.46 Mb PubMed search [3] [4]
Wikidata
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Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene. ^[5]

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.