DPM3

DPM3
Identifiers
Aliases	DPM3, CDG1O, dolichyl-phosphate mannosyltransferase subunit 3
External IDs	MGI: 1915813 HomoloGene: 17810 GeneCards: DPM3
Gene ontology Molecular function • dolichyl-phosphate beta-D-mannosyltransferase activity • protein binding Cellular component • integral component of membrane • dolichol-phosphate-mannose synthase complex • integral component of endoplasmic reticulum membrane • mannosyltransferase complex • endoplasmic reticulum membrane • endoplasmic reticulum • membrane Biological process • protein glycosylation • GPI anchor biosynthetic process • protein mannosylation • protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan • regulation of protein stability • protein O-linked mannosylation • protein N-linked glycosylation via asparagine • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54344	68563
Ensembl	ENSG00000179085	ENSMUSG00000042737
UniProt	Q9P2X0 Q86TM7	Q9D1Q4
RefSeq (mRNA)	NM_153741 NM_018973	NM_026767
RefSeq (protein)	NP_061846.2 NP_714963.1 NP_714963.1	NP_081043.1
Location (UCSC)	Chr 1: 155.14 – 155.14 Mb	Chr 3: 89.26 – 89.27 Mb
PubMed search	[1]	[2]
Wikidata

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dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.^[3][4]

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. 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 subunit of dolichyl-phosphate mannosyltransferase and acts as a stabilizer subunit of the dolichyl-phosphate mannosyltransferase complex.^[3]

Clinical significance

Mutations in this gene are associated with congenital disorder of glycosylation type 1O.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: dolichyl-phosphate mannosyltransferase polypeptide 3".
4. Maeda Y, Tanaka S, Hino J, Kangawa K, Kinoshita T (June 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.
5. Haeuptle MA, Hennet T (December 2009). "Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides". Hum. Mutat. 30 (12): 1628–41. doi:10.1002/humu.21126. PMID 19862844.

Further reading

• Maeda Y, Watanabe R, Harris CL, et al. (2001). "PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER.". EMBO J. 20 (1-2): 250–61. doi:10.1093/emboj/20.1.250. PMC 140182. PMID 11226175.
• 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.
• 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.
• 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.
• Manos EJ, Kim ML, Kassis J, et al. (2001). "Dolichol-phosphate-mannose-3 (DPM3)/prostin-1 is a novel phospholipase C-gamma regulated gene negatively associated with prostate tumor invasion.". Oncogene. 20 (22): 2781–90. doi:10.1038/sj.onc.1204379. PMID 11420690.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview

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