DPM3

dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.[5][6]

DPM3
Identifiers
Aliases	DPM3, CDG1O, dolichyl-phosphate mannosyltransferase subunit 3, dolichyl-phosphate mannosyltransferase subunit 3, regulatory
External IDs	OMIM: 605951 MGI: 1915813 HomoloGene: 17810 GeneCards: DPM3
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q22 Start 155,139,891 bp[1] End 155,140,595 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F1 Start 89,259,358 bp[2] End 89,267,079 bp[2]
Gene ontology Molecular function • dolichyl-phosphate beta-D-mannosyltransferase activity • GO:0001948 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 NP_714963 NP_714963.1	NP_081043
Location (UCSC)	Chr 1: 155.14 – 155.14 Mb	Chr 3: 89.26 – 89.27 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. 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.[5]

Clinical significance

Mutations in this gene are associated with congenital disorder of glycosylation type 1O.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000179085 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000042737 - 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 3".
6. 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.
7. Haeuptle MA, Hennet T (December 2009). "Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides" (PDF). 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.