DPM3

DPM3
Identifiers
Aliases	DPM3, CDG1O, dolichyl-phosphate mannosyltransferase subunit 3, dolichyl-phosphate mannosyltransferase subunit 3, regulatory, MDDGB15, MDDGC15
External IDs	OMIM: 605951; MGI: 1915813; HomoloGene: 17810; GeneCards: DPM3; OMA:DPM3 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q22 Start 155,139,891 bp End 155,140,595 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F1 Start 89,166,665 bp End 89,174,386 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon anterior pituitary left adrenal cortex right adrenal gland right uterine tube right adrenal cortex monocyte body of pancreas canal of the cervix right lobe of liver Top expressed in intestinal villus blastocyst Ileal epithelium choroid plexus of fourth ventricle yolk sac lip right kidney esophagus lactiferous gland ventricular zone More reference expression data BioGPS n/a
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 NP_714963 NP_714963.1 NP_081043 Location (UCSC) Chr 1: 155.14 – 155.14 Mb Chr 3: 89.17 – 89.17 Mb PubMed search
Wikidata
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dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.

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.

Clinical significance

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

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. Bibcode:2002PNAS...9916899M. 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. S2CID 24726733.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. 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.