Dolichol-phosphate mannosyltransferase subunit 3 (DPM3)

The protein contains 92 amino acids for an estimated molecular weight of 10094 Da.

 

Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  2. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  5. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 89%
Model score: 8

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VariantDescription
MDDGC15

The reference OMIM entry for this protein is 605951

Dolichyl-phosphate mannosyltransferase 3; dpm3
Dolichol-phosphate mannosyltransferase 3
Dolichol-phosphate-mannose synthase 3

DESCRIPTION

Dolichol-phosphate-mannose is a mannosyl donor important for the biosynthesis of various glycoconjugates (see DPM1; 603503).

CLONING

Using tagged DPM1 protein, Maeda et al. (2000) purified a protein complex with human DPM synthase activity. The complex contained DPM1, DPM2 (603564), and a novel protein, DPM3. Using peptide sequencing and database searches, the authors identified a cDNA encoding DPM3. The predicted 92-amino acid DPM3 protein contains 2 putative N-terminal transmembrane domains and a hydrophilic C-terminal portion. It shares 25%, 31%, and 97% amino acid identity with the C. elegans, S. pombe, and rat Dpm3 proteins, respectively. By fractionation of transfected cells, Maeda et al. (2000) determined that DPM3 is a membrane protein in the endoplasmic reticulum (ER). Using DPM2 mutant cells, they demonstrated that the ER localization of DPM3 is independent of DPM2.

GENE FUNCTION

Using coprecipitation experiments with full-length and truncated DPM3, Maeda et al. (2000) found that DPM2 associates with the N-terminal region of DPM3 and that DPM1 associates with the C-terminal domain of DPM3. DPM1 expression increased following transient overexpression of DPM3 in the absence of DPM2, suggesting that DPM3 directly stabilizes DPM1. Using cotransfection experiments, Maeda et al. (2000) showed that the stability of DPM3 is dependent upon DPM2.

MAPPING

Maeda et al. (2000) identified an STS within the DPM3 gene that maps to 1q12-q21.

MOLECULAR GENETICS

In a Greek female patient with congenital disorder of glycosylation type Io (CDH1O; 612937), Lefeber et al. (2009) identified a homozygous mutation in the DPM3 gene (L85S; 605951.0001). She had mild myopathic features and cardiomyopathy. Biochemical studies showed defective O-mannosylation. ... More on the omim web site

Subscribe to this protein entry history

Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.

Feb. 23, 2019: Protein entry updated
Automatic update: model status changed

Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 605951 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).