DPM1

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DPM1
Identifiers
Aliases DPM1, CDGIE, MPDS, dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit
External IDs MGI: 1330239 HomoloGene: 2865 GeneCards: 8813
RNA expression pattern
PBB GE DPM1 202673 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003859
NM_001317034
NM_001317035
NM_001317036

NM_010072
NM_001310084

RefSeq (protein)

NP_003850.1
NP_001303963.1
NP_001303964.1
NP_001303965.1

NP_001297013.1
NP_034202.1

Location (UCSC) Chr 20: 50.93 – 50.96 Mb Chr 2: 168.21 – 168.23 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.[1][2][3]

Function[edit]

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. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2.[3]

Model organisms[edit]

Model organisms have been used in the study of DPM1 function. A conditional knockout mouse line called Dpm1tm1b(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[4] Male and female animals underwent a standardized phenotypic screen[5] to determine the effects of deletion.[6][7][8][9] Additional screens performed: - In-depth immunological phenotyping[10]

References[edit]

  1. ^ Colussi PA, Taron CH, Mack JC, Orlean P (Jul 1997). "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe". Proceedings of the National Academy of Sciences of the United States of America 94 (15): 7873–8. doi:10.1073/pnas.94.15.7873. PMC 21522. PMID 9223280. 
  2. ^ Tomita S, Inoue N, Maeda Y, Ohishi K, Takeda J, Kinoshita T (Apr 1998). "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells". The Journal of Biological Chemistry 273 (15): 9249–54. doi:10.1074/jbc.273.15.9249. PMID 9535917. 
  3. ^ a b "Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit". 
  4. ^ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  5. ^ a b "International Mouse Phenotyping Consortium". 
  6. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750. 
  7. ^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  8. ^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  9. ^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131. 
  10. ^ a b "Infection and Immunity Immunophenotyping (3i) Consortium". 

Further reading[edit]

External links[edit]