DPM1

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Dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit
Identifiers
Symbols DPM1 ; CDGIE; MPDS
External IDs OMIM603503 MGI1330239 HomoloGene2865 ChEMBL: 2572 GeneCards: DPM1 Gene
EC number 2.4.1.83
RNA expression pattern
PBB GE DPM1 202673 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8813 13480
Ensembl ENSG00000000419 ENSMUSG00000078919
UniProt O60762 O70152
RefSeq (mRNA) NM_003859 NM_010072
RefSeq (protein) NP_003850 NP_034202
Location (UCSC) Chr 20:
49.55 – 49.58 Mb
Chr 2:
168.18 – 168.23 Mb
PubMed search [1] [2]

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

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]

References[edit]

  1. ^ Colussi PA, Taron CH, Mack JC, Orlean P (Aug 1997). "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe". Proc Natl Acad Sci U S A 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 (May 1998). "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells". J Biol Chem 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". 

Further reading[edit]

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