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Identification
HMDB Protein ID HMDBP00384
Secondary Accession Numbers
  • 5621
Name Dolichol-phosphate mannosyltransferase
Synonyms
  1. DPM synthase
  2. Dolichol-phosphate mannose synthase
  3. Dolichyl-phosphate beta-D-mannosyltransferase
  4. MPD synthase
  5. Mannose-P-dolichol synthase
Gene Name DPM1
Protein Type Enzyme
Biological Properties
General Function Cell wall/membrane/envelope biogenesis
Specific Function Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Pathways
  • N-Glycan biosynthesis
  • protein glycosylation
Reactions
Guanosine diphosphate mannose + Dolichol-20 → Guanosine diphosphate + Dolichyl beta-D-mannosyl phosphate details
Guanosine diphosphate mannose + Dolichol-20 → Guanosine diphosphate + Dolichyl phosphate D-mannose details
GO Classification
Biological Process
GPI anchor biosynthetic process
dolichol-linked oligosaccharide biosynthetic process
protein N-linked glycosylation via asparagine
C-terminal protein lipidation
dolichol metabolic process
GDP-mannose metabolic process
protein O-linked mannosylation
Cellular Component
endoplasmic reticulum membrane
dolichol-phosphate-mannose synthase complex
Molecular Function
alcohol binding
dolichyl-phosphate beta-D-mannosyltransferase activity
dolichyl-phosphate-mannose-protein mannosyltransferase activity
mannose binding
Cellular Location
  1. Endoplasmic reticulum
Gene Properties
Chromosome Location 20
Locus 20q13.13
SNPs DPM1
Gene Sequence
>783 bp
ATGGCCTCCTTGGAAGTCAGTCGTAGTCCTCGCAGGTCTCGGCGGGAGCTGGAAGTGCGC
AGTCCACGACAGAACAAATATTCGGTGCTTTTACCTACCTACAACGAGCGCGAGAACCTG
CCGCTCATCGTGTGGCTGCTGGTGAAAAGCTTCTCCGAGAGTGGAATCAACTATGAAATT
ATAATCATAGATGATGGAAGCCCAGATGGAACAAGGGATGTTGCTGAACAGTTGGAGAAG
ATCTATGGGTCAGACAGAATTCTTCTAAGACCACGAGAGAAAAAGTTGGGACTAGGAACT
GCATATATTCATGGAATGAAACATGCCACAGGAAACTACATCATTATTATGGATGCTGAT
CTCTCACACCATCCAAAATTTATTCCTGAATTTATTAGGAAGCAAAAGGAGGGTAATTTT
GATATTGTCTCTGGAACTCGCTACAAAGGAAATGGAGGTGTATATGGCTGGGATTTGAAA
AGAAAAATAATCAGCCGTGGGGCCAATTTTTTAACTCAGATCTTGCTGAGACCAGGAGCA
TCTGATTTAACAGGAAGTTTCAGATTATACCGAAAAGAAGTTCTAGAGAAATTAATAGAA
AAATGTGTTTCTAAAGGCTACGTCTTCCAGATGGAGATGATTGTTCGGGCAAGACAGTTG
AATTATACTATTGGCGAGGTTCCAATATCATTTGTGGATCGTGTTTATGGTGAATCCAAG
TTGGGAGGAAATGAAATAGTATCTTTCTTGAAAGGATTATTGACTCTTTTTGCTACTACA
TAA
Protein Properties
Number of Residues 260
Molecular Weight 29633.995
Theoretical pI 9.563
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dolichol-phosphate mannosyltransferase
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEI
IIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDAD
LSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGA
SDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESK
LGGNEIVSFLKGLLTLFATT
GenBank ID Protein 4503363
UniProtKB/Swiss-Prot ID O60762
UniProtKB/Swiss-Prot Entry Name DPM1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_003859.1
GeneCard ID DPM1
GenAtlas ID DPM1
HGNC ID HGNC:3005
References
General References
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  10. Colussi PA, Taron CH, Mack JC, Orlean P: 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. 1997 Jul 22;94(15):7873-8. [PubMed:9223280 ]
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