DPM

DPM is a three-letter initialism, and may refer to:

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DPM1

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 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. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2.

Model organisms

Model organisms have been used in the study of DPM1 function. A conditional knockout mouse line called Dpm1^{tm1b(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping

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DPM3

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.

References

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.