DHRSX

DHRSX
Identifiers
Aliases	DHRSX , CXorf11, DHRS5X, DHRS5Y, DHRSXY, DHRSY, SDR46C1, SDR7C6, dehydrogenase/reductase (SDR family) X-linked, dehydrogenase/reductase X-linked
External IDs	MGI: 2181510; HomoloGene: 78041; GeneCards: DHRSX; OMA:DHRSX - orthologs
Gene location (Human) Chr. X chromosome (human) [1] Band Xp22.33 and Yp11.2 Start 2,219,506 bp [1] End 2,502,805 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium ventricular zone ganglionic eminence body of pancreas apex of heart right atrium right auricle right lobe of liver gastrocnemius muscle left ventricle n/a More reference expression data BioGPS n/a
Gene ontology Molecular function oxidoreductase activity Cellular component extracellular region Biological process positive regulation of autophagy Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 207063 236082 Ensembl ENSG00000169084 ENSMUSG00000063897 UniProt Q8N5I4 Q8VBZ0 RefSeq (mRNA) NM_145177 NM_001033326 RefSeq (protein) NP_660160 n/a Location (UCSC) Chr X: 2.22 – 2.5 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Dehydrogenase/reductase (SDR family) X-linked also known as DHRSX is an enzyme which in humans is encoded by the pseudoautosomal DHRSX gene. ^[4] DHRSX is a member of the short-chain dehydrogenase family of oxidoreductase enzymes. ^[5]

DHRSX is required for two steps in the biosynthesis of dolichol: i) the NAD⁺-dependent conversion of polyprenol to its aldehyde analogue, polyprenal; ii) the NADPH-dependent reduction of dolichal to dolichol. ^[6] Dolichol is a long polyisoprenoid lipid required as the carrier of mono- and oligosaccharides in the processes of N-glycosylation, C-/O-mannosylation and the formation of glycosylphosphatidylinositol (GPI) anchors.

References

1. GRCh38: Ensembl release 89: ENSG00000169084 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Gianfrancesco F, Sanges R, Esposito T, Tempesta S, Rao E, Rappold G, et al. (December 2001). "Differential divergence of three human pseudoautosomal genes and their mouse homologs: implications for sex chromosome evolution". Genome Research. 11 (12): 2095–2100. doi:10.1101/gr.197001. PMC   311231 . PMID   11731500.
5. Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, et al. (March 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1–3): 94–98. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC   2896744 . PMID   19027726.
6. Wilson MP, Kentache T, Althoff CR, Schulz C, de Bettignies G, Mateu Cabrera G, et al. (July 2024). "A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis". Cell. 187 (14): 3585–3601.e22. doi:10.1016/j.cell.2024.04.041. PMC   11250103 . PMID   38821050.

Further reading

• Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, et al. (December 2005). "Transcriptome analysis of human gastric cancer". Mammalian Genome. 16 (12): 942–954. doi:10.1007/s00335-005-0075-2. PMID   16341674. S2CID   69278.
• Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, et al. (October 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Research. 13 (10): 2265–2270. doi:10.1101/gr.1293003. PMC   403697 . PMID   12975309.
• Barbe L, Lundberg E, Oksvold P, Stenius A, Lewin E, Björling E, et al. (March 2008). "Toward a confocal subcellular atlas of the human proteome". Molecular & Cellular Proteomics. 7 (3): 499–508. doi: 10.1074/mcp.M700325-MCP200 . PMID   18029348.