DHRS9

Dehydrogenase/reductase SDR family member 9 is an enzyme that in humans is encoded by the DHRS9 gene.[4][5][6][7]

DHRS9
Identifiers
Aliases	DHRS9, 3-alpha-HSD, 3ALPHA-HSD, RDH-E2, RDH-TBE, RDH15, RDHL, RDHTBE, RETSDR8, SDR9C4, dehydrogenase/reductase (SDR family) member 9, dehydrogenase/reductase 9
External IDs	OMIM: 612131 MGI: 2442798 HomoloGene: 26079 GeneCards: DHRS9
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q31.1 Start 169,064,789 bp[1] End 169,096,167 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • oxidoreductase activity • testosterone dehydrogenase (NAD+) activity • alcohol dehydrogenase (NAD) activity • racemase and epimerase activity • retinol dehydrogenase activity • androsterone dehydrogenase activity • androstan-3-alpha,17-beta-diol dehydrogenase activity Cellular component • intracellular membrane-bounded organelle • organelle membrane • integral component of endoplasmic reticulum membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane Biological process • retinoic acid biosynthetic process • retinol metabolic process • 9-cis-retinoic acid biosynthetic process • epithelial cell differentiation • oxidation-reduction process • androgen metabolic process • progesterone metabolic process • lipid metabolism • steroid metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10170	241452
Ensembl	ENSG00000073737	n/a
UniProt	Q9BPW9	Q58NB6
RefSeq (mRNA)	NM_001142270 NM_001142271 NM_001289763 NM_005771 NM_199204 NM_001376924	NM_175512
RefSeq (protein)	NP_001135742 NP_001135743 NP_001276692 NP_954674 NP_001363853	NP_780721
Location (UCSC)	Chr 2: 169.06 – 169.1 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000073737 - 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. Soref CM, Di YP, Hayden L, Zhao YH, Satre MA, Wu R (Jun 2001). "Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol". J Biol Chem. 276 (26): 24194–202. doi:10.1074/jbc.M100332200. PMID 11304534.
5. Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY (Jun 2001). "Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties". J Biol Chem. 276 (25): 22278–86. doi:10.1074/jbc.M102076200. PMID 11294878.
6. Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1–3): 94–8. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
7. "Entrez Gene: DHRS9 dehydrogenase/reductase (SDR family) member 9".

Further reading

• Haeseleer F, Palczewski K (2000). Short-chain dehydrogenases/reductases in retina. Meth. Enzymol. Methods in Enzymology. 316. pp. 372–83. doi:10.1016/S0076-6879(00)16736-9. ISBN 9780121822170. PMID 10800688.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Markova NG, Pinkas-Sarafova A, Karaman-Jurukovska N, et al. (2003). "Expression pattern and biochemical characteristics of a major epidermal retinol dehydrogenase". Mol. Genet. Metab. 78 (2): 119–35. doi:10.1016/S1096-7192(02)00226-3. PMID 12618084.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Jette C, Peterson PW, Sandoval IT, et al. (2004). "The tumor suppressor adenomatous polyposis coli and caudal related homeodomain protein regulate expression of retinol dehydrogenase L." J. Biol. Chem. 279 (33): 34397–405. doi:10.1074/jbc.M314021200. PMID 15190067.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Jones RJ, Dickerson S, Bhende PM, et al. (2007). "Epstein-Barr virus lytic infection induces retinoic acid-responsive genes through induction of a retinol-metabolizing enzyme, DHRS9". J. Biol. Chem. 282 (11): 8317–24. doi:10.1074/jbc.M608667200. PMID 17244623.
• Riquelme P, Amodio G, Macedo C, Moreau A, Obermajer N, Brochhausen C, Ahrens N, Kekarainen T, Faendrich F, Cuturi C, Gregori S, Metes D, Schlitt HJ, Thomson AW, Geissler EK, Hutchinson JA (2017). "DHRS9 Is a Stable Marker of Human Regulatory Macrophages". Transplantation. 101 (11): 2731–38. doi:10.1097/TP.0000000000001814. PMC 6319563. PMID 28594751.

External links

• DHRS9 human gene location in the UCSC Genome Browser.
• DHRS9 human gene details in the UCSC Genome Browser.