DHRS9

From Wikipedia, the free encyclopedia

Dehydrogenase/reductase (SDR family) member 9

Identifiers

DHRS9; 3alpha-HSD; RDH15; RDHL; RETSDR8

External IDs

Gene ontology
Molecular Function:	• alcohol dehydrogenase activity • retinol dehydrogenase activity • oxidoreductase activity • racemase and epimerase activity • 3-alpha(17-beta)-hydroxysteroid dehydrogenase (NAD+) activity
Cellular Component:	• microsome • membrane • integral to endoplasmic reticulum membrane
Biological Process:	• metabolic process • androgen metabolic process • epithelial cell differentiation • progesterone metabolic process • retinol metabolic process • 9-cis-retinoic acid biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005771 (mRNA)
NP_005762 (protein)

NM_175512 (mRNA)
NP_780721 (protein)

Location

Chr 2: 169.63 - 169.66 Mb

Chr 2: 69.18 - 69.2 Mb

Pubmed search

[1]

[2]

Dehydrogenase/reductase (SDR family) member 9, also known as DHRS9, is a human gene.^[1]

[edit] References

^ Entrez Gene: DHRS9 dehydrogenase/reductase (SDR family) member 9.

[edit] Further reading

Haeseleer F, Palczewski K (2000). "Short-chain dehydrogenases/reductases in retina.". Meth. Enzymol. 316: 372–83. PMID 10800688.
Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY (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.
Soref CM, Di YP, Hayden L, et al. (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.
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. 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. 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. 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. 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.