Retinol dehydrogenase 11 (RDH11)
The protein contains 318 amino acids for an estimated molecular weight of 35386 Da.
Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol (PubMed:12226107, PubMed:12036956, PubMed:29410696). Exhibits a low reductive activity towards unsaturated medium-chain aldehydes such as cis -6-nonenal and no activity toward nonanal or 4-hydroxy-nonenal (PubMed:15865448). Has no dehydrogenase activity towards steroid (PubMed:12226107, PubMed:12036956). (updated: Jan. 16, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Adaptation of rhodopsin mediated signaling
Cellular detoxification of aldehyde
Phototransduction, visible light
Retinal metabolic process
Retinoid metabolic process
Retinol metabolic process
Visual perception
The reference OMIM entry for this protein is 607849
Retinol dehydrogenase 11; rdh11
Prostate short-chain dehydrogenase/reductase 1; psdr1
Retinal reductase 1; ralr1
DESCRIPTION
RHD11, a member of the short-chain dehydrogenase/reductase (SDR) superfamily of oxidoreductases, is expressed at high levels in prostate epithelium, and its expression is regulated by androgens.CLONING
Using microarrays, Lin et al. (2001) found that RDH11, which they designated PSDR1, was upregulated by synthetic androgen in an androgen-sensitive prostate cancer cell line. By database analysis and screening of a prostate cDNA library, they cloned full-length RDH11. The deduced protein contains 318 amino acids, and the transcript contains 2 potential polyadenylation signals. RDH11 shares conserved motifs with the SDR family of oxidoreductases, including an N-terminal coenzyme-binding motif, which binds NAD(H) or NADP(H), and a C-terminal catalytic domain. RDH11 shares about 25% sequence identity with other SDR family members. Northern blot and RNA dot blot analyses detected a 2.5-kb transcript expressed at a high level in prostate and at low levels in other tissues, including spleen, thymus, testis, ovary, small intestine, colon, peripheral blood leukocytes, kidney, adrenal gland, and fetal liver. Testis expressed an additional transcript of about 0.9 kb. In situ hybridization of normal prostate detected RDH11 expression in basal and luminal epithelial cells, but not in fibromuscular stromal cells, endothelial cells, or infiltrating lymphocytes. Primary prostate adenocarcinoma cells were uniformly positive for RDH11 expression. Kedishvili et al. (2002) determined that RDH11, which they called RALR1, localized to the endoplasmic reticulum when transfected into COS-7 cells. Moore et al. (2002) cloned mouse Rdh11. The deduced 316-amino acid protein shares 85% identity with human RDH11. Northern blot analysis detected highest expression in testis and liver, where there were 2 Rdh11 isoforms. RNA dot blot analysis detected expression in all tissues examined, with highest expression in testis.GENE STRUCTURE
Lin et al. (2001) determined that the RDH11 gene contains 7 exons and spans about 18.9 kb. The promoter region contains a TATA box and putative androgen, progesterone, and interleukin-6 (IL6; 147620) response elements.MAPPING
By radiation hybrid analysis, Lin et al. (2001) mapped the RDH11 gene to chromosome 14q23-q24.3. Moore et al. (2002) mapped the mouse Rdh11 gene to chromosome 12 in a region that shows homology of synteny to human chromosome 14q23-q24.3. By genomic sequence analysis, Haeseleer et al. (2002) mapped the RDH11 and RDH12 (608830) genes within about 30 kb of each other.GENE FUNCTION
Kedishvili et al. (2002) characterized the substrate specificity of recombinant RDH11 expressed in sf9 insect cells. They determined that RDH11 had oxidoreductase activity toward retinoids but not steroids. It also showed a preference for NADP+ and NADPH versus NAD+ and NADH as cofactors. The enzyme was about 50-fold more efficient in the reduction of all-trans-retinal than in the oxidation of all-trans-retinol. RDH11 reduced all-trans-retinal in the presence of a 10-fold molar excess of cellular retinol-binding protein-1 (180260), which was believed to sequester all-trans-retinal from nonspecific enzymes.MOLECULAR GENETICS
In a family of Italian American descent in which 3 sibs had retinal dystrophy, juvenile cataracts, and short stature syndrome (RDJCSS; 616108), Xie et al. (2014) identified compound heterozygosity for nonsense mutations in the RDH11 gene (R67X, ... More on the omim web site
Jan. 21, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607849 was added.