Estradiol 17-beta-dehydrogenase 11 (HSD17B11)
The protein contains 300 amino acids for an estimated molecular weight of 32936 Da.
Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell lymphoma. (updated: April 1, 2015)
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.
- 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.
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.
This protein is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Androgen catabolic process
Estrogen biosynthetic process
Steroid biosynthetic process
The reference OMIM entry for this protein is 612831
17-@beta-hydroxysteroid dehydrogenase xi; hsd17b11
17-@beta-hsdxi
Retsdr2
Pan1b
DESCRIPTION
Short-chain alcohol dehydrogenases, such as HSD17B11, metabolize secondary alcohols and ketones (Brereton et al., 2001).CLONING
By searching EST databases for sequences similar to 11-beta-HSD1 (HSD11B1; 600713), followed by screening a lung cDNA library, Li et al. (1998) cloned HSD17B11, which they called PAN1B. Northern blot analysis detected high expression of a 1.9-kb transcript in liver, lung, small intestine, adrenal cortex, medulla, and adrenal carcinoma. Lower expression was detected in kidney, heart, placenta, stomach, thymus, testis, thyroid, and pancreas. By searching EST databases for short-chain dehydrogenases/reductases (SDRs), followed by 3-prime and 5-prime RACE and nested PCR of a human retina cDNA library, Haeseleer and Palczewski (2000) cloned HSD17B11, which they called RETSDR2. The deduced 300-amino acid protein has a calculated molecular mass of 33.0 kD. It has all the characteristics of SDRs, including a cofactor-binding Rossman-fold domain and highly conserved motifs in the nucleotide-binding site and active site. Northern blot analysis detected HSD17B11 expression in all tissues examined. By immunohistochemical analysis, Brereton et al. (2001) detected PAN1B in ciliated epithelium and acini of adult human trachea and in bronchioles, but not in alveoli. Similar staining was detected in human fetus, with stronger staining in the second half of pregnancy. In the eye, PAN1B was detected in nonpigmented epithelium of the ciliary body, with lower expression in the inner nuclear layer of the retina. Expression was also detected in normal adrenal cortex, granulosa cells, paraluteal cells, Leydig cells, and syncytiotrophoblasts. Chai et al. (2003) cloned 17-beta-HSDXI from a pregnant human uterus cDNA library. The deduced 300-amino acid protein has a potential N-glycosylation site at residue 228. The 5-prime UTR of the cDNA has a polymorphic adenosine repeat. Northern blot analysis detected high 17-beta-HSDXI expression in pancreas, kidney, liver, lung, adrenal gland, ovary, and heart. Immunohistochemical analysis showed strong expression in steroidogenic cells, such as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa cells of the dominant follicle and corpus luteum. Expression in fetal adrenal gland increased after birth.GENE FUNCTION
By assaying transfected CHOP Chinese hamster ovary cells, Li et al. (1998) showed that PAN1B converted estradiol to estrone. It did not use other steroid substrates tested, including glucocorticoids. Using several 17-keto- and 17-beta-hydroxysteroids as substrates, Brereton et al. (2001) showed that CHOP cells expressing PAN1B converted the androgen metabolite 3-alpha-diol (5-alpha-androstane-3-alpha,17-beta-diol) to androsterone in a nonsaturable reaction. Several retinoids inhibited 3-alpha-diol metabolism more than 90%, but PAN1B did not metabolize these retinoids. Chai et al. (2003) found that cAMP downregulated 17-beta-Hsdxi enzymatic activity in a mouse adrenocortical cell line and reduced 17-beta-Hsdxi message to undetectable levels. All-trans-retinoic acid (RA) did not affect 17-beta-Hsdxi expression or activity, but addition of RA together with cAMP significantly decreased activity over cAMP alone.GENE STRUCTURE
Chai et al. (2003) found that the 5-prime flanking region of the HSD17B11 gene contains a CpG island. They also identified a potential nuclear receptor steroidogenic factor-1 (SF1, or NR5A1; 184757 ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 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 612831 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed