Summary: Progesterone receptor
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Progesterone receptor Edit Wikipedia article
PDB rendering based on 1a28.
|Symbols||; NR3C3; PR|
|External IDs||IUPHAR: ChEMBL: GeneCards:|
|RNA expression pattern|
Progesterone is necessary to induce the progesterone receptors. When no binding hormone is present the carboxyl terminal inhibits transcription. Binding to a hormone induces a structural change that removes the inhibitory action. Progesterone antagonists prevent the structural reconfiguration.
After progesterone binds to the receptor, restructuring with dimerization follows and the complex enters the nucleus and binds to DNA. There transcription takes place, resulting in formation of messenger RNA that is translated by ribosomes to produce specific proteins.
|Progesterone receptor, N-terminal|
In common with other steroid receptors, the progesterone receptor has a N-terminal regulatory domain, a DNA binding domain, a hinge section, and a C-terminal ligand binding domain. A special transcription activation function (TAF), called TAF-3, is present in the progesterone receptor-B, in a B-upstream segment (BUS) at the amino acid terminal. This segment is not present in the receptor-A.
As demonstrated in progesterone receptor-deficient mice, the physiological effects of progesterone depend completely on the presence of the human progesterone receptor (hPR), a member of the steroid-receptor superfamily of nuclear receptors. The single-copy human (hPR) gene uses separate promoters and translational start sites to produce two isoforms, hPR-A and -B, which are identical except for an additional 165 amino acids present only in the N terminus of hPR-B. Although hPR-B shares many important structural domains as hPR-A, they are in fact two functionally distinct transcription factors, mediating their own response genes and physiological effects with little overlap. Selective ablation of PR-A in a mouse model, resulting in exclusive production of PR-B, unexpectedly revealed that PR-B contributes to, rather than inhibits, epithelial cell proliferation both in response to estrogen alone and in the presence of progesterone and estrogen. These results suggest that in the uterus, the PR-A isoform is necessary to oppose estrogen-induced proliferation as well as PR-B-dependent proliferation.
Six variable sites, including four polymorphisms and five common haplotypes have been identified in the human PR gene . One promoter region polymorphism, +331G/A, creates a unique transcription start site. Biochemical assays showed that the +331G/A polymorphism increases transcription of the PR gene, favoring production of hPR-B in an Ishikawa endometrial cancer cell line.
Several studies have now shown no association between progesterone receptor gene +331G/A polymorphisms and breast or endometrial cancers. However, these follow-up studies lacked the sample size and statistical power to make any definitive conclusions, due to the rarity of the +331A SNP. It is currently unknown which if any polymorphisms in this receptor is of significance to cancer.
Knockout mice of the PR have been found to have severely impaired lobuloalveolar development of the mammary glands as well as delayed but otherwise normal mammary ductal development at puberty.
Progesterone receptor antagonists work as antiprogestins. The main example is mifepristone. Selective progesterone receptor modulators may also have more or less antagonist activity. Additional PR antagonists include: onapristone (ZK98299), lonaprisan (ZK230211, BAY86-5044), APR19, EC304, WAY-255348, ORG31710, asoprisnil (J867), telapristone (Proellex, CDB-4124), and CDB-2914 (ulipristal acetates).
Progesterone receptor has been shown to interact with:
- Misrahi M, Atger M, d'Auriol L, Loosfelt H, Meriel C, Fridlansky F, Guiochon-Mantel A, Galibert F, Milgrom E (March 1987). "Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA". Biochem. Biophys. Res. Commun. 143 (2): 740–8. doi:10.1016/0006-291X(87)91416-1. PMID 3551956.
- Law ML, Kao FT, Wei Q, Hartz JA, Greene GL, Zarucki-Schulz T, Conneely OM, Jones C, Puck TT, O'Malley BW (May 1987). "The progesterone receptor gene maps to human chromosome band 11q13, the site of the mammary oncogene int-2". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2877–81. doi:10.1073/pnas.84.9.2877. PMC 304763. PMID 3472240.
- ensembl.org, Gene: ESR1 (ENSG00000091831)
- Gadkar-Sable S, Shah C, Rosario G, Sachdeva G, Puri C (2005). "Progesterone receptors: various forms and functions in reproductive tissues". Front. Biosci. 10: 2118–30. doi:10.2741/1685. PMID 15970482.
- Kase, Nathan G.; Speroff, Leon; Glass, Robert L. (1999). Clinical gynecologic endocrinology and infertility. Hagerstown, MD: Lippincott Williams & Wilkins. ISBN 0-683-30379-1.
- Fritz, Marc A.; Speroff, Leon (2005). Clinical gynecologic endocrinology and infertility. Hagerstown, MD: Lippincott Williams & Wilkins. ISBN 0-7817-4795-3.
- Kastner P, Krust A, Turcotte B, Stropp U, Tora L, Gronemeyer H, Chambon P (1990). "Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B". EMBO J. 9 (5): 1603–14. PMC 551856. PMID 2328727.
- Terry KL, De Vivo I, Titus-Ernstoff L, Sluss PM, Cramer DW (March 2005). "Genetic variation in the progesterone receptor gene and ovarian cancer risk". Am. J. Epidemiol. 161 (5): 442–51. doi:10.1093/aje/kwi064. PMC 1380205. PMID 15718480.
- De Vivo I, Huggins GS, Hankinson SE, Lescault PJ, Boezen M, Colditz GA, Hunter DJ (September 2002). "A functional polymorphism in the promoter of the progesterone receptor gene associated with endometrial cancer risk". Proc. Natl. Acad. Sci. U.S.A. 99 (19): 12263–8. doi:10.1073/pnas.192172299. PMC 129433. PMID 12218173.
- Feigelson HS, Rodriguez C, Jacobs EJ, Diver WR, Thun MJ, Calle EE (2004). "No association between the progesterone receptor gene +331G/A polymorphism and breast cancer". Cancer Epidemiol. Biomarkers Prev. 13 (6): 1084–5. PMID 15184270.
- Dossus L, Canzian F, Kaaks R, Boumertit A, Weiderpass E (2006). "No association between progesterone receptor gene +331G/A polymorphism and endometrial cancer". Cancer Epidemiol. Biomarkers Prev. 15 (7): 1415–6. doi:10.1158/1055-9965.EPI-06-0215. PMID 16835347.
- Macias H, Hinck L (2012). "Mammary gland development". Wiley Interdiscip Rev Dev Biol 1 (4): 533–57. doi:10.1002/wdev.35. PMC 3404495. PMID 22844349.
- Hilton, Heidi N; Graham, J Dinny; Clarke, Christine L (2015). "Progesterone regulation of proliferation in the normal human breast and in breast cancer: a tale of two scenarios?". Molecular Endocrinology: me.2015–1152. doi:10.1210/me.2015-1152. ISSN 0888-8809.
- Aupperlee MD, Leipprandt JR, Bennett JM, Schwartz RC, Haslam SZ (2013). "Amphiregulin mediates progesterone-induced mammary ductal development during puberty". Breast Cancer Res. 15 (3): R44. doi:10.1186/bcr3431. PMC 3738150. PMID 23705924.
- Knutson TP, Lange CA (2014). "Tracking progesterone receptor-mediated actions in breast cancer". Pharmacol. Ther. 142 (1): 114–25. doi:10.1016/j.pharmthera.2013.11.010. PMID 24291072.
- Zhang XL, Zhang D, Michel FJ, Blum JL, Simmen FA, Simmen RC (June 2003). "Selective interactions of Kruppel-like factor 9/basic transcription element-binding protein with progesterone receptor isoforms A and B determine transcriptional activity of progesterone-responsive genes in endometrial epithelial cells". J. Biol. Chem. 278 (24): 21474–82. doi:10.1074/jbc.M212098200. PMID 12672823.
- Giangrande PH, Kimbrel EA, Edwards DP, McDonnell DP (May 2000). "The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding". Mol. Cell. Biol. 20 (9): 3102–15. doi:10.1128/MCB.20.9.3102-3115.2000. PMC 85605. PMID 10757795.
- Nawaz Z, Lonard DM, Smith CL, Lev-Lehman E, Tsai SY, Tsai MJ, O'Malley BW (February 1999). "The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily". Mol. Cell. Biol. 19 (2): 1182–9. PMC 116047. PMID 9891052.
- Butnor KJ, Burchette JL, Robboy SJ (2002). "Progesterone receptor activity in leiomyomatosis peritonealis disseminata". Int. J. Gynecol. Pathol. 18 (3): 259–64. doi:10.1097/00004347-199907000-00012. PMID 12090595.
- Leonhardt SA, Boonyaratanakornkit V, Edwards DP (2004). "Progesterone receptor transcription and non-transcription signaling mechanisms". Steroids 68 (10–13): 761–70. doi:10.1016/S0039-128X(03)00129-6. PMID 14667966.
- Conneely OM, Mulac-Jericevic B, Lydon JP (2004). "Progesterone-dependent regulation of female reproductive activity by two distinct progesterone receptor isoforms". Steroids 68 (10–13): 771–8. doi:10.1016/S0039-128X(03)00126-0. PMID 14667967.
- Bagchi MK, Tsai SY, Tsai MJ, O'Malley BW (1992). "Ligand and DNA-dependent phosphorylation of human progesterone receptor in vitro". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 2664–8. doi:10.1073/pnas.89.7.2664. PMC 48722. PMID 1557371.
- Kastner P, Krust A, Turcotte B, et al. (1990). "Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B". EMBO J. 9 (5): 1603–14. PMC 551856. PMID 2328727.
- Guiochon-Mantel A, Loosfelt H, Lescop P, et al. (1989). "Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers". Cell 57 (7): 1147–54. doi:10.1016/0092-8674(89)90052-4. PMID 2736623.
- Fernandez MD, Carter GD, Palmer TN (1983). "The interaction of canrenone with oestrogen and progesterone receptors in human uterine cytosol". British Journal of Clinical Pharmacology 15 (1): 95–101. doi:10.1111/j.1365-2125.1983.tb01470.x. PMC 1427833. PMID 6849751.
- Oñate SA, Tsai SY, Tsai MJ, O'Malley BW (1995). "Sequence and characterization of a coactivator for the steroid hormone receptor superfamily". Science 270 (5240): 1354–7. doi:10.1126/science.270.5240.1354. PMID 7481822.
- Zhang Y, Beck CA, Poletti A, et al. (1995). "Identification of phosphorylation sites unique to the B form of human progesterone receptor. In vitro phosphorylation by casein kinase II". J. Biol. Chem. 269 (49): 31034–40. PMID 7983041.
- Mansour I, Reznikoff-Etievant MF, Netter A (1995). "No evidence for the expression of the progesterone receptor on peripheral blood lymphocytes during pregnancy". Hum. Reprod. 9 (8): 1546–9. PMID 7989520.
- Kalkhoven E, Wissink S, van der Saag PT, van der Burg B (1996). "Negative interaction between the RelA(p65) subunit of NF-kappaB and the progesterone receptor". J. Biol. Chem. 271 (11): 6217–24. doi:10.1074/jbc.271.11.6217. PMID 8626413.
- Wang JD, Zhu JB, Fu Y, et al. (1996). "Progesterone receptor immunoreactivity at the maternofetal interface of first trimester pregnancy: a study of the trophoblast population". Hum. Reprod. 11 (2): 413–9. doi:10.1093/humrep/11.2.413. PMID 8671234.
- Thénot S, Henriquet C, Rochefort H, Cavaillès V (1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. doi:10.1074/jbc.272.18.12062. PMID 9115274.
- Jenster G, Spencer TE, Burcin MM, et al. (1997). "Steroid receptor induction of gene transcription: a two-step model". Proc. Natl. Acad. Sci. U.S.A. 94 (15): 7879–84. doi:10.1073/pnas.94.15.7879. PMC 21523. PMID 9223281.
- Shanker YG, Sharma SC, Rao AJ (1997). "Expression of progesterone receptor mRNA in the first trimester human placenta". Biochem. Mol. Biol. Int. 42 (6): 1235–40. PMID 9305541.
- Richer JK, Lange CA, Wierman AM, et al. (1998). "Progesterone receptor variants found in breast cells repress transcription by wild-type receptors". Breast Cancer Res. Treat. 48 (3): 231–41. doi:10.1023/A:1005941117247. PMID 9598870.
- Williams SP, Sigler PB (1998). "Atomic structure of progesterone complexed with its receptor". Nature 393 (6683): 392–6. doi:10.1038/30775. PMID 9620806.
- Boonyaratanakornkit V, Melvin V, Prendergast P, et al. (1998). "High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells". Mol. Cell. Biol. 18 (8): 4471–87. PMC 109033. PMID 9671457.
- Nawaz Z, Lonard DM, Smith CL, et al. (1999). "The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily". Mol. Cell. Biol. 19 (2): 1182–9. PMC 116047. PMID 9891052.
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000128
Steroid or nuclear hormone receptors (NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members of the superfamily include the steroid hormone receptors and receptors for thyroid hormone, retinoids, 1,25-dihydroxy-vitamin D3 and a variety of other ligands. The proteins function as dimeric molecules in nuclei to regulate the transcription of target genes in a ligand-responsive manner [PUBMED:7899080, PUBMED:8165128]. In addition to C-terminal ligand-binding domains, these nuclear receptors contain a highly-conserved, N-terminal zinc-finger that mediates specific binding to target DNA sequences, termed ligand-responsive elements. In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity.
NRs are extremely important in medical research, a large number of them being implicated in diseases such as cancer, diabetes, hormone resistance syndromes, etc. While several NRs act as ligand-inducible transcription factors, many do not yet have a defined ligand and are accordingly termed "orphan" receptors. During the last decade, more than 300 NRs have been described, many of which are orphans, which cannot easily be named due to current nomenclature has recently been introduced in an attempt to rationalise the increasingly complex set of names used to describe superfamily members.
The progesterone receptor consists of 3 functional and structural domains: an N-terminal (modulatory) domain; a DNA binding domain that mediates specific binding to target DNA sequences (ligand-responsive elements); and a hormone binding domain. The N-terminal domain is unique to the progesterone receptors and spans approximately the first 500 residues; the highly-conserved DNA-binding domain is smaller (around 65 residues) and occupies the central portion of the protein; and the hormone binding domain lies at the receptor C terminus.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||nucleus (GO:0005634)|
|Molecular function||steroid hormone receptor activity (GO:0003707)|
|DNA binding (GO:0003677)|
|steroid binding (GO:0005496)|
|Biological process||regulation of transcription, DNA-templated (GO:0006355)|
|steroid hormone mediated signaling pathway (GO:0043401)|
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Author:||Mian N, Bateman A|
|Number in seed:||9|
|Number in full:||63|
|Average length of the domain:||396.70 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||58.21 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
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How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Prog_receptor domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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