ID MCR_HUMAN Reviewed; 984 AA. AC P08235; B0ZBF5; B0ZBF7; Q2NKL1; Q96KQ8; Q96KQ9; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 2. DT 27-MAR-2024, entry version 243. DE RecName: Full=Mineralocorticoid receptor; DE Short=MR; DE AltName: Full=Nuclear receptor subfamily 3 group C member 2; GN Name=NR3C2; Synonyms=MCR, MLR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS ILE-180 AND RP ALA-241. RC TISSUE=Kidney; RX PubMed=3037703; DOI=10.1126/science.3037703; RA Arriza J.L., Weinberger C., Cerelli G., Glaser T.M., Handelin B.L., RA Housman D.E., Evans R.M.; RT "Cloning of human mineralocorticoid receptor complementary DNA: structural RT and functional kinship with the glucocorticoid receptor."; RL Science 237:268-275(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), TISSUE SPECIFICITY, RP INTERACTION WITH NCOA1; TIF1 AND NRIP1, AND VARIANTS ILE-180 AND ALA-241. RC TISSUE=Heart; RX PubMed=11518808; DOI=10.1210/mend.15.9.0689; RA Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.; RT "A new human MR splice variant is a ligand-independent transactivator RT modulating corticosteroid action."; RL Mol. Endocrinol. 15:1586-1598(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ILE-180. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 545-984, AND DISEASE. RX PubMed=9662404; DOI=10.1038/966; RA Geller D.S., Rodriguez-Soriano J., Vallo Boado A., Schifter S., Bayer M., RA Chang S.S., Lifton R.P.; RT "Mutations in the mineralocorticoid receptor gene cause autosomal dominant RT pseudohypoaldosteronism type I."; RL Nat. Genet. 19:279-281(1998). RN [7] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=1655735; DOI=10.1016/s0021-9258(18)55238-8; RA Alnemri E.S., Maksymowych A.B., Robertson N.M., Litwack G.; RT "Overexpression and characterization of the human mineralocorticoid RT receptor."; RL J. Biol. Chem. 266:18072-18081(1991). RN [8] RP DEFINITION OF DIFFERENT FORMS OF PSEUDOHYPOALDOSTERONISM TYPE 1. RX PubMed=1939532; DOI=10.1210/jcem-73-5-936; RA Hanukoglu A.; RT "Type I pseudohypoaldosteronism includes two clinically and genetically RT distinct entities with either renal or multiple target organ defects."; RL J. Clin. Endocrinol. Metab. 73:936-944(1991). RN [9] RP IDENTIFICATION (ISOFORM 3). RC TISSUE=Leukocyte; RX PubMed=7495694; DOI=10.1016/0960-0760(95)00162-s; RA Bloem L.J., Guo C., Pratt J.H.; RT "Identification of a splice variant of the rat and human mineralocorticoid RT receptor genes."; RL J. Steroid Biochem. Mol. Biol. 55:159-162(1995). RN [10] RP TISSUE SPECIFICITY. RX PubMed=9141514; DOI=10.1210/jcem.82.5.3933; RA Zennaro M.-C., Farman N., Bonvalet J.-P., Lombes M.; RT "Tissue-specific expression of alpha and beta messenger ribonucleic acid RT isoforms of the human mineralocorticoid receptor in normal and pathological RT states."; RL J. Clin. Endocrinol. Metab. 82:1345-1352(1997). RN [11] RP TERNARY COMPLEX WITH HSP90; HSP70 AND FKBP4, AND DISSOCIATION UPON RP ALDOSTERONE BINDING. RX PubMed=9392437; RA Bruner K.L., Derfoul A., Robertson N.M., Guerriero G., RA Fernandes-Alnemri T., Alnemri E.S., Litwack G.; RT "The unliganded mineralocorticoid receptor is associated with heat shock RT proteins 70 and 90 and the immunophilin FKBP-52."; RL Recept. Signal Transduct. 7:85-98(1997). RN [12] RP MUTAGENESIS OF CYS-808; CYS-849 AND CYS-942. RX PubMed=9724527; DOI=10.1021/bi980593e; RA Lupo B., Mesnier D., Auzou G.; RT "Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for RT steroid binding."; RL Biochemistry 37:12153-12159(1998). RN [13] RP MUTAGENESIS OF ASN-770; GLN-776; ARG-817 AND THR-945. RX PubMed=10760050; DOI=10.1046/j.1523-1755.2000.00958.x; RA Hellal-Levy C., Fagart J., Souque A., Rafestin-Oblin M.-E.; RT "Mechanistic aspects of mineralocorticoid receptor activation."; RL Kidney Int. 57:1250-1255(2000). RN [14] RP INTERACTION WITH NCOA1; TIF1 AND NRIP1, AND MUTAGENESIS OF LEU-952; RP LYS-953; VAL-954; PHE-956 AND PRO-957. RX PubMed=10935545; DOI=10.1210/mend.14.8.0502; RA Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D., RA Rafestin-Oblin M.-E.; RT "Crucial role of the H11-H12 loop in stabilizing the active conformation of RT the human mineralocorticoid receptor."; RL Mol. Endocrinol. 14:1210-1221(2000). RN [15] RP SUBCELLULAR LOCATION, AND INTERACTION WITH HSD11B2. RX PubMed=11350956; DOI=10.1074/jbc.m100374200; RA Odermatt A., Arnold P., Frey F.J.; RT "The intracellular localization of the mineralocorticoid receptor is RT regulated by 11beta-hydroxysteroid dehydrogenase type 2."; RL J. Biol. Chem. 276:28484-28492(2001). RN [16] RP SUBCELLULAR LOCATION. RX PubMed=19029984; DOI=10.1038/nm.1879; RA Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., RA Miyoshi J., Takai Y., Fujita T.; RT "Modification of mineralocorticoid receptor function by Rac1 GTPase: RT implication in proteinuric kidney disease."; RL Nat. Med. 14:1370-1376(2008). RN [17] {ECO:0007744|PDB:2AA2, ECO:0007744|PDB:2AA5, ECO:0007744|PDB:2AA6, ECO:0007744|PDB:2AA7, ECO:0007744|PDB:2AAX, ECO:0007744|PDB:2AB2} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 712-984 OF MUTANT SER-808 IN RP COMPLEXES WITH AGONIST AND ANTAGONISTS SUCH AS 11-DEOXYCORTICOSTERONE; RP ALDOSTERONE AND PROGESTERONE, CHARACTERIZATION OF VARIANT EOHSEP LEU-810, RP AND MUTAGENESIS OF SER-767; ASN-770 AND THR-945. RX PubMed=15967794; DOI=10.1074/jbc.m504098200; RA Bledsoe R.K., Madauss K.P., Holt J.A., Apolito C.J., Lambert M.H., RA Pearce K.H., Stanley T.B., Stewart E.L., Trump R.P., Willson T.M., RA Williams S.P.; RT "A ligand-mediated hydrogen bond network required for the activation of the RT mineralocorticoid receptor."; RL J. Biol. Chem. 280:31283-31293(2005). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 732-984 OF MUTANT SER-808 IN RP COMPLEX WITH STEROID LIGAND AND NCOA2, SUBUNIT, AND MUTAGENESIS OF LYS-782; RP LYS-785 AND GLU-796. RX PubMed=16061183; DOI=10.1016/j.molcel.2005.06.026; RA Li Y., Suino K., Daugherty J., Xu H.E.; RT "Structural and biochemical mechanisms for the specificity of hormone RT binding and coactivator assembly by mineralocorticoid receptor."; RL Mol. Cell 19:367-380(2005). RN [19] {ECO:0007744|PDB:1Y9R, ECO:0007744|PDB:1YA3} RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 731-984 OF MUTANT LEU-810 IN RP COMPLEXES WITH THE STEROID AGONISTS 11-DEOXYCORTICOSTERONE AND RP PROGESTERONE, CHARACTERIZATION OF VARIANT EOHSEP LEU-810, AND MUTAGENESIS RP OF GLN-776 AND ARG-817. RX PubMed=15908963; DOI=10.1038/nsmb939; RA Fagart J., Huyet J., Pinon G.M., Rochel M., Mayer C., Rafestin-Oblin M.-E.; RT "Crystal structure of a mutant mineralocorticoid receptor responsible for RT hypertension."; RL Nat. Struct. Mol. Biol. 12:554-555(2005). RN [20] {ECO:0007744|PDB:4TNT} RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 593-671 IN COMPLEX WITH DNA AND RP ZINC. RX PubMed=25188500; DOI=10.1371/journal.pone.0107000; RA Hudson W.H., Youn C., Ortlund E.A.; RT "Crystal structure of the mineralocorticoid receptor DNA binding domain in RT complex with DNA."; RL PLoS ONE 9:e107000-e107000(2014). RN [21] RP VARIANTS ILE-180; THR-444; GLN-537 AND SER-554. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood- RT pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). RN [22] RP CHARACTERIZATION OF VARIANT PHA1A PRO-924. RX PubMed=11134129; DOI=10.1210/jcem.85.12.7078; RA Tajima T., Kitagawa H., Yokoya S., Tachibana K., Adachi M., Nakae J., RA Suwa S., Katoh S., Fujieda K.; RT "A novel missense mutation of mineralocorticoid receptor gene in one RT Japanese family with a renal form of pseudohypoaldosteronism type 1."; RL J. Clin. Endocrinol. Metab. 85:4690-4694(2000). RN [23] RP VARIANT EOHSEP LEU-810, AND MUTAGENESIS OF SER-810. RX PubMed=10884226; DOI=10.1126/science.289.5476.119; RA Geller D.S., Farhi A., Pinkerton N., Fradley M., Moritz M., Spitzer A., RA Meinke G., Tsai F.T.F., Sigler P.B., Lifton R.P.; RT "Activating mineralocorticoid receptor mutation in hypertension exacerbated RT by pregnancy."; RL Science 289:119-123(2000). RN [24] RP CHARACTERIZATION OF VARIANTS ILE-180 AND ALA-241. RX PubMed=12483305; DOI=10.1007/s00439-002-0855-7; RA Arai K., Nakagomi Y., Iketani M., Shimura Y., Amemiya S., Ohyama K., RA Shibasaki T.; RT "Functional polymorphisms in the mineralocorticoid receptor and amirolide- RT sensitive sodium channel genes in a patient with sporadic RT pseudohypoaldosteronism."; RL Hum. Genet. 112:91-97(2003). RN [25] RP CHARACTERIZATION OF VARIANTS PHA1A ARG-633; ARG-776; PRO-924 AND PRO-979. RX PubMed=12788847; DOI=10.1210/jc.2002-021932; RA Sartorato P., Lapeyraque A.-L., Armanini D., Kuhnle U., Khaldi Y., RA Salomon R., Abadie V., Di Battista E., Naselli A., Racine A., Bosio M., RA Caprio M., Poulet-Young V., Chabrolle J.-P., Niaudet P., De Gennes C., RA Lecornec M.-H., Poisson E., Fusco A.M., Loli P., Lombes M., Zennaro M.-C.; RT "Different inactivating mutations of the mineralocorticoid receptor in RT fourteen families affected by type I pseudohypoaldosteronism."; RL J. Clin. Endocrinol. Metab. 88:2508-2517(2003). RN [26] RP CHARACTERIZATION OF VARIANTS PHA1A LEU-818 AND GLY-972. RX PubMed=16954160; DOI=10.1210/jc.2006-1161; RA Riepe F.G., Finkeldei J., de Sanctis L., Einaudi S., Testa A., Karges B., RA Peter M., Viemann M., Groetzinger J., Sippell W.G., Fejes-Toth G., RA Krone N.; RT "Elucidating the underlying molecular pathogenesis of NR3C2 mutants causing RT autosomal dominant pseudohypoaldosteronism type 1."; RL J. Clin. Endocrinol. Metab. 91:4552-4561(2006). RN [27] RP VARIANT [LARGE SCALE ANALYSIS] GLN-7. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [28] RP VARIANTS PHA1A SER-645; SER-659; SER-759; PRO-769; LYS-770; PRO-805 AND RP ARG-815. RX PubMed=16972228; DOI=10.1002/humu.20371; RA Pujo L., Fagart J., Gary F., Papadimitriou D.T., Claes A., Jeunemaitre X., RA Zennaro M.-C.; RT "Mineralocorticoid receptor mutations are the principal cause of renal type RT 1 pseudohypoaldosteronism."; RL Hum. Mutat. 28:33-40(2007). CC -!- FUNCTION: Receptor for both mineralocorticoids (MC) such as aldosterone CC and glucocorticoids (GC) such as corticosterone or cortisol. Binds to CC mineralocorticoid response elements (MRE) and transactivates target CC genes. The effect of MC is to increase ion and water transport and thus CC raise extracellular fluid volume and blood pressure and lower potassium CC levels. {ECO:0000269|PubMed:3037703}. CC -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70, and CC FKBP4, in the absence of ligand. After ligand binding, it translocates CC to the nucleus and binds to DNA as a homodimer and as a heterodimer CC with NR3C1. May interact with HSD11B2 in the absence of ligand. Binds CC the coactivators NCOA1, NCOA2, TIF1 and NRIP1. CC {ECO:0000269|PubMed:10935545, ECO:0000269|PubMed:11350956, CC ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:16061183}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum CC membrane; Peripheral membrane protein. Note=Cytoplasmic and nuclear in CC the absence of ligand; nuclear after ligand-binding. When bound to CC HSD11B2, it is found associated with the endoplasmic reticulum CC membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P08235-1; Sequence=Displayed; CC Name=2; CC IsoId=P08235-2; Sequence=VSP_007358, VSP_007359; CC Name=3; CC IsoId=P08235-3; Sequence=VSP_007357; CC Name=4; Synonyms=Delta; CC IsoId=P08235-4; Sequence=VSP_007360; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in distal tubules, CC convoluted tubules and cortical collecting duct in kidney, and in sweat CC glands. Detected at lower levels in cardiomyocytes, in epidermis and in CC colon enterocytes. {ECO:0000269|PubMed:11518808, CC ECO:0000269|PubMed:9141514}. CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a CC DNA-binding domain and a C-terminal ligand-binding domain. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:1655735}. CC -!- DISEASE: Pseudohypoaldosteronism 1, autosomal dominant (PHA1A) CC [MIM:177735]: A salt wasting disease resulting from target organ CC unresponsiveness to mineralocorticoids. PHA1A is a mild form CC characterized by target organ defects confined to kidney. Patients may CC present with neonatal renal salt wasting with hyperkalaemic acidosis CC despite high aldosterone levels. These patients improve with age and CC usually become asymptomatic without treatment. CC {ECO:0000269|PubMed:11134129, ECO:0000269|PubMed:12788847, CC ECO:0000269|PubMed:16954160, ECO:0000269|PubMed:16972228}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Early-onset hypertension with severe exacerbation in pregnancy CC (EOHSEP) [MIM:605115]: Inheritance is autosomal dominant. The disease CC is characterized by the onset of severe hypertension before the age of CC 20, and by suppression of aldosterone secretion. CC {ECO:0000269|PubMed:10884226, ECO:0000269|PubMed:15908963, CC ECO:0000269|PubMed:15967794}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks steroid-binding activity and acts as CC ligand-independent transactivator. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44262/NR3C2"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Mineralocorticoid receptor entry; CC URL="https://en.wikipedia.org/wiki/Mineralocorticoid_receptor"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16801; AAA59571.1; -; mRNA. DR EMBL; AJ315514; CAC67405.1; -; mRNA. DR EMBL; AJ315515; CAC67406.1; -; mRNA. DR EMBL; EU326312; ACA05924.1; -; Genomic_DNA. DR EMBL; EU326312; ACA05925.1; -; Genomic_DNA. DR EMBL; FJ515829; ACS13716.1; -; Genomic_DNA. DR EMBL; FJ515829; ACS13717.1; -; Genomic_DNA. DR EMBL; AC069272; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093881; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC106899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC111758; AAI11759.1; -; mRNA. DR EMBL; AH006913; AAC63513.1; -; Genomic_DNA. DR CCDS; CCDS3772.1; -. [P08235-1] DR CCDS; CCDS54811.1; -. [P08235-4] DR PIR; A29513; A29513. DR RefSeq; NP_000892.2; NM_000901.4. [P08235-1] DR RefSeq; NP_001159576.1; NM_001166104.1. [P08235-4] DR RefSeq; XP_011530277.1; XM_011531975.1. [P08235-3] DR RefSeq; XP_011530278.1; XM_011531976.2. DR RefSeq; XP_011530279.1; XM_011531977.2. DR RefSeq; XP_016863706.1; XM_017008217.1. DR PDB; 1Y9R; X-ray; 1.96 A; A/B=731-984. DR PDB; 1YA3; X-ray; 2.34 A; A/B/C=731-984. DR PDB; 2A3I; X-ray; 1.95 A; A=732-984. DR PDB; 2AA2; X-ray; 1.95 A; A=712-984. DR PDB; 2AA5; X-ray; 2.20 A; A/B=712-984. DR PDB; 2AA6; X-ray; 1.95 A; A/B=712-984. DR PDB; 2AA7; X-ray; 2.20 A; A=712-984. DR PDB; 2AAX; X-ray; 1.75 A; A/B=712-984. DR PDB; 2AB2; X-ray; 1.85 A; A/B=712-984. DR PDB; 2ABI; X-ray; 2.33 A; A/B/C=731-984. DR PDB; 2OAX; X-ray; 2.29 A; A/B/C/D/E/F=731-984. DR PDB; 3VHU; X-ray; 2.11 A; A=712-984. DR PDB; 3VHV; X-ray; 1.35 A; A=727-984. DR PDB; 3WFF; X-ray; 2.05 A; A=712-984. DR PDB; 3WFG; X-ray; 1.40 A; A=712-984. DR PDB; 4PF3; X-ray; 1.10 A; A=712-984. DR PDB; 4TNT; X-ray; 2.39 A; A/B=593-671. DR PDB; 4UDA; X-ray; 2.03 A; A=735-984. DR PDB; 4UDB; X-ray; 2.36 A; A=735-984. DR PDB; 5HCV; X-ray; 2.50 A; A/B/C=732-984. DR PDB; 5L7E; X-ray; 1.86 A; A=735-984. DR PDB; 5L7G; X-ray; 2.01 A; A=735-984. DR PDB; 5L7H; X-ray; 1.84 A; A=735-984. DR PDB; 5MWP; X-ray; 1.82 A; A=735-984. DR PDB; 5MWY; X-ray; 1.75 A; A=735-984. DR PDB; 6GEV; X-ray; 1.54 A; A=735-984. DR PDB; 6GG8; X-ray; 1.80 A; A=735-984. DR PDB; 6GGG; X-ray; 1.71 A; A=735-984. DR PDB; 6L88; X-ray; 3.00 A; A/B/C/D=735-984. DR PDBsum; 1Y9R; -. DR PDBsum; 1YA3; -. DR PDBsum; 2A3I; -. DR PDBsum; 2AA2; -. DR PDBsum; 2AA5; -. DR PDBsum; 2AA6; -. DR PDBsum; 2AA7; -. DR PDBsum; 2AAX; -. DR PDBsum; 2AB2; -. DR PDBsum; 2ABI; -. DR PDBsum; 2OAX; -. DR PDBsum; 3VHU; -. DR PDBsum; 3VHV; -. DR PDBsum; 3WFF; -. DR PDBsum; 3WFG; -. DR PDBsum; 4PF3; -. DR PDBsum; 4TNT; -. DR PDBsum; 4UDA; -. DR PDBsum; 4UDB; -. DR PDBsum; 5HCV; -. DR PDBsum; 5L7E; -. DR PDBsum; 5L7G; -. DR PDBsum; 5L7H; -. DR PDBsum; 5MWP; -. DR PDBsum; 5MWY; -. DR PDBsum; 6GEV; -. DR PDBsum; 6GG8; -. DR PDBsum; 6GGG; -. DR PDBsum; 6L88; -. DR AlphaFoldDB; P08235; -. DR SMR; P08235; -. DR BioGRID; 110451; 35. DR CORUM; P08235; -. DR IntAct; P08235; 8. DR STRING; 9606.ENSP00000350815; -. DR BindingDB; P08235; -. DR ChEMBL; CHEMBL1994; -. DR DrugBank; DB04630; Aldosterone. DR DrugBank; DB01013; Clobetasol propionate. DR DrugBank; DB04652; Corticosterone. DR DrugBank; DB06780; Desoxycorticosterone acetate. DR DrugBank; DB01134; Desoxycorticosterone pivalate. DR DrugBank; DB01395; Drospirenone. DR DrugBank; DB00700; Eplerenone. DR DrugBank; DB01023; Felodipine. DR DrugBank; DB16165; Finerenone. DR DrugBank; DB00687; Fludrocortisone. DR DrugBank; DB13867; Fluticasone. DR DrugBank; DB08906; Fluticasone furoate. DR DrugBank; DB00588; Fluticasone propionate. DR DrugBank; DB02998; Metribolone. DR DrugBank; DB00393; Nimodipine. DR DrugBank; DB00396; Progesterone. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB02901; Stanolone. DR DrugBank; DB13951; Stanolone acetate. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB13943; Testosterone cypionate. DR DrugBank; DB13944; Testosterone enanthate. DR DrugCentral; P08235; -. DR GuidetoPHARMACOLOGY; 626; -. DR GlyGen; P08235; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P08235; -. DR PhosphoSitePlus; P08235; -. DR BioMuta; NR3C2; -. DR DMDM; 126885; -. DR jPOST; P08235; -. DR MassIVE; P08235; -. DR MaxQB; P08235; -. DR PaxDb; 9606-ENSP00000350815; -. DR PeptideAtlas; P08235; -. DR ProteomicsDB; 2889; -. DR ProteomicsDB; 2891; -. DR ProteomicsDB; 52088; -. [P08235-1] DR ProteomicsDB; 52089; -. [P08235-2] DR ProteomicsDB; 52090; -. [P08235-3] DR ProteomicsDB; 52091; -. [P08235-4] DR Antibodypedia; 3971; 341 antibodies from 33 providers. DR DNASU; 4306; -. DR Ensembl; ENST00000342437.8; ENSP00000343907.4; ENSG00000151623.15. [P08235-2] DR Ensembl; ENST00000344721.8; ENSP00000341390.4; ENSG00000151623.15. [P08235-1] DR Ensembl; ENST00000358102.8; ENSP00000350815.3; ENSG00000151623.15. [P08235-1] DR Ensembl; ENST00000511528.1; ENSP00000421481.1; ENSG00000151623.15. [P08235-3] DR Ensembl; ENST00000512865.5; ENSP00000423510.1; ENSG00000151623.15. [P08235-4] DR Ensembl; ENST00000625323.2; ENSP00000486719.1; ENSG00000151623.15. [P08235-3] DR GeneID; 4306; -. DR KEGG; hsa:4306; -. DR MANE-Select; ENST00000358102.8; ENSP00000350815.3; NM_000901.5; NP_000892.2. DR UCSC; uc003ilk.5; human. [P08235-1] DR AGR; HGNC:7979; -. DR CTD; 4306; -. DR DisGeNET; 4306; -. DR GeneCards; NR3C2; -. DR HGNC; HGNC:7979; NR3C2. DR HPA; ENSG00000151623; Low tissue specificity. DR MalaCards; NR3C2; -. DR MIM; 177735; phenotype. DR MIM; 600983; gene. DR MIM; 605115; phenotype. DR neXtProt; NX_P08235; -. DR OpenTargets; ENSG00000151623; -. DR Orphanet; 171871; Renal pseudohypoaldosteronism type 1. DR PharmGKB; PA242; -. DR VEuPathDB; HostDB:ENSG00000151623; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000159333; -. DR InParanoid; P08235; -. DR OMA; ITFPKME; -. DR OrthoDB; 5350431at2759; -. DR PhylomeDB; P08235; -. DR PathwayCommons; P08235; -. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors. DR SignaLink; P08235; -. DR SIGNOR; P08235; -. DR BioGRID-ORCS; 4306; 15 hits in 1186 CRISPR screens. DR ChiTaRS; NR3C2; human. DR EvolutionaryTrace; P08235; -. DR GeneWiki; Mineralocorticoid_receptor; -. DR GenomeRNAi; 4306; -. DR Pharos; P08235; Tclin. DR PRO; PR:P08235; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P08235; Protein. DR Bgee; ENSG00000151623; Expressed in endothelial cell and 197 other cell types or tissues. DR ExpressionAtlas; P08235; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0034056; F:estrogen response element binding; IBA:GO_Central. DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central. DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:ProtInc. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW. DR GO; GO:0017025; F:TBP-class protein binding; IPI:DisProt. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IMP:ARUK-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd07172; NR_DBD_GR_PR; 1. DR CDD; cd07075; NR_LBD_MR; 1. DR DisProt; DP01561; -. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR IDEAL; IID00702; -. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. DR PANTHER; PTHR48092:SF19; MINERALOCORTICOID RECEPTOR; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; KW DNA-binding; Endoplasmic reticulum; Lipid-binding; Membrane; Metal-binding; KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..984 FT /note="Mineralocorticoid receptor" FT /id="PRO_0000053682" FT DOMAIN 726..964 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 603..668 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 603..623 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 639..663 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..602 FT /note="Modulating" FT REGION 231..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 347..373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 669..725 FT /note="Hinge" FT REGION 684..710 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 782..785 FT /note="Important for coactivator binding" FT COMPBIAS 690..706 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 603 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 606 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 620 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 623 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 639 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 645 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 655 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 658 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25188500, FT ECO:0007744|PDB:4TNT" FT BINDING 770 FT /ligand="21-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:16973" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1Y9R, FT ECO:0007744|PDB:2AA7" FT BINDING 770 FT /ligand="aldosterone" FT /ligand_id="ChEBI:CHEBI:27584" FT /evidence="ECO:0000269|PubMed:15967794, FT ECO:0007744|PDB:2AA2" FT BINDING 770 FT /ligand="progesterone" FT /ligand_id="ChEBI:CHEBI:17026" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1YA3, FT ECO:0007744|PDB:2AA5, ECO:0007744|PDB:2AA6" FT BINDING 776 FT /ligand="21-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:16973" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1Y9R, FT ECO:0007744|PDB:2AA7" FT BINDING 776 FT /ligand="aldosterone" FT /ligand_id="ChEBI:CHEBI:27584" FT /evidence="ECO:0000269|PubMed:15967794, FT ECO:0007744|PDB:2AA2" FT BINDING 776 FT /ligand="progesterone" FT /ligand_id="ChEBI:CHEBI:17026" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1YA3, FT ECO:0007744|PDB:2AA5, ECO:0007744|PDB:2AA6" FT BINDING 817 FT /ligand="21-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:16973" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1Y9R, FT ECO:0007744|PDB:2AA7" FT BINDING 817 FT /ligand="aldosterone" FT /ligand_id="ChEBI:CHEBI:27584" FT /evidence="ECO:0000269|PubMed:15967794, FT ECO:0007744|PDB:2AA2" FT BINDING 817 FT /ligand="progesterone" FT /ligand_id="ChEBI:CHEBI:17026" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1YA3, FT ECO:0007744|PDB:2AA5, ECO:0007744|PDB:2AA6" FT BINDING 945 FT /ligand="21-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:16973" FT /evidence="ECO:0000269|PubMed:15908963, FT ECO:0000269|PubMed:15967794, ECO:0007744|PDB:1Y9R, FT ECO:0007744|PDB:2AA7" FT BINDING 945 FT /ligand="aldosterone" FT /ligand_id="ChEBI:CHEBI:27584" FT /evidence="ECO:0000269|PubMed:15967794, FT ECO:0007744|PDB:2AA2" FT BINDING 945 FT /ligand="progesterone" FT /ligand_id="ChEBI:CHEBI:17026" FT /evidence="ECO:0000269|PubMed:15967794, FT ECO:0007744|PDB:2AA5, ECO:0007744|PDB:2AA6" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VII8" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VII8" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VII8" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VII8" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VII8" FT VAR_SEQ 633 FT /note="G -> GKCSW (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_007357" FT VAR_SEQ 672..788 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11518808, FT ECO:0000303|PubMed:15489334" FT /id="VSP_007360" FT VAR_SEQ 672..706 FT /note="ARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEE -> ERRCISLPCMNYA FT RGCTKSAFSSFDCSSPLKNTPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11518808" FT /id="VSP_007358" FT VAR_SEQ 707..984 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11518808" FT /id="VSP_007359" FT VARIANT 7 FT /note="H -> Q (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036063" FT VARIANT 180 FT /note="V -> I (decreased mineralocorticoid receptor FT activity; dbSNP:rs5522)" FT /evidence="ECO:0000269|PubMed:10391210, FT ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12483305" FT /id="VAR_014623" FT VARIANT 241 FT /note="V -> A (changed mineralocorticoid receptor activity; FT changed response curve to aldosterone stimulation)" FT /evidence="ECO:0000269|PubMed:11518808, FT ECO:0000269|PubMed:12483305" FT /id="VAR_015625" FT VARIANT 444 FT /note="N -> T (in dbSNP:rs5523)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014624" FT VARIANT 537 FT /note="R -> Q (in dbSNP:rs5526)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014625" FT VARIANT 554 FT /note="N -> S (in dbSNP:rs5527)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014626" FT VARIANT 633 FT /note="G -> R (in PHA1A; reduces transcription FT transactivation upon aldosterone binding; FT dbSNP:rs121912566)" FT /evidence="ECO:0000269|PubMed:12788847" FT /id="VAR_031268" FT VARIANT 645 FT /note="C -> S (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031269" FT VARIANT 659 FT /note="R -> S (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031270" FT VARIANT 759 FT /note="P -> S (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031271" FT VARIANT 769 FT /note="L -> P (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031272" FT VARIANT 770 FT /note="N -> K (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031273" FT VARIANT 776 FT /note="Q -> R (in PHA1A; reduces aldosterone binding; FT dbSNP:rs121912565)" FT /evidence="ECO:0000269|PubMed:12788847" FT /id="VAR_031274" FT VARIANT 805 FT /note="S -> P (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031275" FT VARIANT 810 FT /note="S -> L (in EOHSEP; alters receptor specificity and FT leads to constitutive activation; dbSNP:rs41511344)" FT /evidence="ECO:0000269|PubMed:10884226, FT ECO:0000269|PubMed:15908963, ECO:0000269|PubMed:15967794" FT /id="VAR_015626" FT VARIANT 815 FT /note="S -> R (in PHA1A)" FT /evidence="ECO:0000269|PubMed:16972228" FT /id="VAR_031276" FT VARIANT 818 FT /note="S -> L (in PHA1A; abolishes translocation to the FT nucleus and transcription transactivation upon aldosterone FT binding; dbSNP:rs121912573)" FT /evidence="ECO:0000269|PubMed:16954160" FT /id="VAR_031277" FT VARIANT 826 FT /note="F -> Y (in dbSNP:rs13306592)" FT /id="VAR_029311" FT VARIANT 924 FT /note="L -> P (in PHA1A; abolishes transcription FT transactivation upon aldosterone binding; FT dbSNP:rs121912563)" FT /evidence="ECO:0000269|PubMed:11134129, FT ECO:0000269|PubMed:12788847" FT /id="VAR_015627" FT VARIANT 972 FT /note="E -> G (in PHA1A; reduces affinity for aldosterone FT and transcription transactivation; dbSNP:rs121912574)" FT /evidence="ECO:0000269|PubMed:16954160" FT /id="VAR_031278" FT VARIANT 979 FT /note="L -> P (in PHA1A; loss of aldosterone binding and FT transcription transactivation; dbSNP:rs121912567)" FT /evidence="ECO:0000269|PubMed:12788847" FT /id="VAR_031279" FT MUTAGEN 767 FT /note="S->N: Loss of transcription transactivation." FT /evidence="ECO:0000269|PubMed:15967794" FT MUTAGEN 767 FT /note="S->Q: Strong decrease of transcription FT transactivation." FT /evidence="ECO:0000269|PubMed:15967794" FT MUTAGEN 770 FT /note="N->A,D,H,Q,S,T: Abolishes aldosterone binding and FT transcription transactivation." FT /evidence="ECO:0000269|PubMed:10760050, FT ECO:0000269|PubMed:15967794" FT MUTAGEN 776 FT /note="Q->A: Reduces aldosterone binding and transcription FT transactivation." FT /evidence="ECO:0000269|PubMed:10760050, FT ECO:0000269|PubMed:15908963" FT MUTAGEN 782 FT /note="K->E: Decreased coactivator binding." FT /evidence="ECO:0000269|PubMed:16061183" FT MUTAGEN 785 FT /note="K->E: Loss of coactivator binding." FT /evidence="ECO:0000269|PubMed:16061183" FT MUTAGEN 796 FT /note="E->R: Decreased coactivator binding." FT /evidence="ECO:0000269|PubMed:16061183" FT MUTAGEN 808 FT /note="C->S: Increases aldosterone-binding." FT /evidence="ECO:0000269|PubMed:9724527" FT MUTAGEN 810 FT /note="S->M: Alters receptor specificity." FT /evidence="ECO:0000269|PubMed:10884226" FT MUTAGEN 817 FT /note="R->A: Reduces aldosterone binding and transcription FT transactivation." FT /evidence="ECO:0000269|PubMed:10760050, FT ECO:0000269|PubMed:15908963" FT MUTAGEN 849 FT /note="C->S: Strongly decreases affinity for aldosterone FT and transcription transactivation." FT /evidence="ECO:0000269|PubMed:9724527" FT MUTAGEN 942 FT /note="C->S: Abolishes steroid binding and transcription FT transactivation." FT /evidence="ECO:0000269|PubMed:9724527" FT MUTAGEN 945 FT /note="T->A: Decreases aldosterone-binding and FT cortisol-binding." FT /evidence="ECO:0000269|PubMed:10760050, FT ECO:0000269|PubMed:15967794" FT MUTAGEN 952 FT /note="L->A: Reduces transcription transactivation." FT /evidence="ECO:0000269|PubMed:10935545" FT MUTAGEN 953 FT /note="K->A: Slightly reduces aldosterone binding and FT abolishes transcription transactivation." FT /evidence="ECO:0000269|PubMed:10935545" FT MUTAGEN 954 FT /note="V->A: Reduces aldosterone binding and abolishes FT transcription transactivation." FT /evidence="ECO:0000269|PubMed:10935545" FT MUTAGEN 956 FT /note="F->A: Abolishes aldosterone binding and FT transcription transactivation." FT /evidence="ECO:0000269|PubMed:10935545" FT MUTAGEN 957 FT /note="P->A: Slightly reduces aldosterone binding and FT transcription transactivation." FT /evidence="ECO:0000269|PubMed:10935545" FT CONFLICT 946 FT /note="F -> I (in Ref. 5; AAI11759)" FT /evidence="ECO:0000305" FT TURN 604..606 FT /evidence="ECO:0007829|PDB:4TNT" FT STRAND 612..614 FT /evidence="ECO:0007829|PDB:4TNT" FT HELIX 621..632 FT /evidence="ECO:0007829|PDB:4TNT" FT STRAND 640..643 FT /evidence="ECO:0007829|PDB:4TNT" FT TURN 649..654 FT /evidence="ECO:0007829|PDB:4TNT" FT HELIX 656..665 FT /evidence="ECO:0007829|PDB:4TNT" FT HELIX 728..733 FT /evidence="ECO:0007829|PDB:3VHV" FT HELIX 738..745 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 762..785 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 790..792 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 795..822 FT /evidence="ECO:0007829|PDB:4PF3" FT STRAND 825..830 FT /evidence="ECO:0007829|PDB:4PF3" FT STRAND 833..835 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 837..842 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 846..862 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 866..877 FT /evidence="ECO:0007829|PDB:4PF3" FT STRAND 879..881 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 889..909 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 911..913 FT /evidence="ECO:0007829|PDB:4PF3" FT TURN 914..916 FT /evidence="ECO:0007829|PDB:4UDB" FT HELIX 917..947 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 949..952 FT /evidence="ECO:0007829|PDB:4PF3" FT HELIX 958..972 FT /evidence="ECO:0007829|PDB:4PF3" FT STRAND 976..978 FT /evidence="ECO:0007829|PDB:3VHV" SQ SEQUENCE 984 AA; 107082 MW; 833D900F2CB27390 CRC64; METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC VSGAIPNNST QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT VAESMGLYMD SVRDADYSYE QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR PSTLSCVNTP LRSFMSDSGS SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS PAHASNVGSP LSSPLSSMKS SISSPPSHCS VKSPVSSPNN VTLRSSVSSP ANINNSRCSV SSPSNTNNRS TLSSPAASTV GSICSPVNNA FSYTASGTSA GSSTLRDVVP SPDTQEKGAQ EVPFPKTEEV ESAISNGVTG QLNIVQYIKP EPDGAFSSSC LGGNSKINSD SSFSVPIKQE STKHSCSGTS FKGNPTVNPF PFMDGSYFSF MDDKDYYSLS GILGPPVPGF DGNCEGSGFP VGIKQEPDDG SYYPEASIPS SAIVGVNSGG QSFHYRIGAQ GTISLSRSAR DQSFQHLSSF PPVNTLVESW KSHGDLSSRR SDGYPVLEYI PENVSSSTLR SVSTGSSRPS KICLVCGDEA SGCHYGVVTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI RRKNCPACRL QKCLQAGMNL GARKSKKLGK LKGIHEEQPQ QQQPPPPPPP PQSPEEGTTY IAPAKEPSVN TALVPQLSTI SRALTPSPVM VLENIEPEIV YAGYDSSKPD TAENLLSTLN RLAGKQMIQV VKWAKVLPGF KNLPLEDQIT LIQYSWMCLS SFALSWRSYK HTNSQFLYFA PDLVFNEEKM HQSAMYELCQ GMHQISLQFV RLQLTFEEYT IMKVLLLLST IPKDGLKSQA AFEEMRTNYI KELRKMVTKC PNNSGQSWQR FYQLTKLLDS MHDLVSDLLE FCFYTFRESH ALKVEFPAML VEIISDQLPK VESGNAKPLY FHRK //