MCR_HUMAN
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 03-AUG-2022, entry version 234.
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="http://atlasgeneticsoncology.org/Genes/NR3C2ID44262ch4q31.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Mineralocorticoid receptor entry;
CC URL="https://en.wikipedia.org/wiki/Mineralocorticoid_receptor";
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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; 33.
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 DrugBank; DB13946; Testosterone undecanoate.
DR DrugCentral; P08235; -.
DR GuidetoPHARMACOLOGY; 626; -.
DR iPTMnet; P08235; -.
DR PhosphoSitePlus; P08235; -.
DR BioMuta; NR3C2; -.
DR DMDM; 126885; -.
DR jPOST; P08235; -.
DR MassIVE; P08235; -.
DR MaxQB; P08235; -.
DR PaxDb; P08235; -.
DR PeptideAtlas; P08235; -.
DR PRIDE; 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; 296 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 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; TFPKMEE; -.
DR OrthoDB; 146963at2759; -.
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; 14 hits in 1100 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 195 other 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:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:ProtInc.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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: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 NIK/NF-kappaB signaling; 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 DisProt; DP01561; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
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 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; SSF48508; SSF48508; 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 (variant of uncertain significance; changed
FT mineralocorticoid receptor activity; changed response curve
FT 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 cortisol-
FT 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
