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Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2)

 MCR_HUMAN               Reviewed;         984 AA.
P08235; B0ZBF5; B0ZBF7; Q2NKL1; Q96KQ8; Q96KQ9;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
22-NOV-2017, entry version 201.
RecName: Full=Mineralocorticoid receptor;
Short=MR;
AltName: Full=Nuclear receptor subfamily 3 group C member 2;
Name=NR3C2; Synonyms=MCR, MLR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Kidney;
PubMed=3037703; DOI=10.1126/science.3037703;
Arriza J.L., Weinberger C., Cerelli G., Glaser T.M., Handelin B.L.,
Housman D.E., Evans R.M.;
"Cloning of human mineralocorticoid receptor complementary DNA:
structural and functional kinship with the glucocorticoid receptor.";
Science 237:268-275(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), TISSUE SPECIFICITY,
INTERACTION WITH NCOA1; TIF1 AND NRIP1, AND VARIANTS VAL-180 AND
VAL-241.
TISSUE=Heart;
PubMed=11518808; DOI=10.1210/mend.15.9.0689;
Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.;
"A new human MR splice variant is a ligand-independent transactivator
modulating corticosteroid action.";
Mol. Endocrinol. 15:1586-1598(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-180 AND VAL-241.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS VAL-180
AND VAL-241.
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
VAL-180 AND VAL-241.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 545-984, AND DISEASE.
PubMed=9662404; DOI=10.1038/966;
Geller D.S., Rodriguez-Soriano J., Vallo Boado A., Schifter S.,
Bayer M., Chang S.S., Lifton R.P.;
"Mutations in the mineralocorticoid receptor gene cause autosomal
dominant pseudohypoaldosteronism type I.";
Nat. Genet. 19:279-281(1998).
[7]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=1655735;
Alnemri E.S., Maksymowych A.B., Robertson N.M., Litwack G.;
"Overexpression and characterization of the human mineralocorticoid
receptor.";
J. Biol. Chem. 266:18072-18081(1991).
[8]
DEFINITION OF DIFFERENT FORMS OF PSEUDOHYPOALDOSTERONISM TYPE 1.
PubMed=1939532; DOI=10.1210/jcem-73-5-936;
Hanukoglu A.;
"Type I pseudohypoaldosteronism includes two clinically and
genetically distinct entities with either renal or multiple target
organ defects.";
J. Clin. Endocrinol. Metab. 73:936-944(1991).
[9]
IDENTIFICATION (ISOFORM 3).
TISSUE=Leukocyte;
PubMed=7495694; DOI=10.1016/0960-0760(95)00162-S;
Bloem L.J., Guo C., Pratt J.H.;
"Identification of a splice variant of the rat and human
mineralocorticoid receptor genes.";
J. Steroid Biochem. Mol. Biol. 55:159-162(1995).
[10]
TISSUE SPECIFICITY.
PubMed=9141514; DOI=10.1210/jcem.82.5.3933;
Zennaro M.-C., Farman N., Bonvalet J.-P., Lombes M.;
"Tissue-specific expression of alpha and beta messenger ribonucleic
acid isoforms of the human mineralocorticoid receptor in normal and
pathological states.";
J. Clin. Endocrinol. Metab. 82:1345-1352(1997).
[11]
TERNARY COMPLEX WITH HSP90; HSP70 AND FKBP4, AND DISSOCIATION UPON
ALDOSTERONE BINDING.
PubMed=9392437;
Bruner K.L., Derfoul A., Robertson N.M., Guerriero G.,
Fernandes-Alnemri T., Alnemri E.S., Litwack G.;
"The unliganded mineralocorticoid receptor is associated with heat
shock proteins 70 and 90 and the immunophilin FKBP-52.";
Recept. Signal Transduct. 7:85-98(1997).
[12]
MUTAGENESIS OF CYS-808; CYS-849 AND CYS-942.
PubMed=9724527; DOI=10.1021/bi980593e;
Lupo B., Mesnier D., Auzou G.;
"Cysteines 849 and 942 of human mineralocorticoid receptor are crucial
for steroid binding.";
Biochemistry 37:12153-12159(1998).
[13]
MUTAGENESIS OF ASN-770; GLN-776; ARG-817 AND THR-945.
PubMed=10760050; DOI=10.1046/j.1523-1755.2000.00958.x;
Hellal-Levy C., Fagart J., Souque A., Rafestin-Oblin M.-E.;
"Mechanistic aspects of mineralocorticoid receptor activation.";
Kidney Int. 57:1250-1255(2000).
[14]
INTERACTION WITH NCOA1; TIF1 AND NRIP1, AND MUTAGENESIS OF LEU-952;
LYS-953; VAL-954; PHE-956 AND PRO-957.
PubMed=10935545; DOI=10.1210/mend.14.8.0502;
Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D.,
Rafestin-Oblin M.-E.;
"Crucial role of the H11-H12 loop in stabilizing the active
conformation of the human mineralocorticoid receptor.";
Mol. Endocrinol. 14:1210-1221(2000).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH HSD11B2.
PubMed=11350956; DOI=10.1074/jbc.M100374200;
Odermatt A., Arnold P., Frey F.J.;
"The intracellular localization of the mineralocorticoid receptor is
regulated by 11beta-hydroxysteroid dehydrogenase type 2.";
J. Biol. Chem. 276:28484-28492(2001).
[16]
SUBCELLULAR LOCATION.
PubMed=19029984; DOI=10.1038/nm.1879;
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H.,
Tanaka H., Miyoshi J., Takai Y., Fujita T.;
"Modification of mineralocorticoid receptor function by Rac1 GTPase:
implication in proteinuric kidney disease.";
Nat. Med. 14:1370-1376(2008).
[17]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 712-984 OF MUTANT SER-808 IN
COMPLEXES WITH AGONIST AND ANTAGONISTS, CHARACTERIZATION OF VARIANT
EOHSEP LEU-810, AND MUTAGENESIS OF SER-767; ASN-770 AND THR-945.
PubMed=15967794; DOI=10.1074/jbc.M504098200;
Bledsoe R.K., Madauss K.P., Holt J.A., Apolito C.J., Lambert M.H.,
Pearce K.H., Stanley T.B., Stewart E.L., Trump R.P., Willson T.M.,
Williams S.P.;
"A ligand-mediated hydrogen bond network required for the activation
of the mineralocorticoid receptor.";
J. Biol. Chem. 280:31283-31293(2005).
[18]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 732-984 OF MUTANT SER-808 IN
COMPLEX WITH STEROID LIGAND AND NCOA2, SUBUNIT, AND MUTAGENESIS OF
LYS-782; LYS-785 AND GLU-796.
PubMed=16061183; DOI=10.1016/j.molcel.2005.06.026;
Li Y., Suino K., Daugherty J., Xu H.E.;
"Structural and biochemical mechanisms for the specificity of hormone
binding and coactivator assembly by mineralocorticoid receptor.";
Mol. Cell 19:367-380(2005).
[19]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 731-984 OF MUTANT LEU-810 IN
COMPLEXES WITH STEROID AGONISTS, CHARACTERIZATION OF VARIANT EOHSEP
LEU-810, AND MUTAGENESIS OF GLN-776 AND ARG-817.
PubMed=15908963; DOI=10.1038/nsmb939;
Fagart J., Huyet J., Pinon G.M., Rochel M., Mayer C.,
Rafestin-Oblin M.-E.;
"Crystal structure of a mutant mineralocorticoid receptor responsible
for hypertension.";
Nat. Struct. Mol. Biol. 12:554-555(2005).
[20]
VARIANTS VAL-180; THR-444; GLN-537 AND SER-554.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
[21]
CHARACTERIZATION OF VARIANT PHA1A PRO-924.
PubMed=11134129; DOI=10.1210/jcem.85.12.7078;
Tajima T., Kitagawa H., Yokoya S., Tachibana K., Adachi M., Nakae J.,
Suwa S., Katoh S., Fujieda K.;
"A novel missense mutation of mineralocorticoid receptor gene in one
Japanese family with a renal form of pseudohypoaldosteronism type 1.";
J. Clin. Endocrinol. Metab. 85:4690-4694(2000).
[22]
VARIANT EOHSEP LEU-810, AND MUTAGENESIS OF SER-810.
PubMed=10884226; DOI=10.1126/science.289.5476.119;
Geller D.S., Farhi A., Pinkerton N., Fradley M., Moritz M.,
Spitzer A., Meinke G., Tsai F.T.F., Sigler P.B., Lifton R.P.;
"Activating mineralocorticoid receptor mutation in hypertension
exacerbated by pregnancy.";
Science 289:119-123(2000).
[23]
CHARACTERIZATION OF VARIANTS VAL-180 AND VAL-241.
PubMed=12483305; DOI=10.1007/s00439-002-0855-7;
Arai K., Nakagomi Y., Iketani M., Shimura Y., Amemiya S., Ohyama K.,
Shibasaki T.;
"Functional polymorphisms in the mineralocorticoid receptor and
amirolide-sensitive sodium channel genes in a patient with sporadic
pseudohypoaldosteronism.";
Hum. Genet. 112:91-97(2003).
[24]
CHARACTERIZATION OF VARIANTS PHA1A ARG-633; ARG-776; PRO-924 AND
PRO-979.
PubMed=12788847; DOI=10.1210/jc.2002-021932;
Sartorato P., Lapeyraque A.-L., Armanini D., Kuhnle U., Khaldi Y.,
Salomon R., Abadie V., Di Battista E., Naselli A., Racine A.,
Bosio M., Caprio M., Poulet-Young V., Chabrolle J.-P., Niaudet P.,
De Gennes C., Lecornec M.-H., Poisson E., Fusco A.M., Loli P.,
Lombes M., Zennaro M.-C.;
"Different inactivating mutations of the mineralocorticoid receptor in
fourteen families affected by type I pseudohypoaldosteronism.";
J. Clin. Endocrinol. Metab. 88:2508-2517(2003).
[25]
CHARACTERIZATION OF VARIANTS PHA1A LEU-818 AND GLY-972.
PubMed=16954160; DOI=10.1210/jc.2006-1161;
Riepe F.G., Finkeldei J., de Sanctis L., Einaudi S., Testa A.,
Karges B., Peter M., Viemann M., Groetzinger J., Sippell W.G.,
Fejes-Toth G., Krone N.;
"Elucidating the underlying molecular pathogenesis of NR3C2 mutants
causing autosomal dominant pseudohypoaldosteronism type 1.";
J. Clin. Endocrinol. Metab. 91:4552-4561(2006).
[26]
VARIANT [LARGE SCALE ANALYSIS] GLN-7.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[27]
VARIANTS PHA1A SER-645; SER-659; SER-759; PRO-769; LYS-770; PRO-805
AND ARG-815.
PubMed=16972228; DOI=10.1002/humu.20371;
Pujo L., Fagart J., Gary F., Papadimitriou D.T., Claes A.,
Jeunemaitre X., Zennaro M.-C.;
"Mineralocorticoid receptor mutations are the principal cause of renal
type 1 pseudohypoaldosteronism.";
Hum. Mutat. 28:33-40(2007).
-!- FUNCTION: Receptor for both mineralocorticoids (MC) such as
aldosterone and glucocorticoids (GC) such as corticosterone or
cortisol. Binds to mineralocorticoid response elements (MRE) and
transactivates target genes. The effect of MC is to increase ion
and water transport and thus raise extracellular fluid volume and
blood pressure and lower potassium levels.
{ECO:0000269|PubMed:3037703}.
-!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70,
and FKBP4, in the absence of ligand. After ligand binding, it
translocates to the nucleus and binds to DNA as a homodimer and as
a heterodimer with NR3C1. May interact with HSD11B2 in the absence
of ligand. Binds the coactivators NCOA1, NCOA2, TIF1 and NRIP1.
{ECO:0000269|PubMed:10935545, ECO:0000269|PubMed:11350956,
ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:16061183}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum
membrane; Peripheral membrane protein. Note=Cytoplasmic and
nuclear in the absence of ligand; nuclear after ligand-binding.
When bound to HSD11B2, it is found associated with the endoplasmic
reticulum membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P08235-1; Sequence=Displayed;
Name=2;
IsoId=P08235-2; Sequence=VSP_007358, VSP_007359;
Note=Lacks steroid-binding activity and acts as
ligand-independent transactivator.;
Name=3;
IsoId=P08235-3; Sequence=VSP_007357;
Name=4; Synonyms=Delta;
IsoId=P08235-4; Sequence=VSP_007360;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in distal
tubules, convoluted tubules and cortical collecting duct in
kidney, and in sweat glands. Detected at lower levels in
cardiomyocytes, in epidermis and in colon enterocytes.
{ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:9141514}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:1655735}.
-!- DISEASE: Pseudohypoaldosteronism 1, autosomal dominant (PHA1A)
[MIM:177735]: A salt wasting disease resulting from target organ
unresponsiveness to mineralocorticoids. PHA1A is a mild form
characterized by target organ defects confined to kidney. Patients
may present with neonatal renal salt wasting with hyperkalaemic
acidosis despite high aldosterone levels. These patients improve
with age and usually become asymptomatic without treatment.
{ECO:0000269|PubMed:11134129, ECO:0000269|PubMed:12788847,
ECO:0000269|PubMed:16954160, ECO:0000269|PubMed:16972228}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Early-onset hypertension with severe exacerbation in
pregnancy (EOHSEP) [MIM:605115]: Inheritance is autosomal
dominant. The disease is characterized by the onset of severe
hypertension before the age of 20, and by suppression of
aldosterone secretion. {ECO:0000269|PubMed:10884226,
ECO:0000269|PubMed:15908963, ECO:0000269|PubMed:15967794}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NR3C2ID44262ch4q31.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Mineralocorticoid receptor
entry;
URL="https://en.wikipedia.org/wiki/Mineralocorticoid_receptor";
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EMBL; M16801; AAA59571.1; -; mRNA.
EMBL; AJ315514; CAC67405.1; -; mRNA.
EMBL; AJ315515; CAC67406.1; -; mRNA.
EMBL; EU326312; ACA05924.1; -; Genomic_DNA.
EMBL; EU326312; ACA05925.1; -; Genomic_DNA.
EMBL; FJ515829; ACS13716.1; -; Genomic_DNA.
EMBL; FJ515829; ACS13717.1; -; Genomic_DNA.
EMBL; AC069272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC111758; AAI11759.1; -; mRNA.
EMBL; AH006913; AAC63513.1; -; Genomic_DNA.
CCDS; CCDS3772.1; -. [P08235-1]
CCDS; CCDS54811.1; -. [P08235-4]
PIR; A29513; A29513.
RefSeq; NP_000892.2; NM_000901.4.
RefSeq; NP_001159576.1; NM_001166104.1.
RefSeq; XP_011530277.1; XM_011531975.1.
RefSeq; XP_011530278.1; XM_011531976.2.
RefSeq; XP_011530279.1; XM_011531977.2.
UniGene; Hs.163924; -.
PDB; 1Y9R; X-ray; 1.96 A; A/B=731-984.
PDB; 1YA3; X-ray; 2.34 A; A/B/C=731-984.
PDB; 2A3I; X-ray; 1.95 A; A=732-984.
PDB; 2AA2; X-ray; 1.95 A; A=712-984.
PDB; 2AA5; X-ray; 2.20 A; A/B=712-984.
PDB; 2AA6; X-ray; 1.95 A; A/B=712-984.
PDB; 2AA7; X-ray; 2.20 A; A=712-984.
PDB; 2AAX; X-ray; 1.75 A; A/B=712-984.
PDB; 2AB2; X-ray; 1.85 A; A/B=712-984.
PDB; 2ABI; X-ray; 2.33 A; A/B/C=731-984.
PDB; 2OAX; X-ray; 2.29 A; A/B/C/D/E/F=731-984.
PDB; 3VHU; X-ray; 2.11 A; A=712-984.
PDB; 3VHV; X-ray; 1.35 A; A=727-984.
PDB; 3WFF; X-ray; 2.05 A; A=712-984.
PDB; 3WFG; X-ray; 1.40 A; A=712-984.
PDB; 4PF3; X-ray; 1.10 A; A=712-984.
PDB; 4TNT; X-ray; 2.39 A; A/B=593-671.
PDB; 4UDA; X-ray; 2.03 A; A=735-984.
PDB; 4UDB; X-ray; 2.36 A; A=735-984.
PDB; 5HCV; X-ray; 2.50 A; A/B/C=732-984.
PDB; 5L7E; X-ray; 1.86 A; A=735-984.
PDB; 5L7G; X-ray; 2.01 A; A=735-984.
PDB; 5L7H; X-ray; 1.84 A; A=735-984.
PDBsum; 1Y9R; -.
PDBsum; 1YA3; -.
PDBsum; 2A3I; -.
PDBsum; 2AA2; -.
PDBsum; 2AA5; -.
PDBsum; 2AA6; -.
PDBsum; 2AA7; -.
PDBsum; 2AAX; -.
PDBsum; 2AB2; -.
PDBsum; 2ABI; -.
PDBsum; 2OAX; -.
PDBsum; 3VHU; -.
PDBsum; 3VHV; -.
PDBsum; 3WFF; -.
PDBsum; 3WFG; -.
PDBsum; 4PF3; -.
PDBsum; 4TNT; -.
PDBsum; 4UDA; -.
PDBsum; 4UDB; -.
PDBsum; 5HCV; -.
PDBsum; 5L7E; -.
PDBsum; 5L7G; -.
PDBsum; 5L7H; -.
ProteinModelPortal; P08235; -.
SMR; P08235; -.
BioGrid; 110451; 25.
CORUM; P08235; -.
IntAct; P08235; 5.
STRING; 9606.ENSP00000341390; -.
BindingDB; P08235; -.
ChEMBL; CHEMBL1994; -.
DrugBank; DB04630; Aldosterone.
DrugBank; DB01134; Desoxycorticosterone Pivalate.
DrugBank; DB01395; Drospirenone.
DrugBank; DB00700; Eplerenone.
DrugBank; DB01023; Felodipine.
DrugBank; DB00687; Fludrocortisone.
DrugBank; DB00588; Fluticasone Propionate.
DrugBank; DB00393; Nimodipine.
DrugBank; DB00396; Progesterone.
DrugBank; DB00421; Spironolactone.
GuidetoPHARMACOLOGY; 626; -.
iPTMnet; P08235; -.
PhosphoSitePlus; P08235; -.
BioMuta; NR3C2; -.
DMDM; 126885; -.
MaxQB; P08235; -.
PaxDb; P08235; -.
PeptideAtlas; P08235; -.
PRIDE; P08235; -.
Ensembl; ENST00000511528; ENSP00000421481; ENSG00000151623.
Ensembl; ENST00000512865; ENSP00000423510; ENSG00000151623.
GeneID; 4306; -.
KEGG; hsa:4306; -.
UCSC; uc003ilk.5; human. [P08235-1]
CTD; 4306; -.
DisGeNET; 4306; -.
EuPathDB; HostDB:ENSG00000151623.14; -.
GeneCards; NR3C2; -.
H-InvDB; HIX0024570; -.
HGNC; HGNC:7979; NR3C2.
HPA; CAB009155; -.
HPA; HPA074979; -.
MalaCards; NR3C2; -.
MIM; 177735; phenotype.
MIM; 600983; gene.
MIM; 605115; phenotype.
neXtProt; NX_P08235; -.
Orphanet; 88660; Pseudohyperaldosteronism type 2.
Orphanet; 171871; Renal pseudohypoaldosteronism type 1.
PharmGKB; PA242; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000247011; -.
HOVERGEN; HBG006336; -.
InParanoid; P08235; -.
KO; K08555; -.
PhylomeDB; P08235; -.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P08235; -.
SIGNOR; P08235; -.
ChiTaRS; NR3C2; human.
EvolutionaryTrace; P08235; -.
GeneWiki; Mineralocorticoid_receptor; -.
GenomeRNAi; 4306; -.
PRO; PR:P08235; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000151623; -.
CleanEx; HS_NR3C2; -.
ExpressionAtlas; P08235; baseline and differential.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Endoplasmic reticulum; Lipid-binding;
Membrane; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 984 Mineralocorticoid receptor.
/FTId=PRO_0000053682.
DNA_BIND 603 668 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 603 623 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 639 663 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 602 Modulating.
REGION 669 732 Hinge.
REGION 733 984 Steroid-binding.
REGION 782 785 Important for coactivator binding.
BINDING 770 770 Steroid.
BINDING 776 776 Steroid.
BINDING 817 817 Steroid.
BINDING 945 945 Steroid.
MOD_RES 250 250 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VII8}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VII8}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VII8}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VII8}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VII8}.
VAR_SEQ 633 633 G -> GKCSW (in isoform 3). {ECO:0000305}.
/FTId=VSP_007357.
VAR_SEQ 672 788 Missing (in isoform 4).
{ECO:0000303|PubMed:11518808,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007360.
VAR_SEQ 672 706 ARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEE -> ER
RCISLPCMNYARGCTKSAFSSFDCSSPLKNTPS (in
isoform 2).
{ECO:0000303|PubMed:11518808}.
/FTId=VSP_007358.
VAR_SEQ 707 984 Missing (in isoform 2).
{ECO:0000303|PubMed:11518808}.
/FTId=VSP_007359.
VARIANT 7 7 H -> Q (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036063.
VARIANT 180 180 I -> V (high frequency in healthy
individuals; found in a patient with
sporadic pseudohypoaldosteronism type I;
increases transcription transactivation
at low aldosterone concentrations;
dbSNP:rs5522).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:11518808,
ECO:0000269|PubMed:12483305,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15815621,
ECO:0000269|Ref.3}.
/FTId=VAR_014623.
VARIANT 241 241 A -> V (high frequency in healthy
individuals; found in a patient with
sporadic pseudohypoaldosteronism type I;
reduces transcription transactivation
upon aldosterone binding).
{ECO:0000269|PubMed:11518808,
ECO:0000269|PubMed:12483305,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15815621,
ECO:0000269|Ref.3}.
/FTId=VAR_015625.
VARIANT 444 444 N -> T (in dbSNP:rs5523).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014624.
VARIANT 537 537 R -> Q (in dbSNP:rs5526).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014625.
VARIANT 554 554 N -> S (in dbSNP:rs5527).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014626.
VARIANT 633 633 G -> R (in PHA1A; reduces transcription
transactivation upon aldosterone
binding). {ECO:0000269|PubMed:12788847}.
/FTId=VAR_031268.
VARIANT 645 645 C -> S (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031269.
VARIANT 659 659 R -> S (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031270.
VARIANT 759 759 P -> S (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031271.
VARIANT 769 769 L -> P (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031272.
VARIANT 770 770 N -> K (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031273.
VARIANT 776 776 Q -> R (in PHA1A; reduces aldosterone
binding). {ECO:0000269|PubMed:12788847}.
/FTId=VAR_031274.
VARIANT 805 805 S -> P (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031275.
VARIANT 810 810 S -> L (in EOHSEP; alters receptor
specificity and leads to constitutive
activation; dbSNP:rs41511344).
{ECO:0000269|PubMed:10884226,
ECO:0000269|PubMed:15908963,
ECO:0000269|PubMed:15967794}.
/FTId=VAR_015626.
VARIANT 815 815 S -> R (in PHA1A).
{ECO:0000269|PubMed:16972228}.
/FTId=VAR_031276.
VARIANT 818 818 S -> L (in PHA1A; abolishes translocation
to the nucleus and transcription
transactivation upon aldosterone
binding). {ECO:0000269|PubMed:16954160}.
/FTId=VAR_031277.
VARIANT 826 826 F -> Y (in dbSNP:rs13306592).
/FTId=VAR_029311.
VARIANT 924 924 L -> P (in PHA1A; abolishes transcription
transactivation upon aldosterone
binding). {ECO:0000269|PubMed:11134129,
ECO:0000269|PubMed:12788847}.
/FTId=VAR_015627.
VARIANT 972 972 E -> G (in PHA1A; reduces affinity for
aldosterone and transcription
transactivation).
{ECO:0000269|PubMed:16954160}.
/FTId=VAR_031278.
VARIANT 979 979 L -> P (in PHA1A; loss of aldosterone
binding and transcription
transactivation).
{ECO:0000269|PubMed:12788847}.
/FTId=VAR_031279.
MUTAGEN 767 767 S->N: Loss of transcription
transactivation.
{ECO:0000269|PubMed:15967794}.
MUTAGEN 767 767 S->Q: Strong decrease of transcription
transactivation.
{ECO:0000269|PubMed:15967794}.
MUTAGEN 770 770 N->A,D,H,Q,S,T: Abolishes aldosterone
binding and transcription
transactivation.
{ECO:0000269|PubMed:10760050,
ECO:0000269|PubMed:15967794}.
MUTAGEN 776 776 Q->A: Reduces aldosterone binding and
transcription transactivation.
{ECO:0000269|PubMed:10760050,
ECO:0000269|PubMed:15908963}.
MUTAGEN 782 782 K->E: Decreased coactivator binding.
{ECO:0000269|PubMed:16061183}.
MUTAGEN 785 785 K->E: Loss of coactivator binding.
{ECO:0000269|PubMed:16061183}.
MUTAGEN 796 796 E->R: Decreased coactivator binding.
{ECO:0000269|PubMed:16061183}.
MUTAGEN 808 808 C->S: Increases aldosterone-binding.
{ECO:0000269|PubMed:9724527}.
MUTAGEN 810 810 S->M: Alters receptor specificity.
{ECO:0000269|PubMed:10884226}.
MUTAGEN 817 817 R->A: Reduces aldosterone binding and
transcription transactivation.
{ECO:0000269|PubMed:10760050,
ECO:0000269|PubMed:15908963}.
MUTAGEN 849 849 C->S: Strongly decreases affinity for
aldosterone and transcription
transactivation.
{ECO:0000269|PubMed:9724527}.
MUTAGEN 942 942 C->S: Abolishes steroid binding and
transcription transactivation.
{ECO:0000269|PubMed:9724527}.
MUTAGEN 945 945 T->A: Decreases aldosterone-binding and
cortisol-binding.
{ECO:0000269|PubMed:10760050,
ECO:0000269|PubMed:15967794}.
MUTAGEN 952 952 L->A: Reduces transcription
transactivation.
{ECO:0000269|PubMed:10935545}.
MUTAGEN 953 953 K->A: Slightly reduces aldosterone
binding and abolishes transcription
transactivation.
{ECO:0000269|PubMed:10935545}.
MUTAGEN 954 954 V->A: Reduces aldosterone binding and
abolishes transcription transactivation.
{ECO:0000269|PubMed:10935545}.
MUTAGEN 956 956 F->A: Abolishes aldosterone binding and
transcription transactivation.
{ECO:0000269|PubMed:10935545}.
MUTAGEN 957 957 P->A: Slightly reduces aldosterone
binding and transcription
transactivation.
{ECO:0000269|PubMed:10935545}.
CONFLICT 946 946 F -> I (in Ref. 5; AAI11759).
{ECO:0000305}.
TURN 604 606 {ECO:0000244|PDB:4TNT}.
STRAND 612 614 {ECO:0000244|PDB:4TNT}.
HELIX 621 632 {ECO:0000244|PDB:4TNT}.
STRAND 640 643 {ECO:0000244|PDB:4TNT}.
TURN 649 654 {ECO:0000244|PDB:4TNT}.
HELIX 656 665 {ECO:0000244|PDB:4TNT}.
HELIX 728 733 {ECO:0000244|PDB:3VHV}.
HELIX 738 745 {ECO:0000244|PDB:4PF3}.
HELIX 762 785 {ECO:0000244|PDB:4PF3}.
HELIX 790 792 {ECO:0000244|PDB:4PF3}.
HELIX 795 822 {ECO:0000244|PDB:4PF3}.
STRAND 825 830 {ECO:0000244|PDB:4PF3}.
STRAND 833 835 {ECO:0000244|PDB:4PF3}.
HELIX 837 842 {ECO:0000244|PDB:4PF3}.
HELIX 846 862 {ECO:0000244|PDB:4PF3}.
HELIX 866 877 {ECO:0000244|PDB:4PF3}.
STRAND 879 881 {ECO:0000244|PDB:4PF3}.
HELIX 889 909 {ECO:0000244|PDB:4PF3}.
HELIX 911 913 {ECO:0000244|PDB:4PF3}.
TURN 914 916 {ECO:0000244|PDB:4UDB}.
HELIX 917 947 {ECO:0000244|PDB:4PF3}.
HELIX 949 952 {ECO:0000244|PDB:4PF3}.
HELIX 958 972 {ECO:0000244|PDB:4PF3}.
STRAND 976 978 {ECO:0000244|PDB:3VHV}.
SEQUENCE 984 AA; 107067 MW; 8300CD1A18C1858A CRC64;
METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC VSGAIPNNST
QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT VAESMGLYMD SVRDADYSYE
QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR PSTLSCVNTP LRSFMSDSGS SVNGGVMRAI
VKSPIMCHEK SPSVCSPLNM TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN
AENRGSRSHS 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


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