MCR_SAISC
ID MCR_SAISC Reviewed; 982 AA.
AC Q9N0W8;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Mineralocorticoid receptor;
DE Short=MR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 2;
GN Name=NR3C2; Synonyms=MLR;
OS Saimiri sciureus (Common squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=9521;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11165305; DOI=10.1016/s0022-3956(00)00035-2;
RA Patel P.D., Lopez J.F., Lyons D.M., Burke S., Wallace M., Schatzberg A.F.;
RT "Glucocorticoid and mineralocorticoid receptor mRNA expression in squirrel
RT monkey brain.";
RL J. Psychiatr. Res. 34:383-392(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00407}. Note=Cytoplasmic and nuclear in
CC the absence of ligand, nuclear after ligand-binding. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus, being restricted to the
CC more superficial cortical layers.
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:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF245224; AAF63382.1; -; mRNA.
DR AlphaFoldDB; Q9N0W8; -.
DR SMR; Q9N0W8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR001723; Nuclear_hrmn_rcpt.
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; PR00398; STRDHORMONER.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Steroid-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..982
FT /note="Mineralocorticoid receptor"
FT /id="PRO_0000053686"
FT DOMAIN 724..962
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 602..667
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 602..622
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 638..662
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..601
FT /note="Modulating"
FT REGION 230..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..723
FT /note="Hinge"
FT REGION 682..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..783
FT /note="Important for coactivator binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 345..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 622
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 638
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 768
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 768
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 768
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 774
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 774
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 774
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 815
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 815
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 815
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 943
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 943
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 943
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VII8"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VII8"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VII8"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VII8"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VII8"
SQ SEQUENCE 982 AA; 107084 MW; E90C37E3302BC046 CRC64;
METKGYHSLP EGLDMERRWG QVSQAVEHSS LGSTERTDEN NYMEIVNVSC VSGAIPNNST
QGSSKEKHEL LPCLQQDNNR PGILTSDIKT ELESKELSAT VAESMGLYMD SVRDADYYEQ
QNQQRSMSPA KIYQNVEQLV KFYKENGHRP STLSCVNRPL RSFMSDSVSS VNGGVMRAIV
KSPIMCHEKS PSVCSPLNMT SSVCSPAGIN SVSSTTASFG SFPVHSPITQ GTPLTCSPNV
ENRGSRSHSP AHASNVGSPL SSPLSSMKSS ISSPPSHCSV KSPVSSPNNV TPRSSVSSPA
NINNSRCSVS SPSNTNNRST LSSPAASTVG SICSPVNNAF SYTASGTSAG SSTSRDVVPS
PDTQEKGAQE VPFPKTEEVE SAISNGVTGQ LNIVQYIKPE PDGAFSSSCL GGNSKINSDS
PFSVPIKQES TKHSCSGTSF KGNPTVNPFP FMDGSYFSFM DDKDYYSLSG ILGPPVPGFD
GTCEGSGFPV GIKQEPDDGS YYPEASIPSS AIVGVNSGGQ SFHYRIGAQG TISLSRSARD
QSFQHLSSFP PVNTLVESWK SHGDLSSRRS DGYPVLEYIP ENVSSSTLRS VSTGSSRPSK
ICLVCGDEAS GCHYGVVTCG SCKVFFKRAV EGQHNYLCAG RNDCIIDKIR RKNCPACRLQ
KCLQAGMNLG ARRSKKLGKL KGIHEEQPQQ QPPPPPPPPQ SPEEGTTYIA PAKEPSVNTA
LVPQLSAISR ALTPSPAMVL ENIEPEVVYA GYDNSKPDTA ENLLSTLNRL AGKQMIQVVK
WAKVLPGFKN LPLEDQITLI QYSWMCLSSF ALSWRSYKHT NSQFLYFAPD LVFNEEKMHQ
SAMYELCQGM HQISLQFIRL QLTFEEYTIM KVLLLLSTVP KDGLKSQAAF EEMRTNYIKE
LRKMVTKCPN NSGQSWQRFY QLTKLLDSMH DLVNDLLEFC FYTFRESQAL KVEFPAMLVE
IISDQLPKVE SGNAKPLYFH RK
