MCR_TUPBE
ID MCR_TUPBE Reviewed; 977 AA.
AC Q29131; Q95268;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=37347;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9582428; DOI=10.1016/s0169-328x(98)00004-7;
RA Meyer U., Kruhoeffer M., Flugge G., Fuchs E.;
RT "Cloning of glucocorticoid receptor and mineralocorticoid receptor cDNA and
RT gene expression in the central nervous system of the tree shrew (Tupaia
RT belangeri).";
RL Brain Res. Mol. Brain Res. 55:243-253(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-431.
RC TISSUE=Colon;
RA Kruhoeffer M., Klingenberg M., Fuchs E., Forssmann W.-G.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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 -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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; Z75077; CAA99376.1; -; mRNA.
DR EMBL; X83607; CAA58586.1; -; mRNA.
DR AlphaFoldDB; Q29131; -.
DR SMR; Q29131; -.
DR PRIDE; Q29131; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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 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..977
FT /note="Mineralocorticoid receptor"
FT /id="PRO_0000053690"
FT DOMAIN 719..957
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 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..718
FT /note="Hinge"
FT REGION 682..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..778
FT /note="Important for coactivator binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Basic and acidic 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 763
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 763
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 763
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 769
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 769
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 769
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 810
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 810
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 810
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 938
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 938
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 938
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
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"
SQ SEQUENCE 977 AA; 106489 MW; 63387CFBF104155F CRC64;
METKGYHSRP EGLDMERRWG QVSQPVDRPS LGPAERTEEN NYMEIVNVSC VSGAIPNNST
QGSSKEKQEL LPCLQQDNTQ SGILTSEIKT ELEPKELSAT VAESMGLYMD SVREADYAFE
QHAQQGSLSP AKIYQNVEQL MKFYKENGHR SSTLSNVSRP SRSFLPDPGS AVNGGVMRAM
VKSPILCHEK SPSVCSPLNM TSSVCSPAGI NSVSSTTVRF GSFPVHSPIT QGTPLTCSPT
VDNRGSRSHS PAHASNVGSP LSSPLSSMKS PISSPPSHCS VKSPVSSPNN VTLRSCVSSP
ANINNSRCSV SSPSKANNRS TLSSPAASTV GSICSPNAFS YPASGASVGS SATRDVIPSP
DTHEKGAHEV PFPKTEEVEN AISNGVTGQL NIVQYIKPEP DGAFSSSCLG GNSKIHSDSP
FSSVPIKQES TKHSCSGASF KGNPTVNPFP FMDGSYFSFM DDKDYYSLSG ILGPPVPGFE
GNCEGTGFPM GIKQEPDYGI YYPEASIPSS AIVGVNSGGQ SFHYRIGAQG TISLSRSARD
QSFQHLSSFP PVNTLVESWK SHGDLSARKI DGYPVLEYIP ENVSSSTLRS VSTGSSRPSK
ICLVCGDGAS GCHYGVVTCG SCKVFFKRAV EGQHNYLCAG RNDCIIDKIR RKNCPACRLQ
KCLQAGMNLG ARKSKKLGKL KGLHEEQPQQ PPPPQSPEEG TTYIAPAKEP SVNTALVPQL
SSISRALTPS PVMVLENIEP EIVYAGYDSS KPDTAENLLS TLNRLAGKQM IQVVKWAKVL
PGFKNLPLED QITLIQYSRM CLSSFALSWR SYKHTNSQFF YFAPDLVFNE EKMHQSAMYE
LCQGMHQISL QFVRLQFTFE EYTFMEVLLL LSTIPKDGLK SQAAFEEMRA NYIKELRKMV
TKCPNNSGQS WQGFYQLTKF LDSMHDLVSD LLEFCFYTFR ELQALKVEFP AMLVEIISDQ
LPKVESGNAK PLYFHRK
