MCR_ONCMY
ID MCR_ONCMY Reviewed; 359 AA.
AC Q9IAC6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Mineralocorticoid receptor;
DE Short=MR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 2;
DE Flags: Fragment;
GN Name=nr3c2; Synonyms=mlr;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10802282; DOI=10.1016/s0039-128x(00)00090-8;
RA Colombe L., Fostier A., Bury N., Pakdel F., Guiguen Y.;
RT "A mineralocorticoid-like receptor in the rainbow trout, Oncorhynchus
RT mykiss: cloning and characterization of its steroid binding domain.";
RL Steroids 65:319-328(2000).
CC -!- FUNCTION: Receptor for both mineralocorticoids (MC) such as cortisol.
CC Binds to mineralocorticoid response elements (MRE) and transactivates
CC target genes. The effect of MC is to increase ion and water transport
CC and thus raise extracellular fluid volume and blood pressure and lower
CC potassium 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}.
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DR EMBL; AF209873; AAF61206.1; -; mRNA.
DR AlphaFoldDB; Q9IAC6; -.
DR SMR; Q9IAC6; -.
DR PRIDE; Q9IAC6; -.
DR SABIO-RK; Q9IAC6; -.
DR GO; GO:0045177; C:apical part of cell; IDA:AgBase.
DR GO; GO:1990794; C:basolateral part of cell; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IMP:AgBase.
DR GO; GO:0016020; C:membrane; IMP:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:1903878; F:11-deoxycorticosterone binding; IMP:AgBase.
DR GO; GO:1903876; F:11-deoxycortisol binding; IMP:AgBase.
DR GO; GO:1903879; F:11beta-hydroxyprogesterone binding; IMP:AgBase.
DR GO; GO:1903880; F:17alpha-hydroxyprogesterone binding; IMP:AgBase.
DR GO; GO:1903877; F:21-deoxycortisol binding; IMP:AgBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:1903875; F:corticosterone binding; IMP:AgBase.
DR GO; GO:1903794; F:cortisol binding; IMP:AgBase.
DR GO; GO:0098531; F:ligand-activated transcription factor activity; IDA:AgBase.
DR GO; GO:0031963; F:nuclear cortisol receptor activity; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
DR GO; GO:0051414; P:response to cortisol; IDA:AgBase.
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 SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN <1..359
FT /note="Mineralocorticoid receptor"
FT /id="PRO_0000053689"
FT DOMAIN 108..339
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND <1..49
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 13..37
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 48..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..107
FT /note="Hinge"
FT REGION 157..160
FT /note="Important for coactivator binding"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 145
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 145
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 145
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 151
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 151
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 151
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 192
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 192
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 192
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 320
FT /ligand="21-hydroxyprogesterone"
FT /ligand_id="ChEBI:CHEBI:16973"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 320
FT /ligand="aldosterone"
FT /ligand_id="ChEBI:CHEBI:27584"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT BINDING 320
FT /ligand="progesterone"
FT /ligand_id="ChEBI:CHEBI:17026"
FT /evidence="ECO:0000250|UniProtKB:P08235"
FT NON_TER 1
SQ SEQUENCE 359 AA; 40284 MW; E10983C5109C89A6 CRC64;
FKRAVEGQHN YLCAGRNDCI IDKIRRKNCP ACRVRKCLQA GMNLGARKSK KPGKLKGVNE
DSTPTKEGGQ TCPGSGGGYL SSGEKELSTS PTNALVPHGP GGGLVTPYLP PSICSVLELI
EPEVVFAGYD NTQPDTTDHL LSSLNQLAGK QMIRVVKWAK VLPGFRGLPI EDQITLIQYS
WMCLSSFSLS WRSYKHTNGQ MLYFAPDLVF NEDRMQQSAM YDLCLGMRQV SQEFVRLQLT
YQEFLSMKVL LLLSTVPKEG LKNQAAFEEM RVNYIKELRR SVGKAPTTLD RRGNRSSQLT
KLLDAMHDLG GELLDFCFYT FRESQALKVE FPEMLVEIIS DQIPKVESGN THTLYFHKK
