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

 MCR_ONCMY               Reviewed;         359 AA.
Q9IAC6;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 93.
RecName: Full=Mineralocorticoid receptor;
Short=MR;
AltName: Full=Nuclear receptor subfamily 3 group C member 2;
Flags: Fragment;
Name=nr3c2; Synonyms=mlr;
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
NCBI_TaxID=8022;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=10802282; DOI=10.1016/S0039-128X(00)00090-8;
Colombe L., Fostier A., Bury N., Pakdel F., Guiguen Y.;
"A mineralocorticoid-like receptor in the rainbow trout, Oncorhynchus
mykiss: cloning and characterization of its steroid binding domain.";
Steroids 65:319-328(2000).
-!- FUNCTION: Receptor for both mineralocorticoids (MC) such as
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 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00407}. Note=Cytoplasmic and
nuclear in the absence of ligand, nuclear after ligand-binding.
{ECO:0000250}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
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EMBL; AF209873; AAF61206.1; -; mRNA.
UniGene; Omy.11644; -.
ProteinModelPortal; Q9IAC6; -.
SMR; Q9IAC6; -.
HOVERGEN; HBG073125; -.
SABIO-RK; Q9IAC6; -.
GO; GO:0045177; C:apical part of cell; IDA:AgBase.
GO; GO:1990794; C:basolateral part of cell; IDA:AgBase.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IMP:AgBase.
GO; GO:0016020; C:membrane; IMP:AgBase.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:1903878; F:11-deoxycorticosterone binding; IMP:AgBase.
GO; GO:1903876; F:11-deoxycortisol binding; IMP:AgBase.
GO; GO:1903879; F:11beta-hydroxyprogesterone binding; IMP:AgBase.
GO; GO:1903880; F:17alpha-hydroxyprogesterone binding; IMP:AgBase.
GO; GO:1903877; F:21-deoxycortisol binding; IMP:AgBase.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
GO; GO:1903875; F:corticosterone binding; IMP:AgBase.
GO; GO:1903794; F:cortisol binding; IMP:AgBase.
GO; GO:0031963; F:cortisol receptor activity; IDA:AgBase.
GO; GO:0098531; F:transcription factor activity, direct ligand regulated sequence-specific DNA binding; IDA:AgBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
GO; GO:0051414; P:response to cortisol; IDA:AgBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.565.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
2: Evidence at transcript level;
Cytoplasm; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
Receptor; Steroid-binding; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN <1 359 Mineralocorticoid receptor.
/FTId=PRO_0000053689.
DNA_BIND <1 49 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 13 37 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 50 107 Hinge.
REGION 108 359 Steroid-binding.
REGION 157 160 Important for coactivator binding.
{ECO:0000250}.
BINDING 145 145 Steroid. {ECO:0000250}.
BINDING 151 151 Steroid. {ECO:0000250}.
BINDING 192 192 Steroid. {ECO:0000250}.
BINDING 320 320 Steroid. {ECO:0000250}.
NON_TER 1 1
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


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