Swiss-Prot entry

ID   MCR_PIG        STANDARD;      PRT;   164 AA.
AC   P79404;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Mineralocorticoid receptor (MR) (Fragment).
GN   Name=NR3C2; Synonyms=MLR;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; 
OC   Sus. 
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Large white; TISSUE=Kidney;
RA   Perreau V., Moisan M.P.;
RT   "Sus scrofa mineralocorticoid receptor partial cDNA; hormone binding
RT   domain.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for both mineralocorticoids (MC) such as
CC       aldosterone and glucocorticoids (GC) such as corticosterone or
CC       cortisol. Binds to mineralocorticoid response elements (MRE) and
CC       transactivates target genes. The effect of MC is to increase ion
CC       and water transport and thus raise extracellular fluid volume and
CC       blood pressure and lower potassium levels (By similarity).
CC   -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70,
CC       and FKBP4, in the absence of ligand. After ligand binding, it
CC       translocates to the nucleus and binds to DNA as a homodimer and as
CC       a heterodimer with NR3C1. Binds the coactivator NCOA2. May
CC       interact with HSD11B2 in the absence of ligand. Binds the
CC       coactivators NCOA1, TIF1 and NRIP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear in the absence of
CC       ligand; nuclear after ligand-binding. When bound to HSD11B2, it is
CC       found associated with the endoplasmic reticulum membrane (By
CC       similarity).
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal steroid-binding domain.
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U88893; AAB53273.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P06401; 1A28. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; Graphical view of domain structure.
DR   SMART; SM00430; HOLI; 1.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P79404.
DR   ProtoNet; P79404.
DR   ProtoMap; P79404.
DR   PRESAGE; P79404.
DR   DIP; P79404.
DR   ModBase; P79404.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW   Steroid-binding; Trans-acting factor; Transcription;
KW   Transcription regulation.
FT   NON_TER       1      1
FT   DOMAIN       <1   >164       Steroid-binding.
FT   NON_TER     164    164
SQ   SEQUENCE   164 AA;  19695 MW;  AE97ADF1C32F8BBE CRC64;
     QYSWMCLSSF ALSWRSYKHT NSQFLYFAPD LVFNEEKMHQ SAMYELCQGM HQISLQFVRL
     QLTFEEYTIM KVLLLLSTIP KDGLKSQAAF EEMRTNYIKE LRKMVTRCPN NSGQSWQRFY
     QLTKLLDSMH DLVSDLLEFC FYTFRESQAL KVEFPRCWWR SSPT
//