Swiss-Prot entry

ID   MCR_ONCMY      STANDARD;      PRT;   359 AA.
AC   Q9IAC6;
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   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; 
OC   Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. 
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis;
RX   MEDLINE=20264048; PubMed=10802282 [NCBI, ExPASy, EBI, Israel, Japan]; 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
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   -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear in the absence of
CC       ligand; nuclear after ligand-binding (By 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   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
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; AF209873; AAF61206.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P06536; 1GDC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q9IAC6; 1-51.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00398; STRDHORMONER.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q9IAC6.
DR   ProtoNet; Q9IAC6.
DR   ProtoMap; Q9IAC6.
DR   PRESAGE; Q9IAC6.
DR   DIP; Q9IAC6.
DR   ModBase; Q9IAC6.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   DNA-binding; Metal-binding; Nuclear protein; Receptor;
KW   Steroid-binding; Trans-acting factor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   NON_TER       1      1
FT   DNA_BIND     <1     49       Nuclear receptor-type.
FT   ZN_FING      13     37       C4-type.
FT   DOMAIN       50    107       Hinge.
FT   DOMAIN      108    359       Steroid-binding.
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
//