Swiss-Prot entry
ID ESR2_SHEEP STANDARD; PRT; 527 AA.
AC Q9TU15; Q9N0T6;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Estrogen receptor beta (ER-beta).
GN Name=ESR2; Synonyms=NR3A2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS BETA AND BETA-1).
RC TISSUE=Ovary;
RX MEDLINE=21313342; PubMed=11420232 [NCBI, ExPASy, EBI, Israel, Japan];
RA Cardenas H., Burke K.A., Bigsby R.M., Pope W.F., Nephew K.P.;
RT "Estrogen receptor beta in the sheep ovary during the estrous cycle
RT and early pregnancy.";
RL Biol. Reprod. 65:128-134(2001).
CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an
CC affinity similar to that of ESR1, and activates expression of
CC reporter genes containing estrogen response elements (ERE) in an
CC estrogen-dependent manner.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with
CC ESR1. Interacts with NCOA3, NCOA5 and NCOA6 coactivators, leading
CC to a strong increase of transcription of target genes. Binds UBE1C
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=Beta;
CC IsoId=Q9TU15-1; Sequence=Displayed;
CC Name=Beta-1;
CC IsoId=Q9TU15-2; Sequence=VSP_003700, VSP_003701;
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; AF177936; AAD55772.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF257109; AAF71745.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; Q9UHD3; 1QKM. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9TU15; 141-213, 259-498.
DR GO; GO:0005634; C:nucleus; ISS.
DR GO; GO:0030284; F:estrogen receptor activity; ISS.
DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; ISS.
DR GO; GO:0048019; F:receptor antagonist activity; ISS.
DR GO; GO:0005496; F:steroid binding; ISS.
DR GO; GO:0030520; P:estrogen receptor signaling pathway; ISS.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; ISS.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR000324; VitD_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 PIRSF; PIRSF002527; ER-ab; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00350; VITAMINDR.
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; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9TU15.
DR ProtoNet; Q9TU15.
DR ProtoMap; Q9TU15.
DR PRESAGE; Q9TU15.
DR DIP; Q9TU15.
DR ModBase; Q9TU15.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Alternative splicing; DNA-binding; Nuclear protein; Phosphorylation;
KW Receptor; Steroid-binding; Transcription; Transcription regulation;
KW Zinc-finger.
FT DOMAIN 1 145 Modulating.
FT DNA_BIND 146 211 Nuclear receptor-type.
FT ZN_FING 146 166 C4-type.
FT ZN_FING 182 206 C4-type.
FT DOMAIN 212 527 Steroid-binding.
FT MOD_RES 84 84 Phosphoserine (By similarity).
FT MOD_RES 485 485 Phosphotyrosine (By similarity).
FT VARSPLIC 316 324 FVELSLYDQ -> MKGNVLKEF (in isoform Beta-
FT 1).
FT /FTId=VSP_003700.
FT VARSPLIC 325 527 Missing (in isoform Beta-1).
FT /FTId=VSP_003701.
SQ SEQUENCE 527 AA; 59120 MW; 9CD7A3E89497EDEA CRC64;
MDVKNSPSSL NSPVSYNCGQ SILPLEPGPI YLPSSYVESR HEYSAVTFYS PAVMNYSIPN
NSEDGPGRQT TSPNVLWPTP GHLSPLAIHC QSSLLYAEPQ KSPWCETRSL EHTFPVNRET
LKRKASGSSC ASPVSSPSSK RDAHFCAVCS DYASGYHYGV WSCEGCKAFF KRSIQGHNDY
ICPATNQCTI DKNRRKSCQA CRLRKCYEVG MVKCGSRRER CGYRIVRRQR NSDEQLHCLS
KTKRNGAPMT RVKELLLSAL SPEQLVLTLL EAEPPHVLMS RPSAPFTEAS MMMSLTKLAD
KELVHMISWA KKIPGFVELS LYDQVRLLES CWLEVLMVGL MWRSIDHPGK LIFAPDLVLD
RDEGKCVEGI LEIFDMLLAT TSRFRELKLQ HKEYLCVKAM ILLNSSMYPS ATASQEADSG
RKLTHLLNAV TDALVWVIAK SGMSSQQQSM RLANLLMLLS HVRHASNKGM EHLLNMKCKN
VVPVYDLLLE MLNAHTLRSN KPLVTRSERN LAEDSESKEG SQKPQAQ
//