Swiss-Prot entry
ID ESR2_BOVIN STANDARD; PRT; 527 AA.
AC Q9XSB5; Q9TTS2;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Holstein; TISSUE=Ovarian follicle;
RX MEDLINE=99150196; PubMed=10026117 [NCBI, ExPASy, EBI, Israel, Japan];
RA Rosenfeld C.S., Yuan X., Manikkam M., Calder M.D., Garverick H.A.,
RA Lubahn D.B.;
RT "Cloning, sequencing, and localization of bovine estrogen receptor-
RT beta within the ovarian follicle.";
RL Biol. Reprod. 60:691-697(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 4-527.
RX MEDLINE=99359179; PubMed=10432221 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0303-7207(99)00064-7;
RA Walther N., Lioutas C., Tillmann G., Ivell R.;
RT "Cloning of bovine estrogen receptor beta (Erbeta): expression of
RT novel deleted isoforms in reproductive tissues.";
RL Mol. Cell. Endocrinol. 152:37-45(1999).
CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an
CC affinity similar to that of ESR1 (ER-alpha), and activates
CC expression of reporter genes containing estrogen response elements
CC (ERE) in an estrogen-dependent manner. May play a role in ovarian
CC follicular growth and maturation.
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 -!- TISSUE SPECIFICITY: Present in granulosa cells of antral follicles
CC in various stages of follicular growth.
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; AF110402; AAD24432.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; Y18017; CAB53861.1; ALT_INIT. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; Q9UHD3; 1NDE. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9XSB5; 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; Q9XSB5.
DR ProtoNet; Q9XSB5.
DR ProtoMap; Q9XSB5.
DR PRESAGE; Q9XSB5.
DR DIP; Q9XSB5.
DR ModBase; Q9XSB5.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW Steroid-binding; Transcription; Transcription regulation; 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 CONFLICT 60 60 N -> D (in Ref. 2).
SQ SEQUENCE 527 AA; 59032 MW; 9CEFFE106F4E4C84 CRC64;
MDVKNSPSSL NSPVSYNCGQ SILPLEPGPI YLPSSYVESR HEYSAVTFYS PAVMNYSIPN
NSEDGPGRQT TSPNVLWPTP GHLSPLAIHC QPSVLYAEPQ KSPWRETRSL EHTLPVNRET
LKRKASGSSC ASPATSPSSK RDAHFCAVCS DYASGYHYGV WSCEGCKAFF KRSIQGHNDY
ICPATNQCTI DKNRRKSCQA CRLRKCYEVG MVKCGSRRER CGYRIVRRQR NSDEQLHCLS
KTKRNGGPMT RVKELLLSAL SPEQLVLTLL EAEPPHVLIS RPSTPFTEAS MMMSLTKLAD
KELVHMISWA KKIPGFVELS LYDQVRLLES CWLEVLMVGL MWRSIDHPGK LIFAPDLILD
RDEGKCVEGI LEIFDMLLAT TSRFRELKLQ HKEYLCVKAM ILLNSSMYPS ATAPQEADSG
RKLTHLLNAV TDALVWVIAK SGMSSQQQSM RLANLLMLLS HVRHASNKGM EHLLNMKCKN
VVPVYDLLLE MLNAHTLRGN KSLVTGSERN LVEDSESKEG SQKPQAQ
//