Swiss-Prot entry
ID ESR2_CHICK STANDARD; PRT; 472 AA.
AC Q9PTU5;
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) (cERb).
GN Name=ESR2; Synonyms=NR3A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae;
OC Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=White leghorn; TISSUE=Testis;
RA Suzuki M., Mizuno S., Nakabayashi O.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds estrogens with an affinity similar to that of ER-
CC alpha, and activates expression of reporter genes containing
CC estrogen response elements (ERE) in an estrogen-dependent manner.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-
CC alpha.
CC -!- SUBCELLULAR LOCATION: Nuclear.
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; AB036415; BAA88667.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; Q9UHD3; 1L2J. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9PTU5; 100-172, 213-451.
DR Ensembl; ENSGALG00000011801; Gallus_gallus
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR007110; Ig-like.
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; Q9PTU5.
DR ProtoNet; Q9PTU5.
DR ProtoMap; Q9PTU5.
DR PRESAGE; Q9PTU5.
DR DIP; Q9PTU5.
DR ModBase; Q9PTU5.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 104 Modulating.
FT DNA_BIND 105 170 Nuclear receptor-type.
FT ZN_FING 105 125 C4-type.
FT ZN_FING 141 165 C4-type.
FT DOMAIN 171 472 Steroid-binding.
SQ SEQUENCE 472 AA; 53439 MW; A8CBBB8CACA65650 CRC64;
MAFCSPAMLN YNIASNFGDS ESASVRQTSS PSVLWSAPGH LSPLTLHCQS SLLYAEQPKS
PWCEVRPLDP VLPVTRETLK RKTNGSDCTS PIASNPGSKR DAHFCAVCSD YASGYHYGVW
SCEGCKAFFK RSIQGHNDYI CPATNQCTID KNRRKSCQAC RLRKCYEVGM MKCGSRRERC
GYRILRRHRN SEDCMGKTKK YNEAATRVKE ILLSTVSPEQ FVLTLLEAEP PNVLVSRPSK
PFTEASMMMS LTKLADKELV HMIGWAKKIP GFIDLSLYDQ VRLLESCWME VLMIGLMWRS
IDHPGKLIFA PDLVLDRDEG KCVEGILEIF DMLLAMTSRF RELKLQHKEY LCVKAMILLN
SSMFPLSPEE PESNRKLHHL LNVVTDALVW VIAKSGIPSQ QQTTRLANLL MLLSHVRHAS
NKGMEHLLSM KCKNVVPVYD LLLEMLNAHT LRGQRKSPVT HPEFEQVSHF QV
//