Swiss-Prot entry
ID ESR1_SALSA STANDARD; PRT; 535 AA.
AC P50242;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Estrogen receptor (ER) (Estradiol receptor) (ER-alpha) (Fragment).
GN Name=ESR1; Synonyms=ESR, NR3A1;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Euteleostei;
OC Protacanthopterygii; Salmoniformes; Salmonidae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX MEDLINE=20362504; PubMed=10818271 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0305-0491(99)00184-4;
RA Rogers S.A., Llewellyn L., Wigham T., Sweeney G.E.;
RT "Cloning of the Atlantic salmon (Salmo salar) estrogen receptor-alpha
RT gene.";
RL Comp. Biochem. Physiol. 125B:379-385(2000).
CC -!- FUNCTION: The steroid hormones and their receptors are involved in
CC the regulation of eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-
CC beta (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- TISSUE SPECIFICITY: Highest expression in brain and liver.
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.
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DR EMBL; X89959; CAA61999.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S58224; S58224.
DR HSSP; P03372; 1UOM. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P50242; 101-172.
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 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; P50242.
DR ProtoNet; P50242.
DR ProtoMap; P50242.
DR PRESAGE; P50242.
DR DIP; P50242.
DR ModBase; P50242.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT NON_TER 1 1
FT DOMAIN <1 104 Modulating (Potential).
FT DNA_BIND 105 170 Nuclear receptor-type.
FT ZN_FING 105 125 C4-type.
FT ZN_FING 141 165 C4-type.
FT DOMAIN 171 236 Hinge.
FT DOMAIN 237 535 Steroid-binding (Potential).
SQ SEQUENCE 535 AA; 58900 MW; 669F13D7B243B612 CRC64;
SRMLTDPPRI GSMQSLGSSP TGPLVFVSSS PQLSPFLHPP GHHGLPSQSY YLETSSTPLY
RSSVVTNQLS ASEEKLCITS NRQQSYAAAG SGVRVFEMAN ETRYCAVCSD FASGYHYGFW
SCEGCKAFFK RSIQGHNDYM CPATNQCTMD RNRRKSCQAC RLRKCYEVGM VKGGLRKDRG
GRVLRKDKRY CGPAGDREKP YGDLEHRTAP PQDGGRNSSS SSLSGGGGWC GPRITMPPEQ
VLFLLQGAEP PALCSRQKVA RPYTEVTMMT LLTSMADKEL VHMIAWAKKV PGFQELSLHD
QVQLLESSWL EVLMIGLIWR SIHCPGKLIF AQDLILDRSE GDCVEGMAEI FDMLLATVSR
FRMLKLKPEE FVCLKAIILL NSGAFSFCSN SVESLHNSSA VESMLDNITD ALIHHISHSG
ASVQQQPRRQ VQLLLLLSHI RHMSNKGMEH LYSIKCKNKV PLYDLLLEML DGHRLQSPGK
VAQAGEQTEG PSTTTTTSTG SSIGPMRGSQ DTHIRSPGSG VLQYGSPSSD QMPIP
//