ESR1_SALSA
ID ESR1_SALSA Reviewed; 535 AA.
AC P50242;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Estrogen receptor;
DE Short=ER;
DE AltName: Full=ER-alpha;
DE AltName: Full=Estradiol receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 1;
DE Flags: Fragment;
GN Name=esr1; Synonyms=esr, nr3a1;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10818271; 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 the
CC 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-beta
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highest expression in brain and liver.
CC {ECO:0000269|PubMed:10818271}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; X89959; CAA61999.1; -; mRNA.
DR PIR; S58224; S58224.
DR AlphaFoldDB; P50242; -.
DR SMR; P50242; -.
DR STRING; 8030.ENSSSAP00000015760; -.
DR Proteomes; UP000087266; Genome assembly.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:1903924; F:estradiol binding; ISS:AgBase.
DR GO; GO:0042562; F:hormone binding; IEA:UniProt.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISS:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032355; P:response to estradiol; ISS:AgBase.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR001292; Estr_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02159; Oest_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500101; ER-a; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..535
FT /note="Estrogen receptor"
FT /id="PRO_0000053637"
FT DOMAIN 237..473
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 105..170
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 105..125
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 141..165
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION <1..104
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..236
FT /note="Hinge"
FT REGION 187..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
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
