ID A0A3B4X783_SERLL Unreviewed; 627 AA.
AC A0A3B4X783;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Estrogen receptor {ECO:0000256|ARBA:ARBA00015934, ECO:0000256|PIRNR:PIRNR002527};
DE Short=ER {ECO:0000256|PIRNR:PIRNR002527};
DE AltName: Full=ER-alpha {ECO:0000256|ARBA:ARBA00031973, ECO:0000256|PIRNR:PIRNR002527};
DE AltName: Full=Estradiol receptor {ECO:0000256|ARBA:ARBA00031699, ECO:0000256|PIRNR:PIRNR002527};
DE AltName: Full=Nuclear receptor subfamily 3 group A member 1 {ECO:0000256|ARBA:ARBA00032418, ECO:0000256|PIRNR:PIRNR002527};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000011657.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000011657.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00003830, ECO:0000256|PIRNR:PIRNR002527}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-beta.
CC {ECO:0000256|ARBA:ARBA00026005}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR002527}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000256|ARBA:ARBA00005413,
CC ECO:0000256|PIRNR:PIRNR002527}.
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DR AlphaFoldDB; A0A3B4X783; -.
DR STRING; 1841481.ENSSLDP00000011657; -.
DR Ensembl; ENSSLDT00000012080.1; ENSSLDP00000011657.1; ENSSLDG00000009247.1.
DR GeneTree; ENSGT00940000158133; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042562; F:hormone binding; IEA:UniProt.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd07171; NR_DBD_ER; 1.
DR CDD; cd06949; NR_LBD_ER; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR001292; Estr_rcpt.
DR InterPro; IPR046944; Estr_rcpt_N.
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 PANTHER; PTHR48092:SF16; ESTROGEN RECEPTOR; 1.
DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002527};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW ECO:0000256|PIRNR:PIRNR002527};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR002527};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR002527};
KW Steroid-binding {ECO:0000256|ARBA:ARBA00022665,
KW ECO:0000256|PIRNR:PIRNR002527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR002527};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR002527}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 185..260
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 314..550
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 68661 MW; EE99F702E4F2991A CRC64;
MLLRQSPGQN RQPSGSVLRP RISPAFSKLE TLSPPRLSPP PHVPLSDMYP EESRGSGGVA
TVDFLEGTYD YAAPTPAPTP LYSHSTTGYY SAPLDAHGPP PDGSLQSLGS GPTSPIVFVP
SSPRLSPIMH PPSHHYLETT STPVYRSSQQ PASREDHCGT SDESYSVGES GAGSGAGLFE
MAKETCFCAV CSDYASGYHY GVWSCEGCKA FFKRSIQGHN DYMCPATNQC TIDRNRRKSC
QACRLRKCYE VGMMKGGMRK DRSRVLRPDK RRTGTSDKDK ASKDQEHRRV HLQEGRKHSS
SSTGGGKSSV TGTPPDQVLL LLQGAEPPIL CSHQKLSRPY TEVTIMTLLT SMADKELVHM
ITWAKKLPGF LQLSLHDQVQ LLESSWLEVL MIGLIWRSIH CPGKLIFAQD LILDRNEGDC
VEGMAEIFDM LLATASRFRM LKLKPEEFVC LKAIILLNSG SFSFCTGTME PLHDGTAVQD
MLDTITDALI HHISQSGCSV QQQSRRQAQL LLLLSHIRHM SNKGMEHLYS MKCKNKVPLY
DLLLEMLDAH RLNRPEKPAQ SWFLADKEPS TTSSSSNNNN NNNSSSGSSS AGSSSGPRGS
HESLSRAPTG PGVLQYGGSC SDCTHIL
//
