ESR1_CHICK
ID ESR1_CHICK Reviewed; 589 AA.
AC P06212;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 163.
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;
GN Name=ESR1; Synonyms=ESR, NR3A1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3755102; DOI=10.1002/j.1460-2075.1986.tb04300.x;
RA Krust A., Green S., Argos P., Kumar V., Walter P., Bornert J.-M.,
RA Chambon P.;
RT "The chicken oestrogen receptor sequence: homology with v-erbA and the
RT human oestrogen and glucocorticoid receptors.";
RL EMBO J. 5:891-897(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2901032; DOI=10.1210/mend-1-1-25;
RA Maxwell B.L., McDonnell D.P., Conneely O.M., Schulz T.Z., Greene G.L.,
RA O'Malley B.W.;
RT "Structural organization and regulation of the chicken estrogen receptor.";
RL Mol. Endocrinol. 1:25-35(1987).
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. The
CC modulating domain, also known as A/B or AF-1 domain has a ligand-
CC independent transactivation function. The C-terminus contains a ligand-
CC dependent transactivation domain, also known as E/F or AF-2 domain
CC which overlaps with the ligand binding domain. AF-1 and AF-2 activate
CC transcription independently and synergistically and act in a
CC promoter- and cell-specific manner (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC thought to be weakly associated with nuclear components; hormone
CC binding greatly increases receptor affinity. The hormone-receptor
CC complex appears to recognize discrete DNA sequences upstream of
CC transcriptional start sites.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; X03805; CAA27433.1; -; mRNA.
DR PIR; A40914; QRCHE.
DR RefSeq; NP_990514.1; NM_205183.2.
DR AlphaFoldDB; P06212; -.
DR SMR; P06212; -.
DR STRING; 9031.ENSGALP00000042556; -.
DR PaxDb; P06212; -.
DR GeneID; 396099; -.
DR KEGG; gga:396099; -.
DR CTD; 2099; -.
DR VEuPathDB; HostDB:geneid_396099; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P06212; -.
DR OrthoDB; 487299at2759; -.
DR PhylomeDB; P06212; -.
DR PRO; PR:P06212; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:AgBase.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:AgBase.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF12743; ESR1_C; 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; PR00543; OESTROGENR.
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..589
FT /note="Estrogen receptor"
FT /id="PRO_0000053625"
FT DOMAIN 305..541
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 179..244
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 179..199
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 215..239
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..178
FT /note="Modulating (transactivation AF-1)"
FT REGION 245..304
FT /note="Hinge"
FT REGION 251..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..589
FT /note="Transactivation AF-2"
FT /evidence="ECO:0000250"
FT REGION 549..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 257
FT /note="E -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66746 MW; 1B092233C770A54B CRC64;
MTMTLHTKAS GVTLLHQIQG TELETLSRPQ LKIPLERSLS DMYVESNKTG VFNYPEGATY
DFGTTAPVYG STTLSYAPTS ESFGSSSLAG FHSLNNVPPS PVVFLQTAPQ LSPFIHHHSQ
QVPYYLENEQ GSFGMREAAP PAFYRPSSDN RRHSIRERMS STNEKGSLSM ESTKETRYCA
VCNDYASGYH YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ CTIDKNRRKS CQACRLRKCY
EVGMMKGGIR KDRRGGEMMK QKRQREEQDS RNGEASSTEL RAPTLWTSPL VVKHNKKNSP
ALSLTAEQMV SALLEAEPPI VYSEYDPNRP FNEASMMTLL TNLADRELVH MINWAKRVPG
FVDLTLHDQV HLLECAWLEI LMIGLVWRSM EHPGKLLFAP NLLLDRNQGK CVEGMVEIFD
MLLATAARFR MMNLQGEEFV CLKSIILLNS GVYTFLSSTL KSLEERDYIH RVLDKITDTL
IHLMAKSGLS LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY NMKCKNVVPL YDLLLEMLDA
HRLHAPAARS AAPMEEENRN QLTTAPASSH SLQSFYINSK EEESMQNTI
