ESR2_ICTPU
ID ESR2_ICTPU Reviewed; 575 AA.
AC Q9IAK1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Estrogen receptor beta;
DE Short=ER-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 2;
GN Name=esr2; Synonyms=nr3a2;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10753576; DOI=10.1006/gcen.1999.7447;
RA Xia Z., Gale W.L., Chang X., Langenau D., Patino R., Maule A.G.,
RA Densmore L.D.;
RT "Phylogenetic sequence analysis, recombinant expression, and tissue
RT distribution of a channel catfish estrogen receptor beta.";
RL Gen. Comp. Endocrinol. 118:139-149(2000).
CC -!- FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha,
CC and activates expression of reporter genes containing estrogen response
CC elements (ERE) in an estrogen-dependent manner.
CC {ECO:0000250|UniProtKB:Q92731}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-alpha
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ovary and testis.
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; AF185568; AAF63157.1; -; mRNA.
DR RefSeq; NP_001187012.1; NM_001200083.1.
DR AlphaFoldDB; Q9IAK1; -.
DR SMR; Q9IAK1; -.
DR STRING; 7998.ENSIPUP00000034555; -.
DR GeneID; 100304489; -.
DR KEGG; ipu:100304489; -.
DR CTD; 317733; -.
DR SABIO-RK; Q9IAK1; -.
DR Proteomes; UP000221080; Chromosome 3.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0042562; F:hormone binding; IDA:AgBase.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:AgBase.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:AgBase.
DR GO; GO:0017046; F:peptide hormone binding; IDA:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:1990239; F:steroid hormone binding; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:InterPro.
DR GO; GO:0008406; P:gonad development; TAS:AgBase.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009410; P:response to xenobiotic stimulus; TAS:AgBase.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR021064; ER-beta-like_N.
DR InterPro; IPR028355; ER-beta/gamma.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
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; PF12497; ERbeta_N; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500102; ER-b; 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 Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..575
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053654"
FT DOMAIN 290..526
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 161..226
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 161..181
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 197..221
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..160
FT /note="Modulating"
FT REGION 108..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63907 MW; E3863C6AB8EB824F CRC64;
MSSSLSPTLQ TVNGMDQDEP LPLFPSHYPT ALGVDRGTVC IPSPYADNGH AEMSFCGPSA
PENPAIAPPL SPSLFWSSHN PHAMPALPLH CPPALPYSEP HIHTAWVDTK PHTSGRHSSF
LSRPKLFGKR PEDGDGDEAL DDDDPSSSSS GAVVKRDMHF CVVCHDYASG YHYGVWSCEG
CKAFFKRSIQ GHNDYICPAT NQCTIDKNRR KSCQACRLRK CYEMGMMKCG ARRERCGYRA
SRRTAPMRDG SARPVGVRGQ SQRLPHTPLH VSLSIPVSRA SAESGFSGLS PEQLVYCILE
AEPPQIYLKQ QMKKPYTEST VMMSLTQLAD KELVLMISWA KKIPGFVELS LAHQVQLLEC
CWLEVLMLGL MWRSIDHPGK LIFSLDLKLN RDEGNCVEGI MEIFDMLLAG SSRFRELKLQ
KEEYVCLKAL ILLNSSMYMT SSACEKDLES RTKLLRLLDA VTDALVWAIS RTGLSTQQQS
ARLAHLLMLL SHIRHLSNKG MEHLSSMKRK NVVLLYDLLL EMLDANMAQS RHVSTSVCTD
PVTPATSPNT PLPPQLHSPV AHHVTQVNES QCSQE
