位置:首页 > 蛋白库 > ESR2_PIG
ESR2_PIG
ID   ESR2_PIG                Reviewed;         526 AA.
AC   Q9XSW2; Q9BDW5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 145.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RA   Kowalski A.A., Graddy L.G., Vale-Cruz D.S., Choi I., Katzenellenbogen B.S.,
RA   Simmen F.A., Simmen R.C.M.;
RT   "Molecular cloning of porcine estrogen receptor beta cDNAs and
RT   developmental expression in peri-implantation embryos.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   LaVoie H.A., DeSimone D.C.;
RT   "Cloning and expression of estrogen receptor beta isoforms from porcine
RT   ovary.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity
CC       similar to that of ESR1/ER-alpha, and activates expression of reporter
CC       genes containing estrogen response elements (ERE) in an estrogen-
CC       dependent manner. {ECO:0000250|UniProtKB:Q92731}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1.
CC       Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a
CC       strong increase of transcription of target genes. Interacts with UBE1C
CC       and AKAP13. Interacts with DNTTIP2. Interacts with CCDC62 in the
CC       presence of estradiol/E2; this interaction seems to enhance the
CC       transcription of target genes. Interacts with DNAAF4. Interacts with
CC       PRMT2. Interacts with CCAR2 (via N-terminus) in a ligand-independent
CC       manner. Interacts with RBM39, in the presence of estradiol (E2).
CC       {ECO:0000250|UniProtKB:O08537, ECO:0000250|UniProtKB:Q62986,
CC       ECO:0000250|UniProtKB:Q92731}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- PTM: Phosphorylation at Ser-84 and Ser-102 recruits NCOA1.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF164957; AAD45381.2; -; mRNA.
DR   EMBL; AF267736; AAK15151.1; -; mRNA.
DR   RefSeq; NP_001001533.1; NM_001001533.1.
DR   AlphaFoldDB; Q9XSW2; -.
DR   SMR; Q9XSW2; -.
DR   STRING; 9823.ENSSSCP00000005491; -.
DR   PaxDb; Q9XSW2; -.
DR   GeneID; 396697; -.
DR   KEGG; ssc:396697; -.
DR   CTD; 2100; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; Q9XSW2; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:InterPro.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
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:0030520; P:intracellular estrogen receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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   Activator; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..526
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053645"
FT   DOMAIN          261..494
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        146..211
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         146..166
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         182..206
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..145
FT                   /note="Modulating"
FT   REGION          502..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         84
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:O08537"
FT   MOD_RES         102
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:O08537"
FT   CONFLICT        317
FT                   /note="M -> V (in Ref. 2; AAK15151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="T -> M (in Ref. 2; AAK15151)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  58850 MW;  35CE2DF661078BF6 CRC64;
     MDIKNSPSNL NSPVSYNCSQ SVLPLEPGPI YIPSSYVESC HEYSAMTFYS PAVVNYSISS
     NSEVGPGRQA TSPNVLWPTP GHLSPLAIHC QPSLLYAEPQ KSPWCDTRSL EHTLPVNRET
     LKRKASGSSC ASPVTSPSSK RDAHFCAVCS DYASGYHYGV WSCEGCKAFF KRSIQGHNDY
     ICPATNQCTI DKNRRKSCQA CRLRKCYEVG MVKCGSRRER CGYRIVRKQR NSEGHLHCLS
     RAKKNGDHTT RVKELLLSTL SPEQLVLTLL EAEPPHVLVS RPSTPFTEAS MMMSLTKLAD
     KELVHMISWA KKIPGFMELS LYDQVRLLES CWLEVLMVGL MWRSIDHPGK LIFAPDLVLD
     RDEGKCVEGI LEIFDMLLAT TSRFRELKLQ HKEYLCVKAM ILLNSSMYPS AAAQEAESSR
     KLTHLLNAVT DALVWVIARS GISSQQQSVR LANLLMLLSH VRHASNKGTE HLLNMKCKNV
     VPVYDLLLEM LNAHTLRGNK SLVTGSERSR MEESESKEGS QKPQAQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024