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ESR3_MICUN
ID   ESR3_MICUN              Reviewed;         565 AA.
AC   P57783;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Estrogen receptor gamma;
DE            Short=ER-gamma;
DE   AltName: Full=Nuclear receptor subfamily 3 group A member 3;
GN   Name=esr3; Synonyms=nr3a3;
OS   Micropogonias undulatus (Atlantic croaker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Micropogonias.
OX   NCBI_TaxID=29154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=11005855; DOI=10.1073/pnas.97.20.10751;
RA   Hawkins M.B., Thornton J.W., Crews D., Skipper J.K., Dotte A., Thomas P.;
RT   "Identification of a third distinct estrogen receptor and reclassification
RT   of estrogen receptors in teleosts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10751-10756(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: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Abundant in the ovary and testes, barely detectable
CC       in the brain and muscle and undetectable in the liver.
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; AF298182; AAG16712.1; -; mRNA.
DR   AlphaFoldDB; P57783; -.
DR   SMR; P57783; -.
DR   PRIDE; P57783; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042562; F:hormone binding; IEA:UniProt.
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; IEA:UniProtKB-KW.
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   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..565
FT                   /note="Estrogen receptor gamma"
FT                   /id="PRO_0000053659"
FT   DOMAIN          286..516
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        169..234
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         169..189
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         205..229
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..168
FT                   /note="Modulating"
FT   REGION          235..285
FT                   /note="Hinge"
FT   REGION          522..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62903 MW;  D9954D2F740CCA5E CRC64;
     MAVASSPEKD QPLLQLQKVD SSRVGGQVLS PTLSSSLETS QPICITSPYT DLGHDFPTIP
     FYSPTIFSYA GPSISDCTSV HQSLNPSLFW PSRGHMGSPI PLHHSQHGQP IQSPWVEISP
     LDNVLKTKQD GASLPLAVVP VRHKSARRRS QESEEAVVTS GGKTDLHYCA VCHDYASGYH
     YGVWSCEGCK AFFKRSIQRD NEYICPATNE CTIDKNRRKS CQACRLRKCY EVGMTKCGMR
     KERGNYRSPQ MRRMTRLTSQ GRTDSSSVLT GSAVVSLNAP QPSALTSEQL IERLMEAEPP
     EIYLMKDMKK PLTEAKVMMS LTNLADKELV HMITWAKKIP GFVELGLLDQ VHLLECCWLE
     VLMVGLMWRS VDHPGKLVFS PDLSLSREEG SCVQGFAEIF DMLLAATSRV RELKLQREEY
     VCLKAMILLN SNMCLSSSES SSKLLRLLDA VTDALVSAIG KTVLSFRQQY TRLAHLLMLL
     SHIRHVSNKG MDHLHCMKMK NMVPLYDLLL EMLDAHIMHS SRLPRRSPEQ EPEDQADAPA
     PPHSSGSGPS YTWTPSSSEG AGEPQ
 
 
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