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Database: UniProt
Entry: F6ZBP3_ORNAN
LinkDB: F6ZBP3_ORNAN
Original site: F6ZBP3_ORNAN 
ID   F6ZBP3_ORNAN            Unreviewed;       461 AA.
AC   F6ZBP3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Retinoic acid receptor RXR {ECO:0000256|RuleBase:RU369010};
DE   AltName: Full=Nuclear receptor subfamily 2 group B member {ECO:0000256|RuleBase:RU369010};
GN   Name=RXRA {ECO:0000313|Ensembl:ENSOANP00000006191.4};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000006191.4, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000006191.4, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000006191.4,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000006191.4}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000006191.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC       factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC       and binds to target response elements in response to their ligands,
CC       all-trans or 9-cis retinoic acid, to regulate gene expression in
CC       various biological processes. {ECO:0000256|RuleBase:RU369010}.
CC   -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule.
CC       {ECO:0000256|RuleBase:RU369010}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC       {ECO:0000256|RuleBase:RU369010}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000256|ARBA:ARBA00006421}.
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DR   AlphaFoldDB; F6ZBP3; -.
DR   STRING; 9258.ENSOANP00000006191; -.
DR   Ensembl; ENSOANT00000006193.4; ENSOANP00000006191.4; ENSOANG00000003910.4.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000159789; -.
DR   HOGENOM; CLU_007368_5_4_1; -.
DR   InParanoid; F6ZBP3; -.
DR   OMA; NAVSHIC; -.
DR   TreeFam; TF352097; -.
DR   Proteomes; UP000002279; Chromosome 4.
DR   Bgee; ENSOANG00000003910; Expressed in liver and 8 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0050692; F:DNA binding domain binding; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0050693; F:LBD domain binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042809; F:nuclear vitamin D receptor binding; IEA:Ensembl.
DR   GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR   GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR   GO; GO:0044323; F:retinoic acid-responsive element binding; IBA:GO_Central.
DR   GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR   GO; GO:0070644; F:vitamin D response element binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IBA:GO_Central.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd06956; NR_DBD_RXR; 1.
DR   CDD; cd06943; NR_LBD_RXR_like; 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; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR021780; Nuc_recep-AF1.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24083:SF39; RETINOIC ACID RECEPTOR RXR-ALPHA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF11825; Nuc_recep-AF1; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00545; RETINOIDXR.
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|RuleBase:RU004334};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004334};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004334};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU004334};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT   DOMAIN          131..206
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          226..457
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  50657 MW;  3C5FE937E2DC1777 CRC64;
     MDTKHFLPLD FSTQVNSTSL NSPTGRGPMA APSLHPSLGP GIGSSLGSPI STLSSPINGM
     GPPFSVISSP MGPHSMSVPT TPTLGFGTGS PQLNSPMNPV SSTEDIKPPL GLNGVLKVPA
     HPSGTMASFT KHICAICGDR SSGKHYGVYS CEGCKGFFKR TVRKDLTYTC RDNKDCLIDK
     RQRNRCQYCR YQKCLAMGMK REAVQEERQR GKDRNENEVE STSSANEDMP VEKILEAELA
     VEPKTETYIE ANMGLNPNSP NDPVTNICQA ADKQLFTLVE WAKRIPHFSE LPLDDQVILL
     RAGWNELLIA SFSHRSIAVK DGILLATGLH VHRNSAHSAG VGAIFDRVLT ELVSKMRDMQ
     MDKTELGCLR AIVLFNPDSK GLSNPAEVEA LREKVYASLE AYCKHKYPDQ PGRFAKLLLR
     LPALRSIGLK CLEHLFFFKL IGDTPIDTFL MEMLEAPHQM T
//
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