ID F1D8Q5_HUMAN Unreviewed; 462 AA. AC F1D8Q5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 24-JAN-2024, entry version 100. 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=NR2B1 {ECO:0000313|EMBL:ADZ17354.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ADZ17354.1}; RN [1] {ECO:0000313|EMBL:ADZ17354.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Kidney {ECO:0000313|EMBL:ADZ17354.1}; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RT "Isolation of cDNA coding for multiple human nuclear receptor clones."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. 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}. 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; HQ692843; ADZ17354.1; -; mRNA. DR RefSeq; NP_002948.1; NM_002957.5. DR SMR; F1D8Q5; -. DR Antibodypedia; 3881; 545 antibodies from 41 providers. DR DNASU; 6256; -. DR GeneID; 6256; -. DR KEGG; hsa:6256; -. DR CTD; 6256; -. DR VEuPathDB; HostDB:ENSG00000186350; -. DR HOGENOM; CLU_007368_5_4_1; -. DR OMA; NAVSHIC; -. DR OrthoDB; 5400963at2759; -. DR BioGRID-ORCS; 6256; 72 hits in 1198 CRISPR screens. DR ChiTaRS; RXRA; human. DR GenomeRNAi; 6256; -. DR ExpressionAtlas; F1D8Q5; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. 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 2: Evidence at transcript level; 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 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}. SQ SEQUENCE 462 AA; 50811 MW; 7F952B580AD84C42 CRC64; MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT //