ID A0A068BFV6_MOUSE Unreviewed; 482 AA. AC A0A068BFV6; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JAN-2015, entry version 2. DE SubName: Full=Putative retinoid X receptor beta isoform 3 {ECO:0000313|EMBL:AIC84029.1}; GN Name=Rxrb {ECO:0000313|EMBL:AIC84029.1, ECO:0000313|MGI:MGI:98215}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AIC84029.1}; RN [1] {ECO:0000313|EMBL:AIC84029.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84029.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AIC84029.1}; RA Logunova N.N., Korotetskaya M.V., Apt A.S.; RT "A QTL within the H-2 complex involved in the control of tuberculosis RT infection is the classical class II H2-Ab1 gene: identification by the RT forward genetic approach."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. CC {ECO:0000256|RuleBase:RU000377}. CC -!- SIMILARITY: Contains nuclear receptor DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00116555}. 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; KJ663719; AIC84029.1; -; mRNA. DR UniGene; Mm.1243; -. DR MGI; MGI:98215; Rxrb. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. DR GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 1.10.565.10; -; 1. DR Gene3D; 3.30.50.10; -; 1. DR InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core. DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4. DR InterPro; IPR001723; Str_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR Pfam; PF00104; Hormone_recep; 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; SSF48508; SSF48508; 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|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116462}; KW Metal-binding {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116612}; KW Nucleus {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116420}; KW Receptor {ECO:0000256|RuleBase:RU004334, ECO:0000313|EMBL:AIC84029.1}; KW Transcription {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116478}; KW Transcription regulation {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116499}; KW Zinc {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00116516}; KW Zinc-finger {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116578}. SQ SEQUENCE 482 AA; 51813 MW; 21178652D6D54D83 CRC64; MSWATRPPFL PPRHAAGQCG PVGVRKEMHC GMGDSGRDSR SPDSSSPNPL SQGIRPSSPP GPPLTPSAPP PPMPPPPLGS PFPVISSSMG SPGLPPPAPP GFSGPVSSPQ INSTVSLPGG GSGPPEDVKP PVLGVRGLHC PPPPGGPGAG KRLCAICGDR SSGKHYGVYS CEGCKGFFKR TIRKDLTYSC RDNKDCTVDK RQRNRCQYCR YQKCLATGMK REAVQEERQR GKDKDGDGDG AGGAPEEMPV DRILEAELAV EQKSDQGVEG PGATGGGGSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS SLPLDDQVIL LRAGWNELLI ASFSHRSIDV RDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM RMDKTELGCL RAIILFNPDA KGLSNPGEVE ILREKVYASL ETYCKQKYPE QQGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ LA //