ID A0A068BFV6_MOUSE Unreviewed; 482 AA. AC A0A068BFV6; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 17-JUN-2020, entry version 34. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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 Harrison E.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {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}; RX PubMed=26618355; RA Logunova N., Korotetskaya M., Polshakov V., Apt A.; RT "The QTL within the H2 Complex Involved in the Control of Tuberculosis RT Infection in Mice Is the Classical Class II H2-Ab1 Gene."; RL PLoS Genet. 11:E1005672-E1005672(2015). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334, CC ECO:0000256|SAAS:SAAS01037405}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. CC {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS01037406}. 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 MGI; MGI:98215; Rxrb. DR ChiTaRS; Rxrb; mouse. DR GO; GO:0042025; C:host cell nucleus; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; 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; IPR035500; NHR-like_dom_sf. 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 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; 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|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00476383}; KW Metal-binding {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS00116612}; KW Nucleus {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS01037386}; KW Receptor {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS01037471, KW ECO:0000313|EMBL:AIC84029.1}; KW Transcription {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS01037363}; KW Transcription regulation {ECO:0000256|RuleBase:RU004334, KW ECO:0000256|SAAS:SAAS01037387}; KW Zinc {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00476357}; KW Zinc-finger {ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00476458}. FT DOMAIN 151..226 FT /note="Nuclear receptor" FT /evidence="ECO:0000259|PROSITE:PS51030" FT DOMAIN 245..478 FT /note="NR LBD" FT /evidence="ECO:0000259|PROSITE:PS51843" FT REGION 1..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 225..247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 262..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..52 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..82 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..104 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..119 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..241 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //