RXRB_RAT
ID RXRB_RAT Reviewed; 458 AA.
AC P49743;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Retinoic acid receptor RXR-beta;
DE AltName: Full=Nuclear receptor coregulator 1;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 2;
DE AltName: Full=Retinoid X receptor beta;
DE Flags: Fragment;
GN Name=Rxrb; Synonyms=Nr2b2, Rcor-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC TISSUE=Thyroid;
RX PubMed=1662118; DOI=10.1016/0092-8674(91)90301-e;
RA Yu V.C., Delsert C., Andersen B., Holloway J.M., Devary O.V., Naeaer A.M.,
RA Kim S.Y., Boutin J.-M., Glass C.K., Roesenfeld M.G.;
RT "RXR beta: a coregulator that enhances binding of retinoic acid, thyroid
RT hormone, and vitamin D receptors to their cognate response elements.";
RL Cell 67:1251-1266(1991).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28267642; DOI=10.1016/j.jsbmb.2017.03.002;
RA Cheng B., Al-Shammari F.H., Ghader I.A., Sequeira F., Thakkar J.,
RA Mathew T.C.;
RT "Fundamental studies of adrenal retinoid-X-receptor: Protein isoform,
RT tissue expression, subcellular distribution, and ligand availability.";
RL J. Steroid Biochem. Mol. Biol. 171:110-120(2017).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE). {ECO:0000269|PubMed:1662118}.
CC -!- SUBUNIT: Homodimer (in vitro) (By similarity). Heterodimer with other
CC retinoic acid receptor family members. Binds DNA preferentially as a
CC RAR/RXR heterodimer (PubMed:1662118). Interacts with NR1H3 (By
CC similarity). Interacts with AKAP13 (By similarity).
CC {ECO:0000250|UniProtKB:P28702, ECO:0000250|UniProtKB:P28704,
CC ECO:0000269|PubMed:1662118}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28267642}. Cytoplasm
CC {ECO:0000269|PubMed:28267642}.
CC -!- TISSUE SPECIFICITY: Expressed in the adrenal gland with main expression
CC in the zona fasciculata (at protein level).
CC {ECO:0000269|PubMed:28267642}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42025.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M81766; AAA42025.1; ALT_INIT; mRNA.
DR PIR; A41651; A41651.
DR AlphaFoldDB; P49743; -.
DR SMR; P49743; -.
DR STRING; 10116.ENSRNOP00000040499; -.
DR BindingDB; P49743; -.
DR ChEMBL; CHEMBL2805; -.
DR PhosphoSitePlus; P49743; -.
DR PaxDb; P49743; -.
DR PeptideAtlas; P49743; -.
DR PRIDE; P49743; -.
DR UCSC; RGD:3611; rat.
DR RGD; 3611; Rxrb.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P49743; -.
DR PhylomeDB; P49743; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-RNO-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-RNO-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:RGD.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:RGD.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:RGD.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001893; P:maternal placenta development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN <1..458
FT /note="Retinoic acid receptor RXR-beta"
FT /id="PRO_0000053574"
FT DOMAIN 221..454
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 130..195
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 130..150
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 166..190
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION <1..129
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..220
FT /note="Hinge"
FT REGION 201..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 458 AA; 49078 MW; 22D11956B11DB4BE CRC64;
GEAGRDGMGD TGRDSRSPDS SSPNPLSQGI PPSSPPGPPH TPSAPPPPMP PPPLGSPFPV
ISSSMGSPGL PPPAPPGFSG PVSSPQINST VSLPGGGSGP PEDVKPPVLG VRGLHCPPPP
GGPGAGKRLC AICGDRSSGK HYGVYSCEGC KGFFKRTIRK DLTYSCRDNK DCTVDKRQRN
RCQYCRYQKC LATGMKREAV QEERQRGKDK DGDGDGAGGA PEEMPVDRIL EAELAVEQKS
DQGVEGPGAT GGGGSSPNDP VTNICQAADK QLFTLVEWAK RIPHFSSLPL DDQVILLRAG
WNELLIASFS HRSIDVRDGI LLATGLHVHR NSAHSAGVGA IFDRVLTELV SKMRDMRMDK
TELGCLRAII LFNPDAKGLS NPGEVEILRE KVYASLETYC KQKYPEQQGR FAKLLLRLPA
LRSIGLKCLE HLFFFKLIGD TPIDTFLMEM LEAPHQLA
