RARB_COTJA
ID RARB_COTJA Reviewed; 455 AA.
AC Q9W6B3; Q910C7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Retinoic acid receptor beta;
DE Short=RAR-beta;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 2;
GN Name=RARB; Synonyms=NR1B2;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2), POSSIBLE FUNCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=11133679; DOI=10.1095/biolreprod64.1.231;
RA Fu Z., Kubo T., Sugahara K., Noguchi T., Kato H.;
RT "Cloning of complementary deoxyribonucleic acids encoding quail (Coturnix
RT coturnix japonica) retinoic acid receptor beta isoforms and changes in
RT their gene expression during gonadotropic growth.";
RL Biol. Reprod. 64:231-241(2001).
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) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5 (By similarity). May be required for Sertoli
CC cell differentiation and spermatogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with a RXR molecule. Binds DNA preferentially as
CC a RAR/RXR heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-1;
CC IsoId=Q9W6B3-1; Sequence=Displayed;
CC Name=Beta-2;
CC IsoId=Q9W6B3-2; Sequence=VSP_009096;
CC -!- TISSUE SPECIFICITY: Both isoforms expressed in heart, lung, kidney,
CC liver, brain, lung and testis. Isoform Beta-1 is highly expressed in
CC testes and brain. Levels increase during testes maturation. Isoform
CC beta-2 is predominant in heart, kidney and lung.
CC {ECO:0000269|PubMed:11133679}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF110729; AAD23397.1; -; mRNA.
DR EMBL; AF110730; AAD23398.1; -; mRNA.
DR AlphaFoldDB; Q9W6B3; -.
DR SMR; Q9W6B3; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; 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; IPR003078; Retinoic_acid_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; PR01292; RETNOICACIDR.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..455
FT /note="Retinoic acid receptor beta"
FT /id="PRO_0000053470"
FT DOMAIN 183..417
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 88..153
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 88..108
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 124..148
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..87
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 45..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..182
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 416..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..59
FT /note="MTTSSRTCPVPAVNGHMTHYPAAPYPLLFPPVIGGLSLPSLHGLQSHPPTSG
FT CSTPSPA -> MFDCMDVLAVSPAQMLDFYTASPSSCMLQEKALKACFSGLAQTEWQHR
FT HSAQ (in isoform Beta-2)"
FT /evidence="ECO:0000303|PubMed:11133679"
FT /id="VSP_009096"
SQ SEQUENCE 455 AA; 50694 MW; 608951B106C4CD41 CRC64;
MTTSSRTCPV PAVNGHMTHY PAAPYPLLFP PVIGGLSLPS LHGLQSHPPT SGCSTPSPAS
VETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
VYTCHRDKNC VINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKEPT KQESTENYEM
TAELDDLTEK IRKAHQETFP SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV
EFAKRLPGFT SLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPMKVDK LQEPLLEALK
IYIRKRRPNK PHMFPKILMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGH
EPLTPTSNGN TAEHSPSISP SSVDNSSVSQ SPMVQ
