RARB_NOTVI
ID RARB_NOTVI Reviewed; 158 AA.
AC P18515;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Retinoic acid receptor beta;
DE Short=RAR-beta;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 2;
DE Flags: Fragment;
GN Name=RARB; Synonyms=NR1B2;
OS Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Notophthalmus.
OX NCBI_TaxID=8316;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2536901; DOI=10.1038/337566a0;
RA Giguere V., Ong E.S., Evans R.M., Tabin C.J.;
RT "Spatial and temporal expression of the retinoic acid receptor in the
RT regenerating amphibian limb.";
RL Nature 337:566-569(1989).
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). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with a RXR molecule. Binds DNA preferentially as
CC a RAR/RXR heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
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 PIR; S02758; S02758.
DR AlphaFoldDB; P18515; -.
DR SMR; P18515; -.
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; 3.30.50.10; -; 1.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR003078; Retinoic_acid_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01292; RETNOICACIDR.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00399; ZnF_C4; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..>158
FT /note="Retinoic acid receptor beta"
FT /id="PRO_0000053471"
FT DOMAIN 129..>158
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 31..106
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 34..54
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 70..94
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 158
SQ SEQUENCE 158 AA; 18204 MW; D18B6B003BF6D767 CRC64;
RHSAQSIETQ STSSEELVPS PPSPLPPPRV YKPCFVCQDK SSGYHYGVSA CEGCKGFFRR
SIQKNMIYTC HRDKNCVINK VTRNRCQYCR LQRCFEVGMS KESVRNDRNK KKKEPIKQEC
IESLEMTAEL DDLTEKIRKA HQETFPSLCQ LGKYTTNS
