ID   RARA_XENLA              Reviewed;         458 AA.
AC   P51126;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Retinoic acid receptor alpha;
DE            Short=RAR-alpha;
DE   AltName: Full=Nuclear receptor subfamily 1 group B member 1;
GN   Name=rara; Synonyms=nr1b1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=1312717; DOI=10.1073/pnas.89.6.2321;
RA   Blumberg B., Mangelsdorf D.J., Dyck J.A., Bittner D.A., Evans R.M.,
RA   De Robertis E.M.;
RT   "Multiple retinoid-responsive receptors in a single cell: families of
RT   retinoid 'X' receptors and retinoic acid receptors in the Xenopus egg.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2321-2325(1992).
RN   [2]
RP   FUNCTION, AND HETERODIMERIZATION.
RX   PubMed=9053313; DOI=10.1242/dev.124.2.373;
RA   Blumberg B., Bolado J. Jr., Moreno T.A., Kintner C., Evans R.M.,
RA   Papalopulu N.;
RT   "An essential role for retinoid signaling in anteroposterior neural
RT   patterning.";
RL   Development 124:373-379(1997).
RN   [3]
RP   FUNCTION, AND HETERODIMERIZATION.
RX   PubMed=9053327; DOI=10.1242/dev.124.2.515;
RA   Sharpe C.R., Goldstone K.;
RT   "Retinoid receptors promote primary neurogenesis in Xenopus.";
RL   Development 124:515-523(1997).
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). Required for primary
CC       neurogenesis and for anteroposterior neural patterning. {ECO:0000250,
CC       ECO:0000269|PubMed:9053313, ECO:0000269|PubMed:9053327}.
CC   -!- SUBUNIT: Heterodimer; with an rxr molecule. Binds DNA preferentially as
CC       a rar/rxr heterodimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- DEVELOPMENTAL STAGE: It is synthesized during oogenesis and persists in
CC       the cleaving embryo at approximately constant levels until it is
CC       degraded just before gastrulation. {ECO:0000269|PubMed:1312717}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P10276}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L11445; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A41977; A41977.
DR   Proteomes; UP000186698; Genome assembly.
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:0021955; P:central nervous system neuron axonogenesis; IMP:UniProtKB.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
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   DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..458
FT                   /note="Retinoic acid receptor alpha"
FT                   /id="PRO_0000053466"
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          38..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..182
FT                   /note="Hinge"
FT   REGION          416..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           407..415
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P10276"
FT   COMPBIAS        48..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50574 MW;  4D80BB18678B1E17 CRC64;
     MSSKDNTCPP PGPGHINGFH VPHYAFFFPH MLGGMSXTGG LPGVQHQPPL SGYSTPSPAT
     IETQSTSSEE IVPSPPTPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
     VYTCHRDKNC IINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKESP KPEAIESYIL
     SPETQDLIEK VQKAHQETFP ALCQLGKYTT SFSSEQRVSL DIDLWDKFSE LSTKCIIKTV
     EFAKQLPGFT TLTIADQITL LKSACLDILI LRICTRYTPD QDTMTFSDGL TLNRTQMHNA
     GFGPLTDLVF AFANQPVPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDK LQEPLLEALK
     IYVRTRRPQK PHMFPKMLMK ITDLRTVSAK GAERVITLKM EIPGAMPLIQ EMLENSEGLD
     TLGGGASSDA PVTPVAPGSC SPSLSPSSTH SSPSTHSP