RARA_NOTVI
ID RARA_NOTVI Reviewed; 458 AA.
AC P18514; Q91155;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 123.
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 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 [MRNA] (ISOFORM ALPHA-1), TISSUE SPECIFICITY, AND
RP POSSIBLE FUNCTION.
RX PubMed=2552324; DOI=10.1038/341654a0;
RA Ragsdale C.W. Jr., Petkovich M., Gates P.B., Chambon P., Brockes J.P.;
RT "Identification of a novel retinoic acid receptor in regenerative tissues
RT of the newt.";
RL Nature 341:654-657(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2), AND TISSUE SPECIFICITY.
RC TISSUE=Tail;
RX PubMed=1333589; DOI=10.1093/nar/20.21.5851;
RA Ragsdale C.W. Jr., Gates P.B., Brockes J.P.;
RT "Identification and expression pattern of a second isoform of the newt
RT alpha retinoic acid receptor.";
RL Nucleic Acids Res. 20:5851-5851(1992).
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). Retinoic acid signaling appears
CC to be involved in specifying proximal-distal axis in limb regeneration.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with an rxr molecule. Binds DNA preferentially as
CC a rar/rxr heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha-1;
CC IsoId=P18514-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=P18514-2; Sequence=VSP_003633;
CC -!- TISSUE SPECIFICITY: Expressed in forelimb, in the distal forelimb
CC blastema, kidney, liver and hindlimb blastemal mesenchymal cells.
CC {ECO:0000269|PubMed:1333589, ECO:0000269|PubMed:2552324}.
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; X17585; CAA35602.1; -; mRNA.
DR EMBL; Z14254; CAA78621.1; -; mRNA.
DR PIR; S06123; S06123.
DR PIR; S78481; S78481.
DR AlphaFoldDB; P18514; -.
DR SMR; P18514; -.
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 Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..458
FT /note="Retinoic acid receptor alpha"
FT /id="PRO_0000053465"
FT DOMAIN 183..417
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 87..152
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 87..107
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 123..147
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..86
FT /note="Modulating"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..182
FT /note="Hinge"
FT REGION 417..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 408..416
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P10276"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..59
FT /note="MASNGGSCPSSGGHMNGYPVPHYAFFFPHMLGGLSPPGSLAGIPHPLPVSAY
FT STPSPAT -> MYDSVEVSSPSPYIMIDFYSQNRACLMADKGLGHPVPFGSPIRNPHWS
FT SSSHS (in isoform Alpha-2)"
FT /evidence="ECO:0000303|PubMed:1333589"
FT /id="VSP_003633"
SQ SEQUENCE 458 AA; 50637 MW; B4370822FBAADB54 CRC64;
MASNGGSCPS SGGHMNGYPV PHYAFFFPHM LGGLSPPGSL AGIPHPLPVS AYSTPSPATI
ETQSTSSEEI VPSPPSPPPL PRIYKPCFVC QDKSSGYHYG VSACEGCKGF FRRSIQKNMV
YTCHRDKTCI INKVTRNRCQ YCRLQKCFEV GMSKESVRND RNKKKKQEAP KQECTESYII
TPEVEDLVEK VRKAHQETFP ALCQLGKYTT NNSSEERVSL DIDLWDKFSE LSTKCIIKTV
EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPD QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDK LQEPLLEALK
IYVRKRRPNK PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL
DSLTGQPPRA SSLAPPPGSC SPSLSPSSNR SSPTSHSP
