RARA_TAKRU
ID RARA_TAKRU Reviewed; 447 AA.
AC Q9W5Z3; Q9W5Z4;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
RX PubMed=10452951; DOI=10.1016/s0378-1119(99)00265-6;
RA Wentworth J.M., Schoenfeld V., Meek S., Elgar G., Brenner S.,
RA Chatterjee K.K.;
RT "Isolation and characterization of the retinoic acid receptor-alpha gene in
RT the Japanese pufferfish, F. rubripes.";
RL Gene 236:315-323(1999).
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 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=Q9W5Z3-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=Q9W5Z3-2; Sequence=VSP_003632;
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; AJ012382; CAB96754.1; -; Genomic_DNA.
DR EMBL; AJ012380; CAB96754.1; JOINED; Genomic_DNA.
DR EMBL; AJ012381; CAB43979.1; -; Genomic_DNA.
DR EMBL; AJ012380; CAB43979.1; JOINED; Genomic_DNA.
DR EMBL; AJ012378; CAB43870.1; -; mRNA.
DR EMBL; AJ012379; CAB43871.1; -; mRNA.
DR RefSeq; NP_001027925.1; NM_001032753.1. [Q9W5Z3-2]
DR AlphaFoldDB; Q9W5Z3; -.
DR SMR; Q9W5Z3; -.
DR Ensembl; ENSTRUT00000042107; ENSTRUP00000041963; ENSTRUG00000016415. [Q9W5Z3-1]
DR GeneID; 445948; -.
DR KEGG; tru:445948; -.
DR CTD; 30680; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000165576; -.
DR InParanoid; Q9W5Z3; -.
DR OrthoDB; 1165737at2759; -.
DR Proteomes; UP000005226; Chromosome 1.
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..447
FT /note="Retinoic acid receptor alpha"
FT /id="PRO_0000053464"
FT DOMAIN 175..409
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 80..145
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 80..100
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 116..140
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..79
FT /note="Modulating"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..174
FT /note="Hinge"
FT REGION 407..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 400..408
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P10276"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..52
FT /note="MAGKGNPVPGPHLNGFPVPTYSYFFPHMLGSLSPPALPGLPISGYSTPSPAT
FT -> MYESVDVVGLNPSPNPFLMMEYYNQSRGCLIPEKGLVPGAPHPYSTSIRNQHWNGS
FT NHS (in isoform Alpha-2)"
FT /evidence="ECO:0000303|PubMed:10452951"
FT /id="VSP_003632"
SQ SEQUENCE 447 AA; 49532 MW; E00630F720B1508D CRC64;
MAGKGNPVPG PHLNGFPVPT YSYFFPHMLG SLSPPALPGL PISGYSTPSP ATIETQSTSS
EEIVPSPPSP PPPPRVYKPC FVCQDKSSGY HYGVSACEGC KGFFRRSIQK NMVYTCHREK
NCIINKVTRN RCQYCRLQKC LEVGMSKESV RNDRNKKKKD EKKPECIENY VLSPDTEQMI
NRVRKAHQET FPSLCQLGKY TTTNSSERRV ALDVDLWDKF SELSTKCIIK TVEFAKQLPG
FVTLTIADQI TLLKAACLDI LILRICTRYT PEQDTMTFSD GLTLNRTQMH NAGFGPLTDL
VFAFANQLLP LEMDDAETGL LSAICLLCGD RQDLEQAEKV DILQEPLLEA LKIYVRRRRP
HKPHMFPKML MKITDLRSIS AKGAERVITL KMEIPGSMPP LIQEMLENSE GLESGATGSR
PSGAPPGSCS PSLSPSSAQS SPPTQSP
