RARA_CHICK
ID RARA_CHICK Reviewed; 460 AA.
AC Q90966; Q90967;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8619957;
RA Michaille J.J., Kanzler B., Blanchet S., Garnier J.-M., Dhouailly D.;
RT "Characterization of cDNAs encoding two chick retinoic acid receptor alpha
RT isoforms and distribution of retinoic acid receptor alpha, beta and gamma
RT transcripts during chick skin development.";
RL Int. J. Dev. Biol. 39:587-596(1995).
RN [2]
RP FUNCTION.
RX PubMed=11493540; DOI=10.1242/dev.128.12.2199;
RA Dupe V., Lumsden A.;
RT "Hindbrain patterning involves graded responses to retinoic acid
RT signalling.";
RL Development 128:2199-2208(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). Required for hindbrain
CC patterning and appears to be required for skin development.
CC {ECO:0000250, ECO:0000269|PubMed:11493540}.
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=Q90966-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=Q90966-2; Sequence=VSP_003631;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8619957}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 7-8.5 during feather
CC morphogenesis in dermal and epidermal cells. Also expressed in heart
CC from day 8.5-14.5. At later stages, when the feather follicle forms,
CC expression still abundant in the epidermis, especially in the feather
CC barb ridges. {ECO:0000269|PubMed:8619957}.
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; X73972; CAA52152.1; -; mRNA.
DR EMBL; X78335; CAA55134.1; -; mRNA.
DR PIR; I50674; I50674.
DR RefSeq; NP_989867.1; NM_204536.1. [Q90966-1]
DR AlphaFoldDB; Q90966; -.
DR SMR; Q90966; -.
DR STRING; 9031.ENSGALP00000009016; -.
DR PaxDb; Q90966; -.
DR Ensembl; ENSGALT00000051814; ENSGALP00000047963; ENSGALG00000037935. [Q90966-1]
DR GeneID; 395213; -.
DR KEGG; gga:395213; -.
DR CTD; 5914; -.
DR VEuPathDB; HostDB:geneid_395213; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159997; -.
DR InParanoid; Q90966; -.
DR OrthoDB; 1165737at2759; -.
DR PhylomeDB; Q90966; -.
DR Reactome; R-GGA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-GGA-9616222; Transcriptional regulation of granulopoiesis.
DR PRO; PR:Q90966; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000037935; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; Q90966; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0021575; P:hindbrain morphogenesis; IDA:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
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..460
FT /note="Retinoic acid receptor alpha"
FT /id="PRO_0000053463"
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 REGION 46..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..182
FT /note="Hinge"
FT REGION 418..460
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 46..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..60
FT /note="MASNSSSCPTPGGGHLNGYPVTPYAFFFPHMLGGLSPPSSLPGIQHQLPVSG
FT YSTPSPAT -> MFEGAEVAGLPPPGPLPRMDCCGPGRGCLLPQCPPPPRTAPRRAPHW
FT GASGRS (in isoform Alpha-2)"
FT /evidence="ECO:0000303|PubMed:8619957"
FT /id="VSP_003631"
SQ SEQUENCE 460 AA; 50728 MW; 99711F415E811CA2 CRC64;
MASNSSSCPT PGGGHLNGYP VTPYAFFFPH MLGGLSPPSS LPGIQHQLPV SGYSTPSPAT
VETQSTSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
VYTCHRDKNC IINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKDVP KTECSESYIV
TPEVEELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV
EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDK LQEPLLEALK
IYVRKRRPNK PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGM
DTLGGQPGGP RTGGLGPPPG SCSPSLSPSS TRSSPATHSP
