RXRAA_DANRE
ID RXRAA_DANRE Reviewed; 430 AA.
AC A2T929; Q1L677;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Retinoic acid receptor RXR-alpha-A;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 1-A;
DE AltName: Full=RXRalpha-B;
DE AltName: Full=Retinoid X receptor alpha-A;
GN Name=rxraa {ECO:0000312|ZFIN:ZDB-GENE-070314-2}; Synonyms=nr2b1a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABM89229.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-312, AND DEVELOPMENTAL STAGE.
RX PubMed=17195188; DOI=10.1002/dvdy.21049;
RA Waxman J.S., Yelon D.;
RT "Comparison of the expression patterns of newly identified zebrafish
RT retinoic acid and retinoid X receptors.";
RL Dev. Dyn. 236:587-595(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAY85284.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-430.
RA Bertrand S., Sachs L., Bardet P.-L., Bonnelye E., Dufraisse M., Escriva H.,
RA Haramis A.-P., Marchand O., Safi R., Vanacker J.-M., Zelus D., Thisse C.,
RA Thisse B., Laudet V.;
RT "Nuclear receptors expression during zebrafish development reveals an
RT unsuspected link with nervous system and retina development.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17997606; DOI=10.1371/journal.pgen.0030188;
RA Bertrand S., Thisse B., Tavares R., Sachs L., Chaumot A., Bardet P.-L.,
RA Escriva H., Duffraisse M., Marchand O., Safi R., Thisse C., Laudet V.;
RT "Unexpected novel relational links uncovered by extensive developmental
RT profiling of nuclear receptor expression.";
RL PLoS Genet. 3:E188-E188(2007).
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC and binds to target response elements in response to their ligands,
CC all-trans or 9-cis retinoic acid, to regulate gene expression in
CC 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 to regulate transcription. The high affinity
CC ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the
CC rar/rxr heterodimers associate with a multiprotein complex containing
CC transcription corepressors that induce histone deacetylation, chromatin
CC condensation and transcriptional suppression. On ligand binding, the
CC corepressors dissociate from the receptors and coactivators are
CC recruited leading to transcriptional activation.
CC {ECO:0000250|UniProtKB:P19793}.
CC -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule. Binds DNA
CC preferentially as a rar/rxr heterodimer.
CC {ECO:0000250|UniProtKB:P19793}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. In the
CC embryo, expressed in the posterior hindbrain and anterior spinal cord
CC at the 5-somite stage, with expression increasing through to the 15-
CC somite stage. At the 15-somite stage, also expressed in the tail bud
CC region. At the 18-somite stage, also found in the third neural crest
CC stream. {ECO:0000269|PubMed:17195188, ECO:0000269|PubMed:17997606}.
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. NR2
CC subfamily. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM89229.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF028132; ABM89229.1; ALT_INIT; mRNA.
DR EMBL; DQ017629; AAY85284.1; -; mRNA.
DR AlphaFoldDB; A2T929; -.
DR SMR; A2T929; -.
DR STRING; 7955.ENSDARP00000104454; -.
DR PaxDb; A2T929; -.
DR PeptideAtlas; A2T929; -.
DR PRIDE; A2T929; -.
DR ZFIN; ZDB-GENE-070314-2; rxraa.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; A2T929; -.
DR PhylomeDB; A2T929; -.
DR Reactome; R-DRE-159418; Recycling of bile acids and salts.
DR Reactome; R-DRE-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-DRE-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DRE-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-DRE-200425; Carnitine metabolism.
DR Reactome; R-DRE-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DRE-211976; Endogenous sterols.
DR Reactome; R-DRE-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DRE-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DRE-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-DRE-5362517; Signaling by Retinoic Acid.
DR Reactome; R-DRE-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-DRE-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-DRE-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR PRO; PR:A2T929; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; 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:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IBA:GO_Central.
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; IPR021780; Nuc_recep-AF1.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF11825; Nuc_recep-AF1; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
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..430
FT /note="Retinoic acid receptor RXR-alpha-A"
FT /id="PRO_0000287896"
FT DOMAIN 195..426
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 100..175
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 103..123
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..158
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..99
FT /note="Modulating"
FT /evidence="ECO:0000250|UniProtKB:P10276"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..133
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 174..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..192
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT REGION 316..336
FT /note="Required for nuclear export"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 415..426
FT /note="AF-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 284
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 284
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 295
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 295
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
SQ SEQUENCE 430 AA; 47471 MW; 362DBD748A24191F CRC64;
MHPSLLSPTS LGPSGSLHSP ISTLSSPMNG LGSPFSVISS PMGPHSMASP GVGYGPSISP
QLNSHMNSVS SSEDIKPPLG LNGVMKVPAQ PSGTPLSLTK HICAICGDRS SGKHYGVYSC
EGCKGFFKRT VRKDLTYTCR DNKDCVIDKR QRNRCQYCRY QKCLAMGMKR EAVQEERQRA
KERSENEVES TSSANEDMPV EKILEAELAV EPKTETYIET NVPMPSNSPN DPVTNICQAA
DKQLFTLVEW AKRIPHFSEL PLDDQVILLR AGWNELLIAS FSHRSIAVKD GILLATGLHV
HRNSAHSAGV GAIFDRVLTE LVSKMRDMQM DKTELGCLRA IVLFNPDSKG LSNPGEVEAL
REKVYASLEA YCKHKYPEQP GRFAKLLLRL PALRSIGLKC LEHLFFFKLI GDTPIDTFLM
EMLEAPHQMT
