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UniProtKB - Q05343 (RXRA_RAT)

Entry version 175 (23 Feb 2022)
Sequence version 1 (01 Feb 1994)
Previous versions | rss
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Protein

Retinoic acid receptor RXR-alpha

Gene

Rxra

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor for retinoic acid that acts as a transcription factor (By similarity).

Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (By similarity).

The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (By similarity).

The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (By similarity).

In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (By similarity).

On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (By similarity).

Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (By similarity).

The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (By similarity).

The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (PubMed:8381967).

Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity).

Acts as an enhancer of RARA binding to RARE DNA element (By similarity).

May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (By similarity).

Promotes myelin debris phagocytosis and remyelination by macrophages (By similarity).

Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes (By similarity).

Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (By similarity).

By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi140Zinc 1By similarity1
Metal bindingi143Zinc 1By similarity1
Metal bindingi157Zinc 1By similarity1
Metal bindingi160Zinc 1By similarity1
Metal bindingi176Zinc 2By similarity1
Metal bindingi182Zinc 2By similarity1
Metal bindingi192Zinc 2By similarity1
Metal bindingi195Zinc 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei3219-cis retinoic acidBy similarity1
Binding sitei3329-cis retinoic acid; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi140 – 205Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri140 – 160NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 200NR C4-typePROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-159418, Recycling of bile acids and salts
R-RNO-192105, Synthesis of bile acids and bile salts
R-RNO-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-RNO-193807, Synthesis of bile acids and bile salts via 27-hydroxycholesterol
R-RNO-200425, Carnitine metabolism
R-RNO-204174, Regulation of pyruvate dehydrogenase (PDH) complex
R-RNO-211976, Endogenous sterols
R-RNO-381340, Transcriptional regulation of white adipocyte differentiation
R-RNO-383280, Nuclear Receptor transcription pathway
R-RNO-400206, Regulation of lipid metabolism by PPARalpha
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-5362517, Signaling by Retinoic Acid
R-RNO-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
R-RNO-9616222, Transcriptional regulation of granulopoiesis
R-RNO-9623433, NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis
R-RNO-9707564, Cytoprotection by HMOX1

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rxra
Synonyms:Nr2b1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		3610, Rxra

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4431

DrugCentral

More...DrugCentrali		Q05343

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000535681 – 467Retinoic acid receptor RXR-alphaAdd BLAST467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei22PhosphoserineBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei61Phosphoserine; by MAPK8 and MAPK9By similarity1
Modified residuei75Phosphoserine; by MAPK8 and MAPK9By similarity1
Modified residuei87Phosphothreonine; by MAPK8 and MAPK9By similarity1
Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei134PhosphoserineBy similarity1
Modified residuei150N6-acetyllysineBy similarity1
Modified residuei264PhosphoserineBy similarity1
Modified residuei265Phosphoserine; by MAPK8 and MAPK9By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain (By similarity). Constitutively phosphorylated on Ser-22 in the presence or absence of ligand (By similarity). Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265 (By similarity). Phosphorylated on Ser-28, in vitro, by PKA (By similarity). This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity).By similarity
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.By similarity
Acetylated by EP300; acetylation enhances DNA binding and transcriptional activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q05343

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q05343

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q05343

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the adrenal gland with main expression in the zona fasciculata and medulla (at protein level) (PubMed:28267642). Expressed in aortic endothelial cells, with high expression in the descending thoracic aorta and the outer curvature of the aortic arch, where pulsatory shear stress exists, but very low in the inner curvature of the aortic arch, where oscillatory shear stress prevails (at protein level) (PubMed:28167758).2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Heterodimer (via C-terminus) with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity; association with RARA is enhanced by pulsatile shear stress (By similarity). Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity (By similarity). Heterodimerizes with PPARG (By similarity). Heterodimerizes (via NR LBD) with RARB (By similarity). Heterodimerizes with NR1H4; the heterodimerization enhances the binding affinity for LXXLL motifs from coactivators (By similarity).

Interacts with NCOA3 and NCOA6 coactivators (By similarity).

Interacts with FAM120B (By similarity).

Interacts with coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8 (By similarity).

Interacts with PRMT2 (By similarity).

Interacts with ASXL1 (By similarity).

Interacts with BHLHE40/DEC1, BHLHE41/DEC2, MED1, NCOR1 and NCOR2 (By similarity).

Interacts in a ligand-dependent fashion with MED1 and NCOA1 (By similarity).

Interacts with VDR (By similarity).

Interacts with EP300; the interaction is decreased by 9-cis retinoic acid (By similarity). Heterodimer (via C-terminus) with NR4A1 (DNA-binding domain); the interaction is enhanced by 9-cis retinoic acid (By similarity). NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA (By similarity). In the absence of hormonal ligand, interacts with TACC1 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000012892

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q05343

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q05343

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q05343

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini232 – 463NR LBDPROSITE-ProRule annotationAdd BLAST232

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 139ModulatingBy similarityAdd BLAST139
Regioni1 – 61DisorderedSequence analysisAdd BLAST61
Regioni79 – 109DisorderedSequence analysisAdd BLAST31
Regioni165 – 170Nuclear localization signalBy similarity6
Regioni206 – 229HingeBy similarityAdd BLAST24
Regioni211 – 233DisorderedSequence analysisAdd BLAST23
Regioni353 – 373Required for nuclear exportBy similarityAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi9 – 28Polar residuesSequence analysisAdd BLAST20
Compositional biasi79 – 108Polar residuesSequence analysisAdd BLAST30
Compositional biasi211 – 227Basic and acidic residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of three domains: a modulating N-terminal or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or AF2 domain.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the nuclear hormone receptor family. NR2 subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri140 – 160NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 200NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q05343

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q05343

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.565.10, 1 hit
3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035500, NHR-like_dom_sf
IPR021780, Nuc_recep-AF1
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001723, Nuclear_hrmn_rcpt
IPR000003, Retinoid-X_rcpt/HNF4
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00104, Hormone_recep, 1 hit
PF11825, Nuc_recep-AF1, 1 hit
PF00105, zf-C4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00545, RETINOIDXR
PR00398, STRDHORMONER
PR00047, STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00430, HOLI, 1 hit
SM00399, ZnF_C4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48508, SSF48508, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51843, NR_LBD, 1 hit
PS00031, NUCLEAR_REC_DBD_1, 1 hit
PS51030, NUCLEAR_REC_DBD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q05343-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTKHFLPLD FSTQVNSSSL SSPTGRGSMA APSLHPSLGP GLGSPLGSPG 
        60         70         80         90        100
QLHSPISTLS SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFETGSPQLN 
       110        120        130        140        150
SPMNPVSSSE DIKPPLGLNG VLKVPAHPSG NMSSFTKHIC AICGDRSSGK 
       160        170        180        190        200
HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK DCLIDKRQRN RCQYCRYQKC 
       210        220        230        240        250
LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI LEAELAVEPK 
       260        270        280        290        300
TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD 
       310        320        330        340        350
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI 
       360        370        380        390        400
FDRVLTELVS KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK 
       410        420        430        440        450
VYASLEAYCK HKYPEQPGRF AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT 
       460 
PIDTFLMEML EAPHQTT
Length:467
Mass (Da):51,266
Last modified:February 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAF86A74FD05BD470
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q0VJ96Q0VJ96_RAT
Retinoic acid receptor RXR-alpha
Rxra rCG_45555
467Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L06482 mRNA Translation: AAA42093.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47278
I67427

Genome annotation databases

UCSC genome browser

More...UCSCi		RGD:3610, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06482 mRNA Translation: AAA42093.1
PIRiA47278
I67427

3D structure databases

BMRBiQ05343
SMRiQ05343
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012892

Chemistry databases

BindingDBiQ05343
ChEMBLiCHEMBL4431
DrugCentraliQ05343

PTM databases

iPTMnetiQ05343
PhosphoSitePlusiQ05343

Proteomic databases

PaxDbiQ05343

Genome annotation databases

UCSCiRGD:3610, rat

Organism-specific databases

RGDi3610, Rxra

Phylogenomic databases

eggNOGiKOG3575, Eukaryota
InParanoidiQ05343
PhylomeDBiQ05343

Enzyme and pathway databases

ReactomeiR-RNO-159418, Recycling of bile acids and salts
R-RNO-192105, Synthesis of bile acids and bile salts
R-RNO-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-RNO-193807, Synthesis of bile acids and bile salts via 27-hydroxycholesterol
R-RNO-200425, Carnitine metabolism
R-RNO-204174, Regulation of pyruvate dehydrogenase (PDH) complex
R-RNO-211976, Endogenous sterols
R-RNO-381340, Transcriptional regulation of white adipocyte differentiation
R-RNO-383280, Nuclear Receptor transcription pathway
R-RNO-400206, Regulation of lipid metabolism by PPARalpha
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-5362517, Signaling by Retinoic Acid
R-RNO-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
R-RNO-9616222, Transcriptional regulation of granulopoiesis
R-RNO-9623433, NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis
R-RNO-9707564, Cytoprotection by HMOX1

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q05343

Family and domain databases

Gene3Di1.10.565.10, 1 hit
3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500, NHR-like_dom_sf
IPR021780, Nuc_recep-AF1
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001723, Nuclear_hrmn_rcpt
IPR000003, Retinoid-X_rcpt/HNF4
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA
PfamiView protein in Pfam
PF00104, Hormone_recep, 1 hit
PF11825, Nuc_recep-AF1, 1 hit
PF00105, zf-C4, 1 hit
PRINTSiPR00545, RETINOIDXR
PR00398, STRDHORMONER
PR00047, STROIDFINGER
SMARTiView protein in SMART
SM00430, HOLI, 1 hit
SM00399, ZnF_C4, 1 hit
SUPFAMiSSF48508, SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843, NR_LBD, 1 hit
PS00031, NUCLEAR_REC_DBD_1, 1 hit
PS51030, NUCLEAR_REC_DBD_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRXRA_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05343
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 23, 2022
This is version 175 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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