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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-Experimental evidence at protein leveli

Functioni

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (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.By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi140 – 205Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri140 – 160NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 200NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • retinoic acid receptor binding Source: RGD
  • sequence-specific DNA binding Source: InterPro
  • steroid hormone receptor activity Source: RGD
  • transcription factor activity, sequence-specific DNA binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • axon regeneration Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • female pregnancy Source: RGD
  • inflammatory response Source: RGD
  • liver development Source: RGD
  • midgut development Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • placenta development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • regulation of myelination Source: RGD
  • regulation of transcription, DNA-templated Source: RGD
  • response to ethanol Source: RGD
  • response to glucocorticoid Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to retinoic acid Source: RGD
  • response to selenium ion Source: RGD
  • response to vitamin A Source: RGD
  • response to vitamin D Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
Gene namesi
Name:Rxra
Synonyms:Nr2b1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3610. Rxra.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • axon Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535681 – 467Retinoic acid receptor RXR-alphaAdd BLAST467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 residuei264PhosphoserineBy similarity1
Modified residuei265Phosphoserine; by MAPK8 and MAPK9By similarity1

Post-translational modificationi

Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser-22 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265. Phosphorylated on Ser-28, in vitro, by PKA. 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).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ05343.
PRIDEiQ05343.

PTM databases

iPTMnetiQ05343.
PhosphoSitePlusiQ05343.

Interactioni

Subunit structurei

Homodimer (By similarity). Heterodimer with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity (By similarity). Interacts with NCOA3 and NCOA6 coactivators. Interacts with FAM120B. Interacts with PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Heterodimerizes with PPARG (By similarity). Interacts with PRMT2 (By similarity). Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity. Interacts with ASXL1. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, MED1, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 and NCOA1 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • retinoic acid receptor binding Source: RGD

Protein-protein interaction databases

MINTiMINT-138446.
STRINGi10116.ENSRNOP00000012892.

Chemistry databases

BindingDBiQ05343.

Structurei

3D structure databases

ProteinModelPortaliQ05343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 139ModulatingBy similarityAdd BLAST139
Regioni206 – 229HingeBy similarityAdd BLAST24
Regioni230 – 467Ligand-bindingBy similarityAdd BLAST238

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.

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

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

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiQ05343.
PhylomeDBiQ05343.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. 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.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:iAF86A74FD05BD470
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06482 mRNA. Translation: AAA42093.1.
PIRiA47278.
I67427.
UniGeneiRn.108206.

Genome annotation databases

UCSCiRGD:3610. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06482 mRNA. Translation: AAA42093.1.
PIRiA47278.
I67427.
UniGeneiRn.108206.

3D structure databases

ProteinModelPortaliQ05343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-138446.
STRINGi10116.ENSRNOP00000012892.

Chemistry databases

BindingDBiQ05343.
ChEMBLiCHEMBL4431.

PTM databases

iPTMnetiQ05343.
PhosphoSitePlusiQ05343.

Proteomic databases

PaxDbiQ05343.
PRIDEiQ05343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3610. rat.

Organism-specific databases

RGDi3610. Rxra.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiQ05343.
PhylomeDBiQ05343.

Miscellaneous databases

PROiQ05343.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. 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.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRXRA_RAT
AccessioniPrimary (citable) accession number: Q05343
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.