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Protein

Retinoic acid receptor RXR-beta

Gene

Rxrb

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).1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi130 – 195Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri130 – 150NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri166 – 190NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • 9-cis retinoic acid receptor activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • retinoic acid receptor binding Source: RGD
  • sequence-specific DNA binding Source: InterPro
  • steroid hormone receptor activity Source: InterPro
  • thyroid hormone receptor binding Source: RGD
  • thyroid hormone receptor coactivator activity Source: RGD
  • vitamin D receptor binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • regulation of myelination 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-beta
Alternative name(s):
Nuclear receptor coregulator 1
Nuclear receptor subfamily 2 group B member 2
Retinoid X receptor beta
Gene namesi
Name:Rxrb
Synonyms:Nr2b2, Rcor-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3611. Rxrb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000053574‹1 – 458Retinoic acid receptor RXR-betaAdd BLAST›458

Proteomic databases

PaxDbiP49743.
PeptideAtlasiP49743.
PRIDEiP49743.

PTM databases

PhosphoSitePlusiP49743.

Interactioni

Subunit structurei

Homodimer (in vitro) (By similarity). Heterodimer with other retinoic acid receptor family members. Binds DNA preferentially as a RAR/RXR heterodimer (PubMed:1662118). Interacts with NR1H3 (By similarity). Interacts with AKAP13 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • retinoic acid receptor binding Source: RGD
  • thyroid hormone receptor binding Source: RGD
  • vitamin D receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040499.

Chemistry databases

BindingDBiP49743.

Structurei

3D structure databases

ProteinModelPortaliP49743.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni‹1 – 129ModulatingBy similarityAdd BLAST›129
Regioni196 – 255HingeAdd BLAST60
Regioni256 – 458Ligand-bindingBy similarityAdd BLAST203

Domaini

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

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri130 – 150NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri166 – 190NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
InParanoidiP49743.
PhylomeDBiP49743.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. 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.
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: Fragment.

P49743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GEAGRDGMGD TGRDSRSPDS SSPNPLSQGI PPSSPPGPPH TPSAPPPPMP
60 70 80 90 100
PPPLGSPFPV ISSSMGSPGL PPPAPPGFSG PVSSPQINST VSLPGGGSGP
110 120 130 140 150
PEDVKPPVLG VRGLHCPPPP GGPGAGKRLC AICGDRSSGK HYGVYSCEGC
160 170 180 190 200
KGFFKRTIRK DLTYSCRDNK DCTVDKRQRN RCQYCRYQKC LATGMKREAV
210 220 230 240 250
QEERQRGKDK DGDGDGAGGA PEEMPVDRIL EAELAVEQKS DQGVEGPGAT
260 270 280 290 300
GGGGSSPNDP VTNICQAADK QLFTLVEWAK RIPHFSSLPL DDQVILLRAG
310 320 330 340 350
WNELLIASFS HRSIDVRDGI LLATGLHVHR NSAHSAGVGA IFDRVLTELV
360 370 380 390 400
SKMRDMRMDK TELGCLRAII LFNPDAKGLS NPGEVEILRE KVYASLETYC
410 420 430 440 450
KQKYPEQQGR FAKLLLRLPA LRSIGLKCLE HLFFFKLIGD TPIDTFLMEM

LEAPHQLA
Length:458
Mass (Da):49,078
Last modified:October 1, 1996 - v1
Checksum:i22D11956B11DB4BE
GO

Sequence cautioni

The sequence AAA42025 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81766 mRNA. Translation: AAA42025.1. Different initiation.
PIRiA41651.
UniGeneiRn.49295.

Genome annotation databases

UCSCiRGD:3611. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81766 mRNA. Translation: AAA42025.1. Different initiation.
PIRiA41651.
UniGeneiRn.49295.

3D structure databases

ProteinModelPortaliP49743.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040499.

Chemistry databases

BindingDBiP49743.
ChEMBLiCHEMBL2805.

PTM databases

PhosphoSitePlusiP49743.

Proteomic databases

PaxDbiP49743.
PeptideAtlasiP49743.
PRIDEiP49743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3611. rat.

Organism-specific databases

RGDi3611. Rxrb.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
InParanoidiP49743.
PhylomeDBiP49743.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. 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.
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 nameiRXRB_RAT
AccessioniPrimary (citable) accession number: P49743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 127 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.