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Protein

Retinoic acid receptor RXR

Gene

RXR

Organism
Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ligand-dependent transcription factor probably involved in the retinoic acid response pathway. Binds 9-cis-retinoic acid (9C-RA) and, to a lesser extent, docosahexaenoic acid (DHA), phytanic acid, methoprene acid and oleic acid. Binds to double-stranded DNA sequences containing direct repeats (DR) with the consensus sequence 5'-[AG]GGTCA-3' and 1, 2, 3, 4 or 5 nucleotides in between (DR1, DR2, DR3. DR4 and DR5, respectively). Binding to DR1 is strongest. Transactivates gene expression when 9C-RA or DHA is bound.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi117 – 182Nuclear receptorPROSITE-ProRule annotationBy similarityAdd BLAST66
Zinc fingeri117 – 137NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri153 – 172NR C4-typePROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Vitamin A, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor RXR
Alternative name(s):
RXR-like proteinImported
Retinoid X receptor2 Publications
Short name:
BgRXR2 Publications
Gene namesi
Name:RXRImported
OrganismiBiomphalaria glabrata (Bloodfluke planorb) (Freshwater snail)
Taxonomic identifieri6526 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaPlanorboideaPlanorbidaeBiomphalaria
Proteomesi
  • UP000076420 Componenti: Genome assembly

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003944561 – 436Retinoic acid receptor RXRAdd BLAST436

Interactioni

Subunit structurei

Homodimer (via ligand-binding domain). Heterodimer (Probable). Homotetramer consisting of 2 canonical homodimers. Within the tetramer, each monomer binds one molecule of 9C-RA and a NCOA1-derived peptide containing an L-X(2)-L-L motif (Probable).Curated2 Publications

Structurei

Secondary structure

1436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi214 – 224Combined sources11
Beta strandi232 – 234Combined sources3
Helixi238 – 258Combined sources21
Helixi263 – 265Combined sources3
Helixi268 – 290Combined sources23
Helixi291 – 293Combined sources3
Beta strandi294 – 299Combined sources6
Beta strandi303 – 307Combined sources5
Helixi308 – 313Combined sources6
Helixi317 – 326Combined sources10
Helixi328 – 333Combined sources6
Helixi338 – 349Combined sources12
Helixi360 – 381Combined sources22
Helixi388 – 393Combined sources6
Helixi396 – 417Combined sources22
Helixi423 – 428Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XIUX-ray2.50A/B207-436[»]
ProteinModelPortaliQ8T5C6.
SMRiQ8T5C6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8T5C6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 116ModulatingBy similarityAdd BLAST116
Regioni183 – 206HingeBy similarityAdd BLAST24
Regioni207 – 436Ligand-binding1 PublicationAdd BLAST230
Regioni239 – 2499-cis-retinoic acid-binding1 PublicationAdd BLAST11
Regioni279 – 2909-cis-retinoic acid-binding1 PublicationAdd BLAST12
Regioni299 – 3019-cis-retinoic acid-binding1 Publication3
Regioni316 – 3239-cis-retinoic acid-binding1 Publication8
Regioni406 – 4139-cis-retinoic acid-binding1 Publication8

Domaini

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

Sequence similaritiesi

Belongs to the nuclear hormone receptor family. NR2 subfamily.Sequence analysis
Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri117 – 137NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri153 – 172NR C4-typePROSITE-ProRule annotationAdd BLAST20

Keywords - Domaini

Zinc-finger

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: Complete.

Q8T5C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRSEGMDTL ENSMPSGMSM GMTMGGHQGH PPPDIKPDIS SLTSPTSTHG
60 70 80 90 100
YYGFGPGGMP SMASSTQPSP GPQQMHSPGM HSPTSSMGSP PMLCLSPSGP
110 120 130 140 150
SPSPGLPHSS LHTKHICAIC GDRASGKHYG VYSCEGCKGF FKRTVRKDLT
160 170 180 190 200
YACRDDKNCM IDKRQRNRCQ YCRYMKCLSM GMKREAVQEE RQRVKEKGDG
210 220 230 240 250
EVESTSGANN DMPVEQILEA ELAVDPKIDT YIDAQKDPVT NICQAADKQL
260 270 280 290 300
FTLVEWAKRI PHFTELPLED QVILLRAGWN ELLIAGFSHR SIMAKDGILL
310 320 330 340 350
ATGLHVHRSS AHQAGVGTIF DRVLTELVAK MRDMKMDKTE LGCLRAVVLF
360 370 380 390 400
NPDAKGLTAV QEVEQLREKV YASLEEYTKS RYPEEPGRFA KLLLRLPALR
410 420 430
SIGLKCLEHL FFFKLIGDQP IDTFLMEMLE NPSPAT
Length:436
Mass (Da):48,225
Last modified:June 1, 2002 - v1
Checksum:i94D6E84B5CEBD4F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048663 mRNA. Translation: AAL86461.1.
RefSeqiNP_001298239.1. NM_001311310.1.

Genome annotation databases

GeneIDi106073343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048663 mRNA. Translation: AAL86461.1.
RefSeqiNP_001298239.1. NM_001311310.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XIUX-ray2.50A/B207-436[»]
ProteinModelPortaliQ8T5C6.
SMRiQ8T5C6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi106073343.

Miscellaneous databases

EvolutionaryTraceiQ8T5C6.

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 nameiRXR_BIOGL
AccessioniPrimary (citable) accession number: Q8T5C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.