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IID00365
UniprotP10276
ProteinRetinoic acid receptor alpha
GeneRARA
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
462
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 82-167 Hetero dimer : IID00031Complex
 Evidence X-RAY 1dsz A Reference
       Region 1dsz A 82-86 disorder
       Region 1dsz A 87-161 order
       Region 1dsz A 162-167 disorder
Seq 153-421 Hetero trimer : IID00082Complex,P28700
 Evidence X-RAY 3a9e B Reference
       Region 3a9e B 153-176 disorder
       Region 3a9e B 177-415 order
       Region 3a9e B 416-421 disorder
Seq 176-421 Hetero tetramer : IID00189Complex
 Evidence X-RAY 3kmz A Reference
       Region 3kmz A 176-180 disorder
       Region 3kmz A 181-401 order
       Region 3kmz A 402-421 disorder
 Evidence X-RAY 3kmz B Reference
       Region 3kmz B 176-180 disorder
       Region 3kmz B 181-401 order
       Region 3kmz B 402-421 disorder
Seq 176-421 Hetero dimer : IID00083Complex
 Evidence X-RAY 3kmr A Reference
       Region 3kmr A 176-181 disorder
       Region 3kmr A 182-415 order
       Region 3kmr A 416-421 disorder
Seq 181-426 Monomer :
 Evidence X-RAY 5k13 A Reference
       Region 5k13 A 181-415 order
       Region 5k13 A 416-426 disorder
Seq 182-415 Hetero dimer : IID00083Complex
 Evidence X-RAY 4dqm C Reference
       Region 4dqm C 182-415 order
 Evidence X-RAY 4dqm A Reference
       Region 4dqm A 182-415 order
Seq 182-416 Hetero dimer : P28700
 Evidence X-RAY 1dkf B Reference
       Region 1dkf B 182-210 order
       Region 1dkf B 211-213 disorder
       Region 1dkf B 214-416 order
Seqphosphorylation
    77-77 Phosphoserine; by CDK7
    96-96 Phosphoserine; by PKB/AKT1
    219-219 Phosphoserine; by PKA
    369-369 Phosphoserine; by PKA
 
Prediction
NeProc
Disorder 1-84,162-185,205-221,418-462
Order 85-161,186-204,222-417
ProS 162-162,205-210
AlphaFold
Disorder 1-77,80-83,160-179,416-462
Order 78-79,84-159,180-415
Pfam Hmmer
PF00105 86-161 1.7e-55
PF00104 233-413 4.2e-44
SEG 19-30 ,65-80 ,425-462
Function
Function in SwissProt
Receptor for retinoic acid (PubMed:19850744, PubMed:16417524, PubMed:20215566). 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 (PubMed:28167758). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:28167758). 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 (PubMed:16417524). On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (PubMed:9267036, PubMed:19850744, PubMed:20215566). Formation of a complex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (PubMed:28167758). Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (PubMed:28167758). RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (By similarity). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (By similarity). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (PubMed:28167758).
Biological Process
See also
Diagram with PDB data
NCOA1/RARACrystal structure of RARalpha ligand binding domain in complex with an agonist ligand (Am580) and a coactivator fragment