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Q9EPU2 (NCOA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor coactivator 3

Short name=NCoA-3
EC=2.3.1.48
Alternative name(s):
Amplified in breast cancer-1 protein homolog
Short name=AIB-1
Gene names
Name:Ncoa3
Synonyms:Aib1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1082 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit By similarity.

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Enzyme regulation

Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors By similarity.

Subunit structure

Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase protein CREBBP. Interacts with PCAF and CARM1. Interacts with CASP8AP2 and NR3C1 By similarity. Interacts with ATAD2 and this interaction is enhanced by estradiol By similarity. Interacts with PSMB9. Binds to CSNK1D By similarity. Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus By similarity.

Tissue specificity

Expressed constitutively in uterus. Ref.1

Domain

Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain) By similarity.

Post-translational modification

Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function By similarity.

Methylated by CARM1 By similarity.

Phosphorylated by IKK complex. Regulated its function By similarity.

Sequence similarities

Belongs to the SRC/p160 nuclear receptor coactivator family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   Molecular functionActivator
Acyltransferase
Transferase
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmale gonad development

Inferred from expression pattern PubMed 16189181. Source: RGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 21454665. Source: RGD

positive regulation of cell growth

Inferred from mutant phenotype PubMed 21454665. Source: RGD

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from direct assay PubMed 11713241. Source: RGD

positive regulation of intracellular steroid hormone receptor signaling pathway

Inferred from mutant phenotype PubMed 16179382. Source: RGD

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11713241. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17481888. Source: RGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 16179382. Source: RGD

cytoplasm

Inferred from direct assay PubMed 16189181. Source: RGD

nucleus

Inferred from direct assay PubMed 16179382PubMed 19696011. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16179382. Source: RGD

   Molecular_functionRNA polymerase II regulatory region DNA binding

Inferred from direct assay PubMed 15166231. Source: RGD

androgen receptor binding

Inferred from physical interaction PubMed 17223690. Source: RGD

estrogen receptor binding

Inferred from physical interaction PubMed 11818503. Source: RGD

histone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 11713241. Source: RGD

peroxisome proliferator activated receptor binding

Inferred from physical interaction PubMed 20132223. Source: RGD

protein complex binding

Inferred from mutant phenotype PubMed 20132223. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 1082›1082Nuclear receptor coactivator 3
PRO_0000094408

Regions

Region712 – 78271Interaction with CREBBP By similarity
Region786 – 962177Acetyltransferase
Motif385 – 3895LXXLL motif 1
Motif437 – 4415LXXLL motif 2
Motif723 – 7275LXXLL motif 3
Compositional bias136 – 371236Ser-rich
Compositional bias773 – 936164Gln-rich

Amino acid modifications

Modified residue2511Phosphoserine By similarity
Modified residue3161N6-acetyllysine; by CREBBP By similarity
Modified residue3191N6-acetyllysine; by CREBBP By similarity
Modified residue3201N6-acetyllysine; by CREBBP By similarity
Modified residue3871N6-acetyllysine By similarity
Modified residue4271Phosphoserine By similarity
Modified residue5511Phosphoserine By similarity
Modified residue5541Phosphoserine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q9EPU2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: BA35D946CBC8C080

FASTA1,082115,134
        10         20         30         40         50         60 
IIRRCIQRFF SLNDGQSWSQ KRHYQEAYIH GHAETPVYRF SLADGTIVSA QTKSKLFRNP 

        70         80         90        100        110        120 
VTNDRHGFVS THFLQREQNG CRPNPILQDK GIRPPAAGCG MSLSPSQSVQ MLGSRTYGVA 

       130        140        150        160        170        180 
DPSNTGQMAG ARYGASSSVA SLTPGQSLQS PSSYQSNSYG LNMSSPPHGS PGLGPNQQNI 

       190        200        210        220        230        240 
MISPRNRGSP KMASHQFSPA AGVHSPMGSS GNTGSHSFSS SSLSALQAIS EGVGTSLLST 

       250        260        270        280        290        300 
LSSPGPKLDN SPNMNINQPS KASSQDSKSP LGLYCEQNPV ESSVCPSNSR DPPVTKENKE 

       310        320        330        340        350        360 
NSGEASETPR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSNCKDSS ISVTSPSGVS 

       370        380        390        400        410        420 
SSTSGAVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSTASGGEGS 

       430        440        450        460        470        480 
VXQEQLSPXK KENNALLRYL LDRDDPSDVL AKELQPQADG GDSKLSQCSC XTNPSSGQEK 

       490        500        510        520        530        540 
DPKIKTEEVS GDLDNLDAIL GDLTSSDFYN SPTNGSHPGA KQQMFAGPSS LGLRSPQPVQ 

       550        560        570        580        590        600 
SVRPPYNRAL SLDSPVSVGS VPPVKNVSAF PVLPKQPILA GNPRMMDSQE NYGANMGGPN 

       610        620        630        640        650        660 
RNVPVNPTSS SGDWGLANSR ASRMEPLASS PLGRAGGDYS AALPRPALGS SGPTLPLRSN 

       670        680        690        700        710        720 
RLPGARPTLM LQMRAGEVPM GMGVSPYSPA VPSNQPGSWP EGMLSMEQGP HGAQNRPLLR 

       730        740        750        760        770        780 
NSLDELLGPP SNPEGQSDER ALLDQLHTLL SNTDATGLEE IDRALGIPEL VSQGQALESK 

       790        800        810        820        830        840 
QDVFQGQEAA VMMDQKAALY GQTYPAQGPP LQGGFHLQGQ SPSLNSMMSQ ISQQGSFPLQ 

       850        860        870        880        890        900 
GLHPRASMVR PRTNTPKQLR MQLQQRLQGQ QFLNQSRQAL EMKMESPTGA AVMRPMLQSQ 

       910        920        930        940        950        960 
QAFFNAQMAA QQKRELMNHH LQQQRMAMMM SQPQPQAFSP PPNVTASPSM DGVLAGSAMP 

       970        980        990       1000       1010       1020 
QAPPQQFPYA TNYGMGQPPE PAFGRGSSPP SAMMSSRMGP SQNAMVQHPQ TAPMYQSSEM 

      1030       1040       1050       1060       1070       1080 
KGWPSGNLAR NGSFPQQQFA PQANPAAYNM VHMNSSGSHL GQMTMTPMPM SGMPMGPDQK 


YC 

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References

[1]"Expression of estrogen receptor coactivators in the rat uterus."
Nephew K.P., Ray S., Hlaing M., Ahluwalia A., Wu S.D., Long X., Hyder S.M., Bigsby R.M.
Biol. Reprod. 63:361-367(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF322224 mRNA. Translation: AAG42837.1.
UniGeneRn.20691.

3D structure databases

ProteinModelPortalQ9EPU2.
SMRQ9EPU2. Positions 734-780.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9EPU2.

Proteomic databases

PaxDbQ9EPU2.
PRIDEQ9EPU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:620109. rat.

Organism-specific databases

RGD620109. Ncoa3.

Phylogenomic databases

eggNOGNOG315556.
HOGENOMHOG000230947.
HOVERGENHBG052583.
PhylomeDBQ9EPU2.

Gene expression databases

GenevestigatorQ9EPU2.

Family and domain databases

Gene3D4.10.630.10. 2 hits.
InterProIPR010011. DUF1518.
IPR028818. NCOA3.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR017426. Nuclear_rcpt_coactivator.
IPR000014. PAS.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
PfamPF07469. DUF1518. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
SSF69125. SSF69125. 1 hit.
ProtoNetSearch...

Other

PROQ9EPU2.

Entry information

Entry nameNCOA3_RAT
AccessionPrimary (citable) accession number: Q9EPU2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families