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Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (Amplified in breast cancer-1 protein homolog) (AIB-1) (Fragment)

 NCOA3_RAT               Reviewed;        1082 AA.
Q9EPU2;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 124.
RecName: Full=Nuclear receptor coactivator 3;
Short=NCoA-3;
EC=2.3.1.48;
AltName: Full=Amplified in breast cancer-1 protein homolog;
Short=AIB-1;
Flags: Fragment;
Name=Ncoa3; Synonyms=Aib1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=10906038; DOI=10.1095/biolreprod63.2.361;
Nephew K.P., Ray S., Hlaing M., Ahluwalia A., Wu S.D., Long X.,
Hyder S.M., Bigsby R.M.;
"Expression of estrogen receptor coactivators in the rat uterus.";
Biol. Reprod. 63:361-367(2000).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- 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). {ECO:0000250}.
-!- SUBUNIT: 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. Interacts with NPAS2 (By similarity).
Interacts with NR4A3 (By similarity). Interacts with ESRRB;
mediates the interaction between ESRRB and RNA polymerase II
complexes and allows NCOA3 corecruitment to ESRRB, KLF4, NANOG,
and SOX2 enhancer regions to trigger ESRRB-dependent gene
activation involved in self-renewal and pluripotency (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09000}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Mainly cytoplasmic and weakly nuclear. Upon
TNF activation and subsequent phosphorylation, it translocates
from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed constitutively in uterus.
{ECO:0000269|PubMed:10906038}.
-!- 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). {ECO:0000250}.
-!- PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain,
and disrupts the interaction with nuclear receptors and regulates
its function (By similarity). {ECO:0000250}.
-!- PTM: Methylated by CARM1. {ECO:0000250}.
-!- PTM: Phosphorylated by IKK complex. Regulated its function (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF322224; AAG42837.1; -; mRNA.
UniGene; Rn.20691; -.
ProteinModelPortal; Q9EPU2; -.
STRING; 10116.ENSRNOP00000059144; -.
iPTMnet; Q9EPU2; -.
PhosphoSitePlus; Q9EPU2; -.
PaxDb; Q9EPU2; -.
PRIDE; Q9EPU2; -.
UCSC; RGD:620109; rat.
RGD; 620109; Ncoa3.
eggNOG; KOG3561; Eukaryota.
eggNOG; ENOG410XRJI; LUCA.
HOGENOM; HOG000230947; -.
HOVERGEN; HBG052583; -.
InParanoid; Q9EPU2; -.
PhylomeDB; Q9EPU2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0050681; F:androgen receptor binding; IPI:RGD.
GO; GO:0030331; F:estrogen receptor binding; IPI:RGD.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IBA:GO_Central.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:RGD.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
GO; GO:0000993; F:RNA polymerase II core binding; ISS:UniProtKB.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:RGD.
GO; GO:0043697; P:cell dedifferentiation; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IDA:RGD.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IDA:RGD.
GO; GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; IMP:RGD.
GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.287.1070; -; 1.
InterPro; IPR010011; DUF1518.
InterPro; IPR032565; DUF4927.
InterPro; IPR028818; NCOA3.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
InterPro; IPR017426; Nuclear_rcpt_coactivator.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR014935; SRC/p160_LXXLL.
PANTHER; PTHR10684; PTHR10684; 1.
PANTHER; PTHR10684:SF3; PTHR10684:SF3; 1.
Pfam; PF07469; DUF1518; 1.
Pfam; PF16279; DUF4927; 1.
Pfam; PF08815; Nuc_rec_co-act; 1.
Pfam; PF08832; SRC-1; 1.
SMART; SM01151; DUF1518; 1.
SUPFAM; SSF55785; SSF55785; 1.
SUPFAM; SSF69125; SSF69125; 1.
2: Evidence at transcript level;
Acetylation; Activator; Acyltransferase; Complete proteome; Cytoplasm;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Transferase.
CHAIN <1 1082 Nuclear receptor coactivator 3.
/FTId=PRO_0000094408.
REGION 712 782 Interaction with CREBBP. {ECO:0000250}.
REGION 786 962 Acetyltransferase.
MOTIF 385 389 LXXLL motif 1.
MOTIF 437 441 LXXLL motif 2.
MOTIF 723 727 LXXLL motif 3.
COMPBIAS 136 371 Ser-rich.
COMPBIAS 773 936 Gln-rich.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000250|UniProtKB:O09000}.
MOD_RES 316 316 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 319 319 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 320 320 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 387 387 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:O09000}.
MOD_RES 722 722 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 860 860 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 866 866 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 877 877 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
MOD_RES 988 988 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Q9}.
NON_TER 1 1
SEQUENCE 1082 AA; 115134 MW; BA35D946CBC8C080 CRC64;
IIRRCIQRFF SLNDGQSWSQ KRHYQEAYIH GHAETPVYRF SLADGTIVSA QTKSKLFRNP
VTNDRHGFVS THFLQREQNG CRPNPILQDK GIRPPAAGCG MSLSPSQSVQ MLGSRTYGVA
DPSNTGQMAG ARYGASSSVA SLTPGQSLQS PSSYQSNSYG LNMSSPPHGS PGLGPNQQNI
MISPRNRGSP KMASHQFSPA AGVHSPMGSS GNTGSHSFSS SSLSALQAIS EGVGTSLLST
LSSPGPKLDN SPNMNINQPS KASSQDSKSP LGLYCEQNPV ESSVCPSNSR DPPVTKENKE
NSGEASETPR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSNCKDSS ISVTSPSGVS
SSTSGAVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSTASGGEGS
VXQEQLSPXK KENNALLRYL LDRDDPSDVL AKELQPQADG GDSKLSQCSC XTNPSSGQEK
DPKIKTEEVS GDLDNLDAIL GDLTSSDFYN SPTNGSHPGA KQQMFAGPSS LGLRSPQPVQ
SVRPPYNRAL SLDSPVSVGS VPPVKNVSAF PVLPKQPILA GNPRMMDSQE NYGANMGGPN
RNVPVNPTSS SGDWGLANSR ASRMEPLASS PLGRAGGDYS AALPRPALGS SGPTLPLRSN
RLPGARPTLM LQMRAGEVPM GMGVSPYSPA VPSNQPGSWP EGMLSMEQGP HGAQNRPLLR
NSLDELLGPP SNPEGQSDER ALLDQLHTLL SNTDATGLEE IDRALGIPEL VSQGQALESK
QDVFQGQEAA VMMDQKAALY GQTYPAQGPP LQGGFHLQGQ SPSLNSMMSQ ISQQGSFPLQ
GLHPRASMVR PRTNTPKQLR MQLQQRLQGQ QFLNQSRQAL EMKMESPTGA AVMRPMLQSQ
QAFFNAQMAA QQKRELMNHH LQQQRMAMMM SQPQPQAFSP PPNVTASPSM DGVLAGSAMP
QAPPQQFPYA TNYGMGQPPE PAFGRGSSPP SAMMSSRMGP SQNAMVQHPQ TAPMYQSSEM
KGWPSGNLAR NGSFPQQQFA PQANPAAYNM VHMNSSGSHL GQMTMTPMPM SGMPMGPDQK
YC


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