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Nuclear receptor coactivator 3 (EC 2.3.1.48) (Retinoid X receptor-interacting coactivator xSRC-3)

 NCOA3_XENLA             Reviewed;        1391 AA.
O57539;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
23-MAY-2018, entry version 126.
RecName: Full=Nuclear receptor coactivator 3;
EC=2.3.1.48;
AltName: Full=Retinoid X receptor-interacting coactivator xSRC-3;
Name=ncoa3;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RXRA; THRA AND EP300, AND
MUTAGENESIS OF LEU-622; LEU-683 AND LEU-739.
TISSUE=Oocyte;
PubMed=9658407; DOI=10.1210/mend.12.7.0139;
Kim H.-J., Lee S.-K., Na S.-Y., Choi H.-S., Lee J.W.;
"Molecular cloning of xSRC-3, a novel transcription coactivator from
Xenopus, that is related to AIB1, p/CIP and TIF2.";
Mol. Endocrinol. 12:1038-1047(1998).
-!- 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 retinoids (RAR and RXR), thyroid hormone (TR)
and orphan nuclear receptor (hepatocyte nuclear receptor 4 (HNF4)
and constitutive androstane receptor (CAR)). Displays histone
acetyltransferase activity.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBUNIT: Interacts with the histone acetyltransferase protein
EP300. {ECO:0000269|PubMed:9658407}.
-!- INTERACTION:
O57539-1:ncoa3; NbExp=2; IntAct=EBI-301587, EBI-301595;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic
and weakly nuclear. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms may be produced.;
Name=1;
IsoId=O57539-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Highly expressed in liver and in early stages
of oocyte development.
-!- DEVELOPMENTAL STAGE: Expressed only in early stages of oocyte
development. Expression is more prominent in stage I, strongly
decreases in stage II and then, gradually disappears.
-!- 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).
-!- PTM: Phosphorylated and acetylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF044080; AAC12927.1; -; mRNA.
RefSeq; NP_001081732.1; NM_001088263.1. [O57539-1]
UniGene; Xl.268; -.
ProteinModelPortal; O57539; -.
SMR; O57539; -.
PRIDE; O57539; -.
GeneID; 398021; -.
KEGG; xla:398021; -.
CTD; 398021; -.
Xenbase; XB-GENE-865628; ncoa3.
HOVERGEN; HBG052583; -.
KO; K11256; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IEA:InterPro.
GO; GO:0035257; F:nuclear hormone receptor binding; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.287.1070; -; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR010011; DUF1518.
InterPro; IPR032565; DUF4927.
InterPro; IPR036638; HLH_DNA-bd_sf.
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; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
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; PF00989; PAS; 1.
Pfam; PF08832; SRC-1; 1.
PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
SMART; SM01151; DUF1518; 1.
SMART; SM00353; HLH; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
Acetylation; Activator; Acyltransferase; Alternative splicing;
Cytoplasm; Nucleus; Phosphoprotein; Repeat; Transcription;
Transcription regulation; Transferase.
CHAIN 1 1391 Nuclear receptor coactivator 3.
/FTId=PRO_0000094409.
DOMAIN 27 84 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 112 182 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 1088 1274 Acetyltransferase.
MOTIF 680 684 LXXLL motif 1.
MOTIF 736 740 LXXLL motif 2.
MOTIF 1048 1052 LXXLL motif 3.
COMPBIAS 503 666 Ser-rich.
COMPBIAS 515 522 Poly-Ser.
COMPBIAS 968 971 Poly-Gln.
COMPBIAS 1241 1248 Poly-Gln.
MOD_RES 614 614 N6-acetyllysine. {ECO:0000250}.
MOD_RES 617 617 N6-acetyllysine. {ECO:0000250}.
MOD_RES 618 618 N6-acetyllysine. {ECO:0000250}.
MUTAGEN 622 622 L->A: Weakly impairs interaction with
nuclear receptors.
{ECO:0000269|PubMed:9658407}.
MUTAGEN 683 683 L->A: Strongly impairs interaction with
nuclear receptors.
{ECO:0000269|PubMed:9658407}.
MUTAGEN 739 739 L->A: Strongly impairs interaction with
nuclear receptors.
{ECO:0000269|PubMed:9658407}.
SEQUENCE 1391 AA; 152532 MW; AD28F5CD934AC33D CRC64;
MSGLGENSLD PLASETRKRK PSSCDTPGPG LTCSGEKRRR EQESKYIEEL ADLISANLSD
IDNFNVKPDK CAILKETVRQ IRQIKEQGKA SSNDDDVQKA DVSSTGQGVI DKDSLGPLLL
QALDGFLYVV NREGSIVFVS ENVTQYLQYK QEDLVNTSVY SILHEEDRKD FLKNLPKSTV
NGVPWFSETP RQKSHTFNCR MLVKTSHDHL EDGSNLDARQ RYETMQCFAL SQPRAMIEEG
EDLQSCMICV ARRITTAERA FSANPESFIT RHDLTGKVVN IDANSLRSSM RPGFEDTIRR
CIQRFLFHSE GQPWTYKRHY QEAYVHGLSE TPLYRFSLAD GTMVTAQTKS KLFRNPVTND
PHGFVSTHFL QREQNGYRPN PNPMAQGIRP QMNPNLPNTM NSMPPQAMQQ QNRNYGMGDP
NSMAQMQGMR YKSPGNMAPV NQAPGVQQSP YQNNSNYGLN MNSPPHGSPG MNANQPNLMV
SPRNRASPKM ASNQFSPVPG MNSPMGSSGN AGGGSFSSSS LSALHAISEG VGSSLLSSLS
SPGQKVENNS NMNMPQQGKI CNQDCKSPSG LYCEQGQVES SVCQSSGREH LGEKDVKENI
FEGSESQRSQ AESKGHKKLL QLLTCFTEER GQSLMSSSSM DCKDSSNVTS PSGVSSSTSI
GVSSTSNLHG SMLQEKHRIL HKLLQNGNSP AEVAKITAEA TGKDVFQETV SSAPCTEATV
KREQLSPKKK ENNALLRHLL DKDDWKDPLA KDIKPKVEHM DIKMGSCSSS NVPTSSQDKE
VKIKTEPGEE VPGDLDNLDA ILGDLAGSDF YSNSMSSRAS DLGPKQPVFQ DSPTLAMRSP
DSMQGSRPPF NRAMSLDSRS STPPVRNVNS FPMLPKQGMI GSPRMMDGQD NFGVMMGSGP
NRSMNQHPGG DWAMQNSAVN RLEPPNVGSV GRPGPDYSSA MTRPAMGGNM PGLLTRSNSI
PGSRPVMQQQ QHILPMRPND MAMSMGSNPY GQQAPSNPPG SWPDAIMMNQ GRGGAQNRQL
GRNSLDDLLC PPSTVEGQTD EIALLDQLHT LLSNTDATGL EEIDRALGIP DLVSQGQALE
PQPDSYQPQG SPVMIDQKPP MYGQHYAGQG AAMSAGGFNN MQGQHPPFNT VMGQMNQQQG
MHPLQGMHPR ANLIRPRNNI PKQLRMQLQQ RLQGQQFLNQ NRQALEMKVD PMNPGGAGVM
RPVMQTPVSQ QGFLNAQMVA QKNRELISHQ IRQHRMAMMM QQQQGQPQAF SPPPNVTASA
SMDNPLGGPP MPQAPPQQFS YPPNYGINQQ TDPTFGRVSS PPNAMMSSRM APSQNPHPQT
TQMYPSPDMK GWPSGNMARP NSFPQQQYSH QTNPATYNMM HMNGNGNHMG QMNINSLPMS
GMPMGPDQKY C


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