NCOA3_XENLA
ID NCOA3_XENLA Reviewed; 1391 AA.
AC O57539;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nuclear receptor coactivator 3;
DE EC=2.3.1.48;
DE AltName: Full=Retinoid X receptor-interacting coactivator xSRC-3;
GN Name=ncoa3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RXRA; THRA AND EP300, AND
RP MUTAGENESIS OF LEU-622; LEU-683 AND LEU-739.
RC TISSUE=Oocyte;
RX PubMed=9658407; DOI=10.1210/mend.12.7.0139;
RA Kim H.-J., Lee S.-K., Na S.-Y., Choi H.-S., Lee J.W.;
RT "Molecular cloning of xSRC-3, a novel transcription coactivator from
RT Xenopus, that is related to AIB1, p/CIP and TIF2.";
RL Mol. Endocrinol. 12:1038-1047(1998).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Plays a central role in creating a multisubunit
CC coactivator complex, probably via remodeling of chromatin. Involved in
CC the coactivation of different nuclear receptors, such as retinoids (RAR
CC and RXR), thyroid hormone (TR) and orphan nuclear receptor (hepatocyte
CC nuclear receptor 4 (HNF4) and constitutive androstane receptor (CAR)).
CC Displays histone acetyltransferase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Interacts with the histone acetyltransferase protein EP300.
CC {ECO:0000269|PubMed:9658407}.
CC -!- INTERACTION:
CC O57539; O57539-1: ncoa3; NbExp=2; IntAct=EBI-301587, EBI-301595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and
CC weakly nuclear. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1;
CC IsoId=O57539-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and in early stages of
CC oocyte development.
CC -!- DEVELOPMENTAL STAGE: Expressed only in early stages of oocyte
CC development. Expression is more prominent in stage I, strongly
CC decreases in stage II and then, gradually disappears.
CC -!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and
CC 2 are essential for the association with nuclear receptors, and
CC constitute the RID domain (Receptor-interacting domain).
CC -!- PTM: Phosphorylated and acetylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
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DR EMBL; AF044080; AAC12927.1; -; mRNA.
DR RefSeq; NP_001081732.1; NM_001088263.1. [O57539-1]
DR AlphaFoldDB; O57539; -.
DR GeneID; 398021; -.
DR KEGG; xla:398021; -.
DR CTD; 398021; -.
DR Xenbase; XB-GENE-865628; ncoa3.S.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 398021; Expressed in camera-type eye and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:InterPro.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.410; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
DR InterPro; IPR028818; NCOA3.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR014935; SRC/p160_LXXLL.
DR PANTHER; PTHR10684; PTHR10684; 1.
DR PANTHER; PTHR10684:SF3; PTHR10684:SF3; 1.
DR Pfam; PF07469; DUF1518; 1.
DR Pfam; PF16279; DUF4927; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Alternative splicing; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..1391
FT /note="Nuclear receptor coactivator 3"
FT /id="PRO_0000094409"
FT DOMAIN 27..84
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 112..182
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1274
FT /note="Acetyltransferase"
FT REGION 1242..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 680..684
FT /note="LXXLL motif 1"
FT MOTIF 736..740
FT /note="LXXLL motif 2"
FT MOTIF 1048..1052
FT /note="LXXLL motif 3"
FT COMPBIAS 832..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 614
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 617
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 618
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 622
FT /note="L->A: Weakly impairs interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:9658407"
FT MUTAGEN 683
FT /note="L->A: Strongly impairs interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:9658407"
FT MUTAGEN 739
FT /note="L->A: Strongly impairs interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:9658407"
SQ 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
