NCOA1_PIG
ID NCOA1_PIG Reviewed; 1440 AA.
AC Q4PJW2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Nuclear receptor coactivator 1;
DE Short=NCoA-1;
DE EC=2.3.1.48;
DE AltName: Full=Steroid receptor coactivator 1;
DE Short=SRC-1;
GN Name=NCOA1; Synonyms=SRC1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16753821; DOI=10.1080/10425170500476343;
RA Yu D., Mneg H., Bai C., Zhao W., Wang Q.S., Pan Y.;
RT "Molecular cloning of nuclear receptor coactivator-1 gene in pig.";
RL DNA Seq. 17:79-82(2006).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Involved in the coactivation of different nuclear
CC receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs),
CC thyroid hormone (TRs) and prostanoids (PPARs). Also involved in
CC coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription
CC factors. Displays histone acetyltransferase activity toward H3 and H4;
CC the relevance of such activity remains however unclear. Plays a central
CC role in creating multisubunit coactivator complexes that act via
CC remodeling of chromatin, and possibly acts by participating in both
CC chromatin remodeling and recruitment of general transcription factors.
CC Required with NCOA2 to control energy balance between white and brown
CC adipose tissues. Required for mediating steroid hormone response (By
CC similarity). {ECO:0000250}.
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 NCOA6 and NCOA2. Interacts with the FDL motif
CC of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6.
CC Interacts with STAT3 following IL-6 stimulation. Interacts with the
CC basal transcription factor GTF2B. Interacts with COPS5, NR3C1, PCAF and
CC TTLL5/STAMP. Interacts with the histone acetyltransferases EP300 and
CC CREBBP, and the methyltransferase CARM1. Interacts with UBE2L3; they
CC functionally interact to regulate progesterone receptor transcriptional
CC activity. Interacts with PRMT2 and DDX5. Interacts with ASXL1.
CC Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC
CC (via AF-2 motif). Interacts in a ligand-dependent fashion with RXRA.
CC Interacts with TRIP4. Interacts with NR4A3. Interacts with VDR.
CC {ECO:0000250|UniProtKB:P70365, ECO:0000250|UniProtKB:Q15788}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- DOMAIN: The C-terminal (1107-1447) part mediates the histone
CC acetyltransferase (HAT) activity. {ECO:0000250}.
CC -!- DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3,
CC 4 and 5 are essential for the association with nuclear receptors.
CC -!- PTM: Sumoylated; sumoylation increases its interaction with PGR and
CC prolongs its retention in the nucleus. It does not prevent its
CC ubiquitination and does not exert a clear effect on the stability of
CC the protein (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated; leading to proteasome-mediated degradation.
CC Ubiquitination and sumoylation take place at different sites (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
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DR EMBL; DQ078269; AAY82453.1; -; mRNA.
DR RefSeq; NP_001020399.1; NM_001025228.1.
DR AlphaFoldDB; Q4PJW2; -.
DR SMR; Q4PJW2; -.
DR STRING; 9823.ENSSSCP00000009151; -.
DR PaxDb; Q4PJW2; -.
DR PRIDE; Q4PJW2; -.
DR GeneID; 574068; -.
DR KEGG; ssc:574068; -.
DR CTD; 8648; -.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; Q4PJW2; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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; IPR028819; NCOA1.
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:SF1; PTHR10684:SF1; 1.
DR Pfam; PF07469; DUF1518; 2.
DR Pfam; PF00010; HLH; 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; 2.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Acyltransferase; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT CHAIN 2..1440
FT /note="Nuclear receptor coactivator 1"
FT /id="PRO_0000300687"
FT DOMAIN 23..80
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 109..180
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..567
FT /note="Interaction with STAT3"
FT /evidence="ECO:0000250"
FT REGION 368..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..988
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000250"
FT REGION 1142..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..50
FT /note="LXXLL motif 1"
FT /evidence="ECO:0000250"
FT MOTIF 112..116
FT /note="LXXLL motif 2"
FT /evidence="ECO:0000250"
FT MOTIF 633..637
FT /note="LXXLL motif 3"
FT /evidence="ECO:0000250"
FT MOTIF 690..694
FT /note="LXXLL motif 4"
FT /evidence="ECO:0000250"
FT MOTIF 749..753
FT /note="LXXLL motif 5"
FT /evidence="ECO:0000250"
FT MOTIF 913..917
FT /note="LXXLL motif 6"
FT /evidence="ECO:0000250"
FT MOTIF 1434..1438
FT /note="LXXLL motif 7"
FT /evidence="ECO:0000250"
FT COMPBIAS 373..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 1073
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1091
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1124
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1131
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15788"
SQ SEQUENCE 1440 AA; 156925 MW; 79B850ED7958AF50 CRC64;
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDEVQKSDIS SSSQGVIEKE SLGPLLLEAL
DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG
VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ
SCLICIARRL PRPPAIMGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWEE FMRKCIYAFF
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG
IHIIDREHSG LSPQDDTNSG MSIPRVNPPV NPSISPAHGV ARSSSLPPSN SNMVSTRVNR
QQSSDLHSSS HSNSSNSQGS FGCSPGNQIV AGVALNQGQA SSQSTNPPLN LNNSPMEGTG
ISLAQFMSPR RQVSSGLATR PRMPNNSFPP NIPTLNSPVS MTSTACNNSN RSYSNIPVTS
LQSMNEGPNN SVGFSAGSPV LRQMSSQNSP SRLNIQPAKA ESKDNKETAS ILNEMIQSDN
SSNDGKPLDS GLLHNNDRLS DGDNKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKEVLSC
TGTSSSASAN SSSGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS
VTGQVPGNSG IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ
MDPCNTNPTP MTKPPPEEIK LESQSQFTAD LDQFDQLLPT LEKAAQLPGL CETERMDGAV
TSVTIKSEIL PATLQSTTAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WANNTVTAVN
QNKPEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL
VQGGGLDVLS ERFPPQQATP PLMMEERPNL YSQPYSSPSP TANLSGPFQG MVRQKPSLGT
MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF
AANAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRRRQLIQQQ RAMLMRQQSF
GNNLPPSSGL PVPMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AENPEATLGN
RNSMVNRGMT GNMGGQFGTG INPQMQQNVF QYPGSGMVPQ GEANFAPSLS PGSSMVPMPI
PPPQSSLLQQ TPPASGYQSP DMKAWQQGAM GNNNVFSQAV QNQPTPAQPG VYNNMSITVS
MAGGNTNVQN MNPMMGQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE
ADGTQVQQVQ VFADVQCTVN LVGGDPYLNQ PGPLGTQKPT AGPQTPQAQQ KSLLQQLLTE
