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Database: UniProt
Entry: A0A6I8NAS0_ORNAN
LinkDB: A0A6I8NAS0_ORNAN
Original site: A0A6I8NAS0_ORNAN 
ID   A0A6I8NAS0_ORNAN        Unreviewed;      1398 AA.
AC   A0A6I8NAS0;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   18-JUN-2025, entry version 24.
DE   RecName: Full=Nuclear receptor coactivator 1 {ECO:0000256|ARBA:ARBA00067182};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE   AltName: Full=Steroid receptor coactivator 1 {ECO:0000256|ARBA:ARBA00075136};
GN   Name=NCOA1 {ECO:0000313|Ensembl:ENSOANP00000038154.1};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000038154.1, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000038154.1, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000038154.1,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000038154.1}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000038154.1};
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein]
CC         + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00048017};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family. {ECO:0000256|ARBA:ARBA00009933}.
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DR   FunCoup; A0A6I8NAS0; 2083.
DR   Ensembl; ENSOANT00000059926.1; ENSOANP00000038154.1; ENSOANG00000004546.4.
DR   GeneTree; ENSGT00950000183021; -.
DR   InParanoid; A0A6I8NAS0; -.
DR   OMA; SRTCPQQ; -.
DR   Proteomes; UP000002279; Chromosome X2.
DR   Bgee; ENSOANG00000004546; Expressed in cerebellum and 7 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl.
DR   GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:0030520; P:estrogen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:Ensembl.
DR   GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd18948; bHLH-PAS_NCoA1_SRC1; 1.
DR   CDD; cd00130; PAS; 1.
DR   FunFam; 3.30.450.20:FF:000007; Nuclear receptor coactivator; 1.
DR   FunFam; 3.30.450.20:FF:000031; Nuclear receptor coactivator; 1.
DR   FunFam; 4.10.280.10:FF:000008; Nuclear receptor coactivator; 1.
DR   Gene3D; 6.10.140.410; -; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR056193; bHLH_NCOA1-3.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR010011; NCO_DUF1518.
DR   InterPro; IPR028819; NCOA1_bHLH.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF1; NUCLEAR RECEPTOR COACTIVATOR 1; 1.
DR   Pfam; PF23172; bHLH_NCOA; 1.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF16665; NCOA_u2; 1.
DR   Pfam; PF08815; Nuc_rec_co-act; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF14598; PAS_11; 1.
DR   SMART; SM01151; DUF1518; 2.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          23..80
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          109..180
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1003..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..391
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..422
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..433
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..446
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..492
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..526
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..591
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..648
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1398 AA;  144862 MW;  943D9CDF8D7FE7DC CRC64;
     MSGLGDSPTD PANLDSRKRK GSPCDTLGSS PEKRRREQEN KYLEELAELL SANLGDIDSL
     SVKPDKCEIL RKTVGQIQQM RRREQEKAAA DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
     DGFFFVVNRE GRIVFVSENV TGYLGYKQEE LMNTSVYSVL HVGDHAELIK NLLPKSLVNN
     VPWPQEAPRR SGHTFNCRML LRGPGGQGAD GTDGAGGAEA RSQRYEMMQC FTVSQPKSIT
     EEPEDFHSCL ICIARRFPRP PAVPGSESFM TKQDTTGKII SIDTSSLRAA GRTGWEDLVR
     KCIYAFFQPH GREPSYARQL FQEVMTRGAA FSPPYRFSLS DGTVLSARTK CKLCYPQSPD
     AQPFIMGIHI VDRDPSALSP PESPSSGLAL PRVNPTGHPA LSPAPGLAPA SALPPAASGQ
     QPTPGPPAGP PPGSGSGGGG GGGSGSSPGQ SNFGCLLGSQ APAAGLASSA PGPGPALGLS
     GSPLGSPAGL PPTQFASPRR QMSPGLLARP RVPGNPFSPP SLPPLGSPVG GASGACPGAH
     RPYAPGPGAA LQGVCEGPGH PAGFAPTPPV LRPPGSQGSP GPPAPQGPSG PPGRLGSKTE
     PRDGKEVASL LSEMMQAGDS PGEGQAPDAG TPPGGGGRGD HRRPEGDGKG PQGGGHRPGQ
     LPANAAERRP LPADADPGSG CRDASSCPGR HKILHRLLQE GSPSDIGSPP PEPERRDSGP
     PGLPANRAEQ EGTRKKDQKD HQLLRYLLDK NEKTGAAPGP LSLDDVEVNL ERAEPGSPPS
     PDEARLGPQG RFTSDLEQLD QLLPALEKAV QLPGLCGSDR TEGSAPGVTL KQEIVPTPLQ
     PSSARLFTGL KRLPDPDLGS TDLQSGQPGA GDPLPWADNA LSSVARGGPP AKPEDPCLGS
     QLDELLCPPT TAEGRNDEKA LLEQLVAFLS GQDETELAEL DRALGIDKLV QGGGVEVLGE
     GFQPPPAPQP ALLDPKPGMY AQPYPSSASP ASAAAAAFQG LARQKPTFGP GPGQGPAPRG
     AFPTAMGLQP AIRLTVPPPP PRPLSPPISI QLMHQNRQAL FSQFAASAPV GIAVRSGMLQ
     QMASQPPLNA QMLAQRQREL YSQQHRQRQL LQQRAMLMRQ HSFAGSLPPT APGMSAQMGA
     ARLAQPSPHQ FPYPPSYGTN PGTPPSSSSP FSPLPPGPEA ALVSRGGVGG RAMMGGQFGA
     GMSPQTQQNV FQYAGSGMGQ PGEAGFAPAL SPGSPTGSPQ MAAAQPSPGY QSPDVKTWQQ
     GALGASNMFG QAAASQQALY NNMSITVAMA GPGVQALNPV NGHVQMGSLS GLNAAAVCAE
     QVADPTLMPG SLYCSQLPSD LLKADPDGAQ MQQVQVFADV QCTVNVVGGE PYHLGQAAPL
     GAPSSQVPKS LLQQLLTE
//
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