ID A0A8U0SER1_MUSPF Unreviewed; 2486 AA.
AC A0A8U0SER1;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 10-JUN-2026, entry version 17.
DE RecName: Full=Nuclear receptor corepressor 1 {ECO:0000256|ARBA:ARBA00044171};
GN Name=NCOR1 {ECO:0000313|RefSeq:XP_044941358.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Proteomes:UP000000715, ECO:0000313|RefSeq:XP_044941358.1};
RN [1] {ECO:0000313|RefSeq:XP_044941358.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044941358.1};
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- FUNCTION: Mediates transcriptional repression by certain nuclear
CC receptors. Part of a complex which promotes histone deacetylation and
CC the formation of repressive chromatin structures which may impede the
CC access of basal transcription factors. Participates in the
CC transcriptional repressor activity produced by BCL6. Recruited by
CC ZBTB7A to the androgen response elements/ARE on target genes,
CC negatively regulates androgen receptor signaling and androgen-induced
CC cell proliferation. Mediates the NR1D1-dependent repression and
CC circadian regulation of TSHB expression. The NCOR1-HDAC3 complex
CC regulates the circadian expression of the core clock gene ARTNL/BMAL1
CC and the genes involved in lipid metabolism in the liver.
CC {ECO:0000256|ARBA:ARBA00054129}.
CC -!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B and
CC histone deacetylases HDAC1 and HDAC2. This complex associates with the
CC thyroid receptor (TR) and the retinoid acid receptor (RAR) in the
CC absence of ligand. Interacts directly with RARA; the interaction is
CC facilitated with RARA trimethylation. Component of the N-Cor repressor
CC complex, at least composed of CBFA2T3, HEXIM1, NCOR1, NCOR2, HDAC3,
CC TBL1X, TBL1XR1, CORO2A and GPS2. Interacts with ZBTB33; the interaction
CC serves to recruit the N-CoR complex to promoter regions containing
CC methylated CpG dinucleotides. Interacts with TRIM28 and KDM3A.
CC Interacts (via the RD1 domain) with BAZ1A (via its N-terminal); the
CC interaction corepresses a number of NCOR1-regulated genes. Interacts
CC with BCL6, C1D, DACH1, HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A
CC and SIN3B. May interact with DEAF1. Interacts with RXRA. Interacts with
CC SETD5. Interacts with VDR. Interacts with ZBTB7A. Interacts with AR.
CC Interacts with HDAC3. {ECO:0000256|ARBA:ARBA00065205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000256|ARBA:ARBA00010097}.
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DR RefSeq; XP_044941358.1; XM_045085423.1.
DR GeneID; 101677398; -.
DR CTD; 9611; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0017053; C:transcription repressor complex; IEA:UniProtKB-ARBA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IEA:TreeGrafter.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:TreeGrafter.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-KW.
DR GO; GO:1902532; P:negative regulation of intracellular signal transduction; IEA:UniProtKB-ARBA.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 2.
DR FunFam; 1.20.58.1880:FF:000004; nuclear receptor corepressor 1 isoform X4; 1.
DR FunFam; 1.10.10.60:FF:000026; Nuclear receptor corepressor 2 isoform 1; 1.
DR FunFam; 1.20.5.430:FF:000001; Nuclear receptor corepressor 2 isoform 1; 1.
DR Gene3D; 1.20.5.430; -; 1.
DR Gene3D; 1.20.58.1880; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeodomain-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR051571; N-CoR_corepressor.
DR InterPro; IPR031557; N-CoR_GPS2_interact.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR PANTHER; PTHR13992; NUCLEAR RECEPTOR CO-REPRESSOR RELATED NCOR; 1.
DR PANTHER; PTHR13992:SF5; NUCLEAR RECEPTOR COREPRESSOR 1; 1.
DR Pfam; PF15784; GPS2_interact; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF27579; NCOR1_N; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|RefSeq:XP_044941358.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 444..495
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 630..684
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 630..680
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 633..684
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1931..1968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1990..2087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2336..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..64
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..615
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..740
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..816
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2010
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2083
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2171..2188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2447..2461
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2477..2486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2486 AA; 274332 MW; 9AB414368BDB8568 CRC64;
MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP STRHQQEFAV PDYRSSHLEV SQASQLLQQQ
QQQQLRRRPS LLSEFHPGSD RPQERRTGYE QFHPGPSPVD HDSLESKRPR LEQVSDPHFQ
RVSAAVLPVV HTLPEGLRSS ADAKKDPAFG GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE
LIQSMDRVDR EIAKVEQQIL KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY
DENRKKAEEA HKIFEGLGPK VELPLYNQPS DTKVYHENIK TGVPARRMMK NQVMRKKLIL
FFKRRNHARK QREQKICQRY DQLMEAWEKK VDRIENNPRR KAKESKTREY YEKQFPEIRK
QREQQERFQR VGQRGAGLSA TIARSEHEIS EIIDGLSEQE NNEKQMRQLS VIPPMMFDAE
QRRVKFINMN GLMEDPMKVY KDRQFMNVWT DHEKEIFKDK FIQHPKNFGL IASYLERKSV
PDCVLYYYLT KKNENYKALV RRNYGKRRGR NQQQIARPSQ EEKVEEKEED KAEKTEKKEE
EKKDEEEKDE KEDSKENTKE KDKTEGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT
NEAAAASAAA AAATEEPPPP LPPPPEPVST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI
AKMVGTKSEA QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE SVASTVSAQE
DEDIEASNEE ENPEDSEGFV ENEARVAGMK RILEQQSFGA ENSSDTESAP SPSPVEAVKP
SEDSTDNATS RGNTEPGAEL ESTTEPAPSA SPSSAAQSGK PVESESVETQ VSDSTPTEAA
EPMDVERQEH SAEVPSVLDL PTTTKSDSGD IEMRAPENNP SKVEGDTKER DLERASEKTE
PRDEDLVVAQ QIGAQRPEPQ SDNDSSATCS ADEDVDGEPE RQRMFPMDSK PSLLNPPGSL
LVSSPIKPNP LDLPQLQHRA AVIPPMVSCT PCNIPIGTPV SGYALYQRHI KAMHESALLE
EQRQRQEQID LECRSSTSPC GAAKSPNREW EVLQPAPHQV ITNLPETVRL PTTRPTRPPP
PLIPSSKTTV ASEKPSFILG GSISQGTPGT YLTSHNQTSY TPEAAKPSVG SISLGLPRQQ
ESAKSATVPY IKQEEFSPRS QNSQPEGLLV RAQHEGVVRG TTGAIQEGSI TRGTPTSKIS
MEGIPSLRGS ITQGTPALSQ AGIPTEALVK GSISRMPIEE SSPEKGREEA ASKGHVIYEG
KSGHILSYDN IKNAREGTRS PRTAHEISLK RSYESVEGNI KQGLSMRESP VSAPLEGLIC
RALPRGSPHS DLKERTVLSG SIMQGTPRAT TDSFEDGLKY PKQIKRESPP IRAFEGAITK
GKPYDGITTI KEMGRSIHEI PRQDILTQES RKTPEVVQST RPIIEGSISQ GTPIKFDSNS
GQSAIKHNVK SLITGPNKLP RGMPPLEIVP ENIKVVERGK YEDVKAGEPV RSRHTSVVSS
GPSVLRSALH EAPKAQLSPG LYEDSSARRT PVSYQNTMSR GSPMMSRTSD VTISSSKSTN
HERKSTLTPT QRESIPAKSP VPGVDPVVSH SPFDPHHRGS ATGEVYRSHL PTHLDPAMPF
HRALDPAAAA YLFQRQLSPT PAYPSQYQLY AMENTRQTIL NDYITSQQMQ VNLRPDVARG
LSPREQQLGL PYPATRGIID LTNMPPAILV PHPGGTSTPP MDRITYIPGT QITFPPRPYN
SASMSPGHST HLAAAASAER EREREREREK ERERIAAAAS SDLYLRSGSE QPGRPGSHGY
VRSPSPSVRA QETMLQQRPS VFQGTNGTSV ITPLDPSAQL RIMPLPAGGP SISQGLPASR
YSTAADALAA LVDAAASAPQ MEVSKTKESK HEASRLEENL RSRSAAVSEQ QQLEQKSLEA
EKRPVQCLYT PAAFPSGKPQ PHSSVVYSEA GNEKGPPPKS RYEEELRTRG KTTITAANFI
DVIITRQIAS DKDARERGSQ SSDSSSSLSS HRYEAAGDAI EVISPASSPA PPQEKLQAYQ
QDVAKANQAE GEATRQYEGP LHHYRPQQEP LSPQQQLPAS SQADGVGQVP RTHRLITLAD
HICQIITQDF ARNQVSSQPL QQPPTSTFQN SPSALVSTPV RTKTSNRYSP ESQSQSVHHQ
RPGSRVSPEN LVDKARGRPG KSPERSHVPS ESYEPISPPQ VPVVHEKQDS MLLLSQRGAE
PTEQRNDSRS PGSISYLPSF FTKLENTSPM VKSKKQEIFR KLNSSGGGDS DMAAAQPGTE
IFNLPAVTSS GSVSSRGHSF ADPASNLGLE DIIRKALMGS FDDKAEEHGV VLTQPVGVVP
GGANTSVVTS SETRREEGDP SPHSGGVCKP KLISKSNSRK SKSPIPGQGY LGTERPSSVS
SVHSEGDYHR QTPGWAWEDR PSSTGSTQFP YNPLTMRMLS STPPTPIACA PASAAQAAPH
PQNRLWEREP APLLSAQYET LSDSDD
//
