NCOR1_RAT
ID NCOR1_RAT Reviewed; 533 AA.
AC Q9WUB5; O70463;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nuclear receptor corepressor 1;
DE Short=N-CoR;
DE Short=N-CoR1;
DE Flags: Fragment;
GN Name=Ncor1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10441327; DOI=10.1093/hmg/8.9.1647;
RA Boutell J.M., Thomas P., Neal J.W., Weston V.J., Duce J., Harper P.S.,
RA Jones A.L.;
RT "Aberrant interactions of transcriptional repressor proteins with the
RT Huntington's disease gene product, huntingtin.";
RL Hum. Mol. Genet. 8:1647-1655(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 476-528.
RC TISSUE=Skeletal muscle;
RX PubMed=10491148; DOI=10.1046/j.1432-1327.1999.00706.x;
RA Schuler M.J., Buehler S., Pette D.;
RT "Effects of contractile activity and hypothyroidism on nuclear hormone
RT receptor mRNA isoforms in rat skeletal muscle.";
RL Eur. J. Biochem. 264:982-988(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-196; SER-214;
RP SER-230; SER-245; SER-529 AND SER-531, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Mediates the NR1D1-dependent
CC repression and circadian regulation of TSHB expression (By similarity).
CC The NCOR1-HDAC3 complex regulates the circadian expression of the core
CC clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in
CC the liver (By similarity). {ECO:0000250|UniProtKB:O75376,
CC ECO:0000250|UniProtKB:Q60974}.
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 (By similarity).
CC Interacts with AR (By similarity). Interacts with HDAC3 (By
CC similarity). {ECO:0000250|UniProtKB:O75376,
CC ECO:0000250|UniProtKB:Q60974}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region contains three independent domains that
CC are capable of mediating transcriptional repression (RD1, RD2 and RD3).
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal region contains two separate nuclear receptor-
CC interacting domains (ID1 and ID2), each of which contains a conserved
CC sequence referred to as the CORNR box. This motif is necessary and
CC sufficient for binding to unligated nuclear hormone receptors, while
CC sequences flanking the CORNR box determine the precise nuclear hormone
CC receptor specificity (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF124821; AAD32566.1; -; mRNA.
DR EMBL; AF059311; AAC14567.1; -; mRNA.
DR AlphaFoldDB; Q9WUB5; -.
DR iPTMnet; Q9WUB5; -.
DR PeptideAtlas; Q9WUB5; -.
DR UCSC; RGD:3612; rat.
DR RGD; 3612; Ncor1.
DR InParanoid; Q9WUB5; -.
DR PhylomeDB; Q9WUB5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0035033; F:histone deacetylase regulator activity; ISO:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:RGD.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:RGD.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:RGD.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; ISO:RGD.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:RGD.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:RGD.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISO:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:1901725; P:regulation of histone deacetylase activity; ISO:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR GO; GO:0051225; P:spindle assembly; ISO:RGD.
DR GO; GO:0021794; P:thalamus development; ISO:RGD.
PE 1: Evidence at protein level;
KW Biological rhythms; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN <1..533
FT /note="Nuclear receptor corepressor 1"
FT /id="PRO_0000055619"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..209
FT /note="ID1"
FT /evidence="ECO:0000250"
FT REGION 145..148
FT /note="Required for interaction with RARA in the absence of
FT its ligand"
FT /evidence="ECO:0000250"
FT REGION 165..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..367
FT /note="ID2"
FT /evidence="ECO:0000250"
FT REGION 382..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..33
FT /note="CORNR box 1"
FT MOTIF 153..157
FT /note="CORNR box 2"
FT MOTIF 357..361
FT /note="CORNR box 3"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 484
FT /note="R -> W (in Ref. 2; AAC14567)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> V (in Ref. 2; AAC14567)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 533 AA; 57795 MW; 7DF60F8228227EC2 CRC64;
KDKGPPPKSR YEEELRTRGK TTITAANFID VIITRQIASD KDARERGSQS SDSSSSLSSH
RYEAPSDAIE VISPASSPAP PQEKPQTYQP EMVKANQAEN ESPQQYEGPL THYRSQQGSP
SPQQQPPLPP SSQAEGMGQV PRTHRLITLA DHICQIITQD FARNQVPSQP STSTFQTSPS
ALSSTPVRTK PSSRYSPESQ SQTVLHPRPG PRVSPENLVD KSRGSRPGKS PERSHIPSEP
YEPISPPQGP AVHEKQDSML LLSQRGMDPA EQRSDSRSPG SISYLPYFFT KLESTSPMVK
SKKQEIFRKL NSSGGGDSDM AAAQPGTEIF NLPAVTTSGA VSSRSHSFAD PASNLGLEDI
IRKALMGSFD DKVEDHGVVM PHPVGVVPGS ASTSVVTSSE TRRDEGDPSP HSGVCKPKLI
NKSNSRKSKS PIPGQNYLGT ERPSSVSSVH SEGDYHRQTP GWAWEDRPSS TGSTQFPYNP
LTIRMLSSTP PTPIACAPSA ITQAAPHQQS RIWEREPAPL LSAQYETLSD SDD
