NCOR1_XENLA
ID NCOR1_XENLA Reviewed; 2498 AA.
AC Q8QG78;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nuclear receptor corepressor 1;
DE Short=N-CoR;
DE Short=N-CoR1;
DE Short=xN-CoR;
GN Name=ncor1;
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], FUNCTION, INTERACTION WITH RXRA AND THRB,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12446772; DOI=10.1128/mcb.22.24.8527-8538.2002;
RA Sachs L.M., Jones P.L., Havis E., Rouse N., Demeneix B.A., Shi Y.-B.;
RT "Nuclear receptor corepressor recruitment by unliganded thyroid hormone
RT receptor in gene repression during Xenopus laevis development.";
RL Mol. Cell. Biol. 22:8527-8538(2002).
RN [2]
RP INTERACTION WITH HDAC1; HDAC2; RBBP4; RXRA; SIN3A; SIN3B AND THRB.
RX PubMed=11254656; DOI=10.1074/jbc.c000879200;
RA Jones P.L., Sachs L.M., Rouse N., Wade P.A., Shi Y.-B.;
RT "Multiple N-CoR complexes contain distinct histone deacetylases.";
RL J. Biol. Chem. 276:8807-8811(2001).
RN [3]
RP PROMOTER BINDING.
RX PubMed=11914274; DOI=10.1101/gad.962502;
RA Li J., Lin Q., Wang W., Wade P.A., Wong J.;
RT "Specific targeting and constitutive association of histone deacetylase
RT complexes during transcriptional repression.";
RL Genes Dev. 16:687-692(2002).
RN [4]
RP FUNCTION.
RX PubMed=12947412; DOI=10.1038/sj.embor.embor908;
RA Havis E., Sachs L.M., Demeneix B.A.;
RT "Metamorphic T3-response genes have specific co-regulator requirements.";
RL EMBO Rep. 4:883-888(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH RARA; RXRA AND TBL1XR1-A.
RX PubMed=12794076; DOI=10.1074/jbc.m303309200;
RA Tomita A., Buchholz D.R., Obata K., Shi Y.-B.;
RT "Fusion protein of retinoic acid receptor-alpha with promyelocytic leukemia
RT protein or promyelocytic leukemia zinc finger protein recruits N-CoR-TBLR1
RT corepressor complex to repress transcription in vivo.";
RL J. Biol. Chem. 278:30788-30795(2003).
RN [6]
RP FUNCTION, INTERACTION WITH RXRA; THRB AND TBL1XR1-A, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15060155; DOI=10.1128/mcb.24.8.3337-3346.2004;
RA Tomita A., Buchholz D.R., Shi Y.-B.;
RT "Recruitment of N-CoR/SMRT-TBLR1 corepressor complex by unliganded thyroid
RT hormone receptor for gene repression during frog development.";
RL Mol. Cell. Biol. 24:3337-3346(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH ZBTB33.
RX PubMed=15935774; DOI=10.1016/j.devcel.2005.04.010;
RA Park J.-I., Kim S.-W., Lyons J.P., Ji H., Nguyen T.T., Cho K., Barton M.C.,
RA Deroo T., Vleminckx K., Moon R.T., McCrea P.D.;
RT "Kaiso/p120-catenin and TCF/beta-catenin complexes coordinately regulate
RT canonical Wnt gene targets.";
RL Dev. Cell 8:843-854(2005).
CC -!- FUNCTION: Mediates transcriptional repression by certain nuclear
CC receptors. Participates in complexes which promote histone
CC deacetylation and the formation of repressive chromatin structures
CC which may impede access by the basal transcription machinery. In
CC association with hdac3, may play a role in the regulation of the
CC circadian clock (By similarity). {ECO:0000250|UniProtKB:Q60974,
CC ECO:0000269|PubMed:12446772, ECO:0000269|PubMed:12794076,
CC ECO:0000269|PubMed:12947412, ECO:0000269|PubMed:15060155,
CC ECO:0000269|PubMed:15935774}.
CC -!- SUBUNIT: Forms a large corepressor complex that contains sin3a/b,
CC histone deacetylases hdac1 and hdac2, rbbp4 and possibly rbbp7.
CC Interacts with the thyroid receptor (TR, composed of rxra and thrb) and
CC the retinoid acid receptor (RAR, composed of rxra and rara) in the
CC absence of ligand. Interacts with tbl1xr1-A and possibly tbl1xr1-B.
CC Interacts with zbtb33/kaiso. {ECO:0000269|PubMed:11254656,
CC ECO:0000269|PubMed:12446772, ECO:0000269|PubMed:12794076,
CC ECO:0000269|PubMed:15060155, ECO:0000269|PubMed:15935774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing intestine both prior
CC to and during remodeling (stages NF54 to NF66). Also expressed at high
CC levels in the tail during tail regression (stages NF62 and NF64) and in
CC the hindlimbs during hindlimb morphogenesis (stage NF56).
CC {ECO:0000269|PubMed:12446772, ECO:0000269|PubMed:15060155}.
CC -!- INDUCTION: By thyroid hormone in the developing intestine and tail.
CC {ECO:0000269|PubMed:12446772}.
CC -!- DOMAIN: The CORNR box motifs in the C-terminal region may be necessary
CC and sufficient for binding to unligated nuclear hormone receptors.
CC Sequences flanking these motifs may determine the precise nuclear
CC hormone receptor specificity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000305}.
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DR EMBL; AF495886; AAM12658.1; -; mRNA.
DR RefSeq; NP_001082225.1; NM_001088756.1.
DR AlphaFoldDB; Q8QG78; -.
DR SMR; Q8QG78; -.
DR BioGRID; 99637; 5.
DR PRIDE; Q8QG78; -.
DR GeneID; 398304; -.
DR KEGG; xla:398304; -.
DR CTD; 398304; -.
DR Xenbase; XB-GENE-864966; ncor1.S.
DR OrthoDB; 853340at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 398304; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR031557; N-CoR_GPS2_interact.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF15784; GPS2_interact; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51293; SANT; 2.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2498
FT /note="Nuclear receptor corepressor 1"
FT /id="PRO_0000055620"
FT DOMAIN 427..478
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 628..665
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..304
FT /note="Interaction with tbl1xr1-A"
FT REGION 198..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2136..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2344..2446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..208
FT /evidence="ECO:0000255"
FT COILED 502..552
FT /evidence="ECO:0000255"
FT COILED 1765..1804
FT /evidence="ECO:0000255"
FT MOTIF 2012..2016
FT /note="CORNR box 1"
FT MOTIF 2123..2127
FT /note="CORNR box 2"
FT MOTIF 2326..2330
FT /note="CORNR box 3"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2136..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2352..2381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2389..2420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2429..2446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2498 AA; 277828 MW; 8A026610EB227C93 CRC64;
MSSSGYPPNQ GAFSTEQGRY SSHPVQYTFP SSRHQQEYSV SEYRTAHLEA SQLIQQQQLR
RRPSLLSEFH PVSDRPQDRR SGYDQQYHSI SQNEHEALES KRPRLDQVSD SHYRLNPAMV
LLVPTIQEGV RVQSEVKKEQ GLSSKHESSS SPLSGQPGDD QDASPSKLSK EELIQSMDRV
DREIAKVEQQ ILKLKKKQQQ LEEEAAKPPE PEKPVSPPPV EQKHRSVVQI IYDENRKKAE
EAHKFLEGLG PKVELPLYNQ PSDTKVYHEN IKTNQVMRKK LILFFKRRNH ARKLREQNIC
QRYDQLMEAW EKKVDRIENN PRRKAKESKT REYYEKQFPE IRKQREQQER FQRVGQRGTG
MSATIARSEH EISEIIDGLS EQENNEKQMR QLSVIPPMMF DAEQRRVKFI NTNGLMEDPM
KVYKDRQFMN VWTDHEKEIF KEKFVRHPKN FGLIASYLER KNVSDCVLYY YLTKKNENLK
SLVRRNYPKR RGRNQQQITR PSQEEKEIEK VEEEKADRND KKEDERREEE EKEEKEELRE
GAKDKIDAVA EDGDEKDQSM PRGRKTANNQ GRRKGRVTRS MASEAAAANA VTTATTAPVT
TTSTATTVAP VPVAPPPEEP TPPPPPQEQS LVDHGRNWGA IAKMVGSKSE SQCKNFYFNY
KRRHNLDNLL QQHKQKSSRR PREERDVSQC DSIASTVSAQ EDDENEASNE EENPEDSEGA
ENSSDTESAP SPSPAEAARL GDDSVDRTTS SVSMEAPPEQ DAASKPASDS SPSPIVENTK
PPETQYAELK VKEEISTENE QTMEVEERSQ SAELKSALNL QVQTKAEPYE TEAKPTESTT
QVKTEVDSKE DDSMERLMDR AEAADMGYAP PQNISQARQE SQPDNDSSAT CSADEEVDGE
PDRPRMYSFG SRPSLLNQAG TFLKQGPMDL QQLQHRAAVI PPMTSCSPCN LTTGTAIAAS
NFSMYQRHLY ENSLLEEQRQ RQEQLTLENR MSASPGNMSK SPNMDWEGKS VYMPYTEVKH
PFEHEAQMQN VARSVSPYRL SPRDVGRVSP QVDMNPSRYC VPPVLQPAPH QVITSLSDSA
RLPVTRPTRP PPPLIPSSKT SATSSDKPSF ITGGSISQGT PGTYLASLSQ PYSQETLKPS
VGSISLGLPR QHESTKIGCV TYIKQEEFPS RGQSSQPEGL LVRAQHEGVV RGSMAAIQEG
SIARGTPATK VPLEAVSTLR GSITQGTPAL SQSGIAADVL LKSTITRLAA EDIGSPERCR
EDTSAKGHVI YEGKSGHIVS YDTIKNMREG TRSPRTAPEV ALKRAYDTME GNIKQAMSVR
EAAVSGPMEG LICRTLPKGS PHPELKDRQV LSGSIMKGTP RTTSDNFDDG LKYAKQIKLE
SPPIRSFEGA ISKGKPYEGV TTIKELGRSI HEIPRQDLVS QESRKTPESS RQIMEGSISQ
GTPIKYESTS GQSAIKHNVK SLITGPSNLS WGVPQMDNMP ENLKMGERSK HEDTKSSDAI
RSRHTSVVSS GPSVLRSTLH EASKSQLSPG IYEDNNARRT PVNYPSPMSR SSPMARSAEG
CLTPSKSSSH ERKSTLTPTQ RESIVVKSPV PGVDPSAAHS PFDTHLRSAP PGDVYRAHLP
PHLDPALQFH RPLDPAAAAY LFQRQLSPTP GYPSQYQLYA MENTRQTILN DYITSQQMQV
NLRPDVARGL SPRDQGLGIP YPGARGIIDL TNMPPAILVP HPGGTSTPPM DRITYIPGTQ
LAFPPRPYNP ASMSPGHPAH LANSVSAERE RERERERERD REREKEQRER ESDRERERDR
LAHAAAAAAA ASAPSEHYLR PVSEQPSRPS SRPSSHGYVR SPSPSVRAQE SIMQQRPSIF
LGTNGKSVIT PLDAAQFRIM PPTPGAASIT QGIPASRYST AADALAALVD AATSAPQMEV
AKPKESKNDS ARSEENLSRR NALEQQQQID CERRVMQSPY TSSSFSSSKS QSQPSSAVYS
EAGKERTAHT KSRYVEELRM RGKTTITAAN FIDVIITQQI ASDKDGRERN SQSSDASSSH
SSHRYEAPRE TIEVISPANS PVQEKESYPQ EMPKSSQTET GEGSRKYDGQ PNRYRQQQES
PPQQTIPGHV PQTHRLITLA DHICHIITQD FARNQPVNQP LQQPPASTFQ STNPTSTAVR
TKASSRFSPE SQVQPMHSPR PASRVSPENI PDKPRGRPGK SPDRGHISEP YEPISPPQAP
MLHTKQDNMM LLSQRQEPPE QRNDSRSPGN INYLPSFFTK LENTSPMVMY KKQEIFRKLN
SSGGGDSDMA AAQPGTEIFN LPAVTTSGAI SSRGHSFADP ASNLGLEDII RKALMGNFDD
KSEDHGVLVG VPQGNQSGTP NSEARREEAN PSPNSGGGTH KQKLISKYGS RKTKSPISGS
QTYLGAERPS SVSSVHSEGD YRQASAWAWE DRPSSTGSTQ FPYNPLTMGM LNSTPPSSMS
CIPTSMTQTS AHQQSRIWER EPAPLLSEQY ETLSDSDE
