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NCOR1_XENTR
ID   NCOR1_XENTR             Reviewed;        2494 AA.
AC   Q4KKX4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Nuclear receptor corepressor 1;
DE            Short=N-CoR;
DE            Short=N-CoR1;
DE            Short=xN-CoR;
GN   Name=ncor1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). In association with hdac3, may play a role in the
CC       regulation of the circadian clock (By similarity).
CC       {ECO:0000250|UniProtKB:Q60974, ECO:0000250|UniProtKB:Q8QG78}.
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. Interacts with zbtb33/kaiso
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
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; BC099620; AAH99620.1; -; mRNA.
DR   RefSeq; NP_001027513.1; NM_001032342.1.
DR   AlphaFoldDB; Q4KKX4; -.
DR   SMR; Q4KKX4; -.
DR   STRING; 8364.ENSXETP00000014702; -.
DR   PaxDb; Q4KKX4; -.
DR   PRIDE; Q4KKX4; -.
DR   GeneID; 613105; -.
DR   KEGG; xtr:613105; -.
DR   CTD; 9611; -.
DR   Xenbase; XB-GENE-483288; ncor1.
DR   eggNOG; KOG1878; Eukaryota.
DR   InParanoid; Q4KKX4; -.
DR   OrthoDB; 12227at2759; -.
DR   Reactome; R-XTR-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-XTR-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-XTR-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-XTR-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   Reactome; R-XTR-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
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   PROSITE; PS51293; SANT; 2.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Chromatin regulator; Coiled coil; DNA-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..2494
FT                   /note="Nuclear receptor corepressor 1"
FT                   /id="PRO_0000055621"
FT   DOMAIN          427..478
FT                   /note="SANT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          622..668
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          53..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..304
FT                   /note="Interaction with tbl1xr1"
FT                   /evidence="ECO:0000250"
FT   REGION          198..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1081..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1413..1434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1488..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1745..1845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1912..1987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2018..2105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2135..2216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2346..2413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2446..2494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          168..208
FT                   /evidence="ECO:0000255"
FT   COILED          502..549
FT                   /evidence="ECO:0000255"
FT   COILED          698..726
FT                   /evidence="ECO:0000255"
FT   COILED          1771..1810
FT                   /evidence="ECO:0000255"
FT   MOTIF           2008..2012
FT                   /note="CORNR box 1"
FT   MOTIF           2119..2123
FT                   /note="CORNR box 2"
FT   MOTIF           2322..2326
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        587..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..725
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..863
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        987..1006
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1413..1427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1488..1503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1565..1585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1771..1811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1914..1932
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1933..1973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2085..2105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2135..2181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2186..2203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2348..2377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2385..2413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2446..2472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2494 AA;  277212 MW;  7E862943961012FA CRC64;
     MSSSGYPPNQ GAFSTEQGRY SSHPVQYTFP SSRHQQEFPV PEYRSSHLEA SQLLQQQQLR
     RRPSLLSEFH PVSDRPQDRR QGYEQQYHSV TQNEHEALES KRPRLDVSDS HYRVGAASVV
     PLVPTIQEGV RVQSEVKKEQ GLPSKHETTS SPLSGQPGEE QEASPSKLSK EELIQSMDRV
     DREIAKVEQQ ILKLKKKQQQ LEEEAAKPPE PEKPVSPPPV EQKHRSIVQI IYDENRKKAE
     EAHKILEGLG PKVELPLYNQ PSDTKVYHEN IKTNQVMRKK LILFFKRRNH ARKLREQNIC
     QRYDQLMEAW EKKVDRIENN PRRKAKESKT REYYEKQFPE IRKQREQQER FQRVGQRGAG
     LSATIARSEH EISEIIDGLS EQENNEKQMR QLSVIPPMMF DAEQRRVKFI NMNGLMEDPM
     KVYKDRQFMN VWTDHEKEIF KEKFVQHPKN FGLIASYLER KTVSDCVLYY YLTKKNENFK
     ALVRRNYPKR RGRNQQQITR PAQEEKEIEK VEEEKAERND KKEEERREEE EKEEKEELRD
     GTKDRTDAIA EDGEDKEQST PRGRKTANSQ GRRKGRITRS MASEAAAAAN AASTATTAPA
     TTTSTTATTT TAALVPVAPP PEEPTPPPTQ EQSLVEHGRN WGAIAKMVGS KSESQCKNFY
     FNYKRRHNLD NLLQQHKQKS SRRPREERDV SQCESVASTV SAQEDEENEA SNEEENAEDS
     EGAENSSDTE SAPSPSPAEA AKLGDDAVDR TTSSVSIEAP PEQDAASKSV SDSSPTPTVE
     NIKPPETQYT ELKVKEEIST ETEEAMEVEE RSQGAEIKST LSLPVQTKAE PDEVESKPSE
     SAEVKIEEDT KDQDMERLMD RAEATDMVYA PPLHISRGRQ ESQSDNDSSA TCSADEEVDG
     EPERPRIYTL DSKPSLLNPA GTILISSSMK QGPMDLQQLQ HRAAVIPPMA SCSPCNITTG
     TSNFSMYQRH LYENNLLEEQ RQRQEQLSLE SRMSASPGNM SKSPNMDWEG KSVYMPYTEV
     KRAFEHEAQM QNVARSVSPY RLSPREVSRA SPQVDMNPAR YCVPPVLQPA PHQVITSLSD
     GARLPVTRPT RPPPPLIPSS KTSATSSDKP SFITGGSISQ GTPGTYLTSL SQSYSQETVK
     PSVGSISLGL PRQQESAKTG SVTYIKQEEF SPRGQSSQPE GLLVRAQHEG VVRGTMTAIQ
     EGSITRGTPA TKVPIEAVST LRGSITQGTP ALSQSGIAAD VLLKTTITRL ATEDIGSPER
     CRDETSAKGH VIYEGKSGHI VSYDTAIKNM REGTRSPRTA PEVTLKRTFD TMEGNIKQAM
     SVREAAVSGP MEGLICRTLP KGSTHAEIKD RQVLSGSIMK GTPRTTSDSF EDGLKYAKQI
     KLESPPIRSF EGAISKGKPY ECVTTIKEMG RSIHEIPRQD LGSQESRKTP ESSRQIIEGS
     ISQGTPIKYE GTSGQSAIKH NVKSLITGPS NLSRGLPQME VMPENLKMGE RSKYEDTKSS
     EAIRSRHTSV VSSGPSVLRS TLHEASKSQL SPGVYEDNNA RRTPVNYPSP MSRSSPMARS
     AEVGLTPGKS SSHERKSTLT PTQRENIVVK SPVPGVDPTA AHSPFDPHLR GAPPGDVYRT
     HLPPHLDPAL QFHRPLDPAA AAAYLFQRQL SPTPGYPSQY QLYAMENTRQ TILNDYITSQ
     QMQVNLRPDV ARGLSPRDQG LAIPYPGARG IIDLTNMPPA ILVPHPGGTS TPPMDRITYI
     PGTQLAFPPR PYNPASMSPG HPTHLAAANS VSAERERERE RDRERDRERE KEQRERERDR
     ERERERLAAA PSDHYLRPVS EQPGRPGSHG FVRSPSPSVR AQESIMQQRP SIFQGTNGKS
     VITPLDAAQL RIMPPTPGAA SITQGIPASR YSTAADALAA LVDAAASAPQ MEVVKPKEMK
     HDPARSEESL SRRNVLEQQQ QQQQIDCERR VMQSPYTSSS FSGSKSQGQP SPAVYSEAGK
     EKTAHTKSRY VEELRMRGKT TITAANFIDV IITQQIASDK DGRDRNSQSS DSSSSHSSHR
     YDAPRDTIEV ISPANSPVQE KESYPPEIPK SSQTESESSR KYEGQPNRYR QQQESPSPQQ
     TIPGHVPQTH RLITLADHIC QIITQDFARN QPVNQALQQP PASTFQSTNP SSTPVRTKAS
     SRFSPESQVQ PVHNQRPASR VSPENVLDRP RGRPGKSPDR GHISEPYEPI SPPQAPLLHA
     KQDSMLLLSQ RQEPPEQRND SRSPGNISYL PSFFTKLENT SPMVMYKKQE IFRKLNSSGG
     GDSEMAAAQP GTEIFNLPAV TTSGAISSRG HSFADPASNL GLEDIIRKAL MGNFDDKSED
     HSVLVGVAQG NPSGTQNSEA RREEANPSPN SGGGTHKQKL ISKYGSRKTK SPISGSQTYL
     GAERPSSVSS VHSEGDYRQA SAWAWEDRPS STGSTQFPYN PLTMGMLNST PPSSMSCAPT
     SMTQTSAHQQ SRIWEREPAP LLSEQYETLS DSDE
 
 
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