C1D_MOUSE
ID C1D_MOUSE Reviewed; 141 AA.
AC O35473; Q5SWJ6; Q61368;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Nuclear nucleic acid-binding protein C1D;
DE Short=mC1D;
DE AltName: Full=Small unique nuclear receptor corepressor;
DE Short=Sun-CoR;
DE Short=SunCoR;
GN Name=C1d; Synonyms=Suncor;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH NR1D1; THRA; THRB; NCOR1
RP AND NCOR2.
RX PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.;
RT "Cloning and characterization of a corepressor and potential component of
RT the nuclear hormone receptor repression complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC STRAIN=NMRI; TISSUE=Ascitic tumor;
RX PubMed=9469821; DOI=10.1093/nar/26.5.1160;
RA Nehls P., Keck T., Greferath R., Spiess E., Glaser T., Rothbarth K.,
RA Stammer H., Werner D.;
RT "cDNA cloning, recombinant expression and characterization of polypeptides
RT with exceptional DNA affinity.";
RL Nucleic Acids Res. 26:1160-1166(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=10362552; DOI=10.1242/jcs.112.13.2223;
RA Rothbarth K., Spiess E., Juodka B., Yavuzer U., Nehls P., Stammer H.,
RA Werner D.;
RT "Induction of apoptosis by overexpression of the DNA-binding and DNA-PK-
RT activating protein C1D.";
RL J. Cell Sci. 112:2223-2232(1999).
CC -!- FUNCTION: Plays a role in the recruitment of the RNA exosome complex to
CC pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this
CC function may include MPHOSPH6. Can activate PRKDC not only in the
CC presence of linear DNA but also in the presence of supercoiled DNA. Can
CC induce apoptosis in a p53/TP53 dependent manner. May regulate the
CC TRAX/TSN complex formation. Potentiates transcriptional repression by
CC NR1D1 and THRB (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10362552, ECO:0000269|PubMed:9405624}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with EXOSC10; the interaction
CC probably mediates the association with the nuclear form of the RNA
CC exosome. The homodimeric form interacts with TSNAX following gamma-
CC radiation. Interacts with RAC3 (By similarity). Interacts with NR1D1,
CC THRA, THRB, NCOR1 and NCOR2. {ECO:0000250, ECO:0000269|PubMed:9405624,
CC ECO:0000269|PubMed:9469821}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9405624}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar
CC localization. Colocalizes with TSNAX in the nucleus.
CC {ECO:0000250|UniProtKB:Q13901}.
CC -!- TISSUE SPECIFICITY: Kidney, heart, brain, spleen, lung, testis, liver
CC and small intestine. {ECO:0000269|PubMed:9405624}.
CC -!- INDUCTION: Up-regulated during adipocyte and myogenic differentiation.
CC {ECO:0000269|PubMed:9405624}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the C1D family. {ECO:0000305}.
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DR EMBL; AF031426; AAC53520.1; -; Genomic_DNA.
DR EMBL; X95591; CAA64844.1; -; mRNA.
DR EMBL; AK028702; BAC26075.1; -; mRNA.
DR EMBL; AK035169; BAC28967.1; -; mRNA.
DR EMBL; AL603925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005436; AAH05436.1; -; mRNA.
DR CCDS; CCDS24451.1; -.
DR RefSeq; NP_001317578.1; NM_001330649.1.
DR RefSeq; NP_065583.2; NM_020558.4.
DR AlphaFoldDB; O35473; -.
DR SMR; O35473; -.
DR CORUM; O35473; -.
DR STRING; 10090.ENSMUSP00000000594; -.
DR iPTMnet; O35473; -.
DR PhosphoSitePlus; O35473; -.
DR MaxQB; O35473; -.
DR PaxDb; O35473; -.
DR PeptideAtlas; O35473; -.
DR PRIDE; O35473; -.
DR ProteomicsDB; 273723; -.
DR Antibodypedia; 30893; 299 antibodies from 33 providers.
DR DNASU; 57316; -.
DR Ensembl; ENSMUST00000000594; ENSMUSP00000000594; ENSMUSG00000000581.
DR GeneID; 57316; -.
DR KEGG; mmu:57316; -.
DR UCSC; uc007ice.1; mouse.
DR CTD; 10438; -.
DR MGI; MGI:1927354; C1d.
DR VEuPathDB; HostDB:ENSMUSG00000000581; -.
DR eggNOG; KOG4835; Eukaryota.
DR GeneTree; ENSGT00390000015405; -.
DR InParanoid; O35473; -.
DR OMA; KLMSMPR; -.
DR OrthoDB; 1436833at2759; -.
DR PhylomeDB; O35473; -.
DR TreeFam; TF314651; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 57316; 23 hits in 73 CRISPR screens.
DR ChiTaRS; C1d; mouse.
DR PRO; PR:O35473; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35473; protein.
DR Bgee; ENSMUSG00000000581; Expressed in pharyngeal arch 2 and 253 other tissues.
DR ExpressionAtlas; O35473; baseline and differential.
DR Genevisible; O35473; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR011082; Exosome-assoc_fac/DNA_repair.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR PANTHER; PTHR15341; PTHR15341; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW rRNA processing; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..141
FT /note="Nuclear nucleic acid-binding protein C1D"
FT /id="PRO_0000316301"
FT REGION 1..100
FT /note="Required for transcriptional repression"
FT REGION 50..100
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000269|PubMed:9405624"
FT REGION 100..141
FT /note="Interaction with NCOR1 and NCOR2"
FT /evidence="ECO:0000269|PubMed:9405624"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13901"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13901"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13901"
FT CONFLICT 120
FT /note="N -> K (in Ref. 2; CAA64844)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> R (in Ref. 2; CAA64844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 15945 MW; C9AF68033A0FD04E CRC64;
MAGEEMNEDY PVEIHESLTA LESSLGAVDD MLKTMMAVSR NELLQKLDPL EQAKVDLVSA
YTLNSMFWVY LATQGVNPKE HPVKQELERI RVYMNRVKEI TDKKKAAKLD RGAASRFVKN
ALWEPKAKST PKVANKGKSK H
