CIART_MOUSE
ID CIART_MOUSE Reviewed; 375 AA.
AC Q3TQ03; Q3U1B8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Circadian-associated transcriptional repressor;
DE AltName: Full=ChIP-derived repressor of network oscillator;
DE Short=Chrono;
DE AltName: Full=Computationally highlighted repressor of the network oscillator;
GN Name=Ciart; Synonyms=Gm129;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND INTERACTION WITH ARNTL AND PER2.
RX PubMed=24385426; DOI=10.1074/jbc.m113.534651;
RA Annayev Y., Adar S., Chiou Y.Y., Lieb J., Sancar A., Ye R.;
RT "Gene model 129 (Gm129) encodes a novel transcriptional repressor that
RT modulates circadian gene expression.";
RL J. Biol. Chem. 289:5013-5024(2014).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ARNTL AND PER2.
RX PubMed=24737000; DOI=10.1371/journal.pbio.1001840;
RA Anafi R.C., Lee Y., Sato T.K., Venkataraman A., Ramanathan C.,
RA Kavakli I.H., Hughes M.E., Baggs J.E., Growe J., Liu A.C., Kim J.,
RA Hogenesch J.B.;
RT "Machine learning helps identify CHRONO as a circadian clock component.";
RL PLoS Biol. 12:E1001840-E1001840(2014).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ARNTL;
RP PER2; CRY2; BHLHE41; HDAC1 AND NR3C1.
RX PubMed=24736997; DOI=10.1371/journal.pbio.1001839;
RA Goriki A., Hatanaka F., Myung J., Kim J.K., Yoritaka T., Tanoue S., Abe T.,
RA Kiyonari H., Fujimoto K., Kato Y., Todo T., Matsubara A., Forger D.,
RA Takumi T.;
RT "A novel protein, CHRONO, functions as a core component of the mammalian
RT circadian clock.";
RL PLoS Biol. 12:E1001839-E1001839(2014).
CC -!- FUNCTION: Transcriptional repressor which forms a negative regulatory
CC component of the circadian clock and acts independently of the
CC circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a
CC histone deacetylase-dependent manner represses the transcriptional
CC activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Abrogates the
CC interaction of ARNTL/BMAL1 with the transcriptional coactivator CREBBP
CC and can repress the histone acetyl-transferase activity of the CLOCK-
CC ARNTL/BMAL1 heterodimer, reducing histone acetylation of its target
CC genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on
CC circadian gene promoters and its occupancy shows circadian oscillation
CC antiphasic to ARNTL/BMAL1. Interacts with the glucocorticoid receptor
CC (NR3C1) and contributes to the repressive function in the
CC glucocorticoid response. {ECO:0000269|PubMed:24385426,
CC ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:24737000}.
CC -!- SUBUNIT: Interacts with ARNTL/BMAL1, PER2, CRY2, BHLHE41, HDAC1 NR3C1.
CC {ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24736997,
CC ECO:0000269|PubMed:24737000}.
CC -!- INTERACTION:
CC Q3TQ03; Q9WTL8: Arntl; NbExp=3; IntAct=EBI-16101489, EBI-644534;
CC Q3TQ03; Q99PV5: Bhlhe41; NbExp=2; IntAct=EBI-16101489, EBI-6143801;
CC Q3TQ03; Q9R194: Cry2; NbExp=2; IntAct=EBI-16101489, EBI-1266619;
CC Q3TQ03; O09106: Hdac1; NbExp=2; IntAct=EBI-16101489, EBI-301912;
CC Q3TQ03; O54943: Per2; NbExp=2; IntAct=EBI-16101489, EBI-1266779;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Co-localizes
CC with the CLOCK-ARNTL/BMAL1 heterodimer in the PML body.
CC -!- INDUCTION: Expression in the liver oscillates in a circadian manner
CC with highest levels at Zeitgeber time (ZT) 12 hours (at protein level).
CC Expression in the heart, lung, stomach and kidney oscillate in a
CC circadian manner with highest levels at approximately circadian time
CC (CT) 12 hours. Its expression levels peak at circadian time 12 hours
CC (CT12), 8 hours earlier than the peak of PER1/2 and CRY1/2
CC transcriptional repressors (peak CT20-CT24). Thus, it can repress the
CC CLOCK-ARNTL/BMAL1 activity in a different time window compared to CRY
CC and PER proteins. {ECO:0000269|PubMed:24736997,
CC ECO:0000269|PubMed:24737000}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a longer circadian period of
CC locomotor activity, alteration in the expression of core clock genes
CC and impairment of the response of the circadian clock to stress. The
CC peaks of DBP, NR1D1 and PER1 gene expression persists longer in the
CC liver between Zeitgeber times (ZT) 12-14 hours.
CC {ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24736997,
CC ECO:0000269|PubMed:24737000}.
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DR EMBL; AK156084; BAE33580.1; -; mRNA.
DR EMBL; AK164001; BAE37582.1; -; mRNA.
DR CCDS; CCDS50997.1; -.
DR RefSeq; NP_001028474.1; NM_001033302.2.
DR RefSeq; XP_006501437.1; XM_006501374.3.
DR RefSeq; XP_006501438.1; XM_006501375.3.
DR AlphaFoldDB; Q3TQ03; -.
DR DIP; DIP-60818N; -.
DR IntAct; Q3TQ03; 6.
DR STRING; 10090.ENSMUSP00000124943; -.
DR iPTMnet; Q3TQ03; -.
DR PhosphoSitePlus; Q3TQ03; -.
DR PaxDb; Q3TQ03; -.
DR PRIDE; Q3TQ03; -.
DR Antibodypedia; 34023; 147 antibodies from 21 providers.
DR Ensembl; ENSMUST00000036418; ENSMUSP00000049308; ENSMUSG00000038550.
DR Ensembl; ENSMUST00000159739; ENSMUSP00000124943; ENSMUSG00000038550.
DR GeneID; 229599; -.
DR KEGG; mmu:229599; -.
DR UCSC; uc008qll.1; mouse.
DR CTD; 148523; -.
DR MGI; MGI:2684975; Ciart.
DR VEuPathDB; HostDB:ENSMUSG00000038550; -.
DR eggNOG; ENOG502RZ6H; Eukaryota.
DR GeneTree; ENSGT00390000018360; -.
DR HOGENOM; CLU_060548_0_0_1; -.
DR InParanoid; Q3TQ03; -.
DR OMA; GPHCHSL; -.
DR OrthoDB; 972715at2759; -.
DR PhylomeDB; Q3TQ03; -.
DR TreeFam; TF332541; -.
DR BioGRID-ORCS; 229599; 1 hit in 65 CRISPR screens.
DR PRO; PR:Q3TQ03; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3TQ03; protein.
DR Bgee; ENSMUSG00000038550; Expressed in retinal neural layer and 148 other tissues.
DR ExpressionAtlas; Q3TQ03; baseline and differential.
DR Genevisible; Q3TQ03; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR031373; Ciart.
DR PANTHER; PTHR35441; PTHR35441; 1.
DR Pfam; PF15673; Ciart; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..375
FT /note="Circadian-associated transcriptional repressor"
FT /id="PRO_0000251194"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 337
FT /note="D -> A (in Ref. 1; BAE33580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 40408 MW; 707E5DEF7CBF508B CRC64;
MDSPSSVSSY SSSSLSPSFS TSSVNSDFSF PSDNEREGKG THELRPDTVG QRGGSRPSPG
PIRCRHRPRV SSNQHTAPHL EQQGSEVKRS RDGEQETSLN TQGCTTEGDL LFAQKCKELQ
GFIRPLTDLL NGLKMGRFDR GLSSFQQSVA MDRIQRIVGV LQKPQMGERY LGTLLQVEGM
LKTWFPHIAA QKSSSGGSRH QISKHFPSHH GDPGAASPAP LLEKMGQTQL GHLVLKPKQP
WHLTGWPAMN LTWIHSTPIC NPPLSSQGSA SGHSPIGTGA SIGVILVLQK GGQPFTHSAP
GTPVPPTPLS PVVPGDLKKL PGEEPRCHSL PVTLPSDWSC ILCPPVLPTT DREMTKGHPE
PQMTSHPPVA PDPQP
