CIPC_MOUSE
ID CIPC_MOUSE Reviewed; 432 AA.
AC Q8R0W1; Q3TUN6; Q3U423; Q3UFM0; Q80T99; Q8C680;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 4.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CLOCK-interacting pacemaker;
DE AltName: Full=CLOCK-interacting circadian protein;
GN Name=Cipc; Synonyms=Kiaa1737;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH CLOCK.
RX PubMed=17310242; DOI=10.1038/ncb1539;
RA Zhao W.N., Malinin N., Yang F.C., Staknis D., Gekakis N., Maier B.,
RA Reischl S., Kramer A., Weitz C.J.;
RT "CIPC is a mammalian circadian clock protein without invertebrate
RT homologues.";
RL Nat. Cell Biol. 9:268-275(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; 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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP FUNCTION.
RX PubMed=19414601; DOI=10.1128/mcb.01864-08;
RA Yoshitane H., Takao T., Satomi Y., Du N.H., Okano T., Fukada Y.;
RT "Roles of CLOCK phosphorylation in suppression of E-box-dependent
RT transcription.";
RL Mol. Cell. Biol. 29:3675-3686(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25862660; DOI=10.1007/s11427-015-4828-1;
RA Qu Z., Wang X., Liu D., Gao X., Xu Y.;
RT "Inactivation of Cipc alters the expression of Per1 but not circadian
RT rhythms in mice.";
RL Sci. China Life Sci. 58:368-372(2015).
CC -!- FUNCTION: Transcriptional repressor which may act as a negative-
CC feedback regulator of CLOCK-ARNTL/BMAL1 transcriptional activity in the
CC circadian-clock mechanism. May stimulate ARNTL/BMAL1-dependent
CC phosphorylation of CLOCK (PubMed:17310242, PubMed:19414601). However,
CC the physiogical relevance of these observations is unsure, since
CC experiments in knockout mice showed that CIPC is not critially required
CC for basic circadian clock (PubMed:25862660).
CC {ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:19414601,
CC ECO:0000269|PubMed:25862660}.
CC -!- SUBUNIT: Interacts with CLOCK. Forms a ternary complex with the CLOCK-
CC ARNTL/BMAL1 heterodimer. Interacts with CAD AND HSPA5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9C0C6, ECO:0000269|PubMed:17310242}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17310242}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q9C0C6}. Note=Predominantly localizes to
CC the nucleus, where it co-localizes with CLOCK. At the G1/S boundary,
CC partially translocated to the cytosol. {ECO:0000250|UniProtKB:Q9C0C6,
CC ECO:0000269|PubMed:17310242}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0W1-2; Sequence=VSP_055396;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, kidney and liver and shows
CC a circadian oscillation in these tissues with a peak at circadian time
CC 14 hours (at protein level). Expressed in the brain, including the
CC suprachiasmatic nucleus (SCN) of the brain, and in multiple peripheral
CC tissues such as heart, liver and kidney. Exhibits a circadian
CC oscillation in the peripheral tissues with a peak at circadian time 14
CC hours. {ECO:0000269|PubMed:17310242}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Knockout mice display
CC normal locomotor activity rhythms and normal behavioral responses to
CC light. Animals show reduction liver PER1 peak levels, but no change in
CC the expression of other core clock genes.
CC {ECO:0000269|PubMed:25862660}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-36 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65828.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122546; BAC65828.1; ALT_INIT; mRNA.
DR EMBL; AK076398; BAC36322.1; -; mRNA.
DR EMBL; AK148415; BAE28540.1; -; mRNA.
DR EMBL; AK154476; BAE32612.1; -; mRNA.
DR EMBL; AK160643; BAE35935.1; -; mRNA.
DR EMBL; BC026384; AAH26384.1; -; mRNA.
DR RefSeq; NP_001276359.1; NM_001289430.1.
DR RefSeq; NP_776096.2; NM_173735.3.
DR RefSeq; XP_011242380.1; XM_011244078.2.
DR PDB; 5VJI; X-ray; 1.86 A; C/F=352-414.
DR PDB; 5VJX; X-ray; 2.69 A; A/D/G/J/M/R/U/X/a/d=352-414.
DR PDBsum; 5VJI; -.
DR PDBsum; 5VJX; -.
DR AlphaFoldDB; Q8R0W1; -.
DR SMR; Q8R0W1; -.
DR IntAct; Q8R0W1; 4.
DR STRING; 10090.ENSMUSP00000141049; -.
DR iPTMnet; Q8R0W1; -.
DR PhosphoSitePlus; Q8R0W1; -.
DR MaxQB; Q8R0W1; -.
DR PaxDb; Q8R0W1; -.
DR PRIDE; Q8R0W1; -.
DR ProteomicsDB; 283921; -. [Q8R0W1-1]
DR ProteomicsDB; 283922; -. [Q8R0W1-2]
DR Antibodypedia; 99; 40 antibodies from 9 providers.
DR Ensembl; ENSMUST00000187814; ENSMUSP00000141049; ENSMUSG00000034157. [Q8R0W1-1]
DR Ensembl; ENSMUST00000191463; ENSMUSP00000140683; ENSMUSG00000034157. [Q8R0W1-2]
DR GeneID; 217732; -.
DR KEGG; mmu:217732; -.
DR UCSC; uc007oib.4; mouse. [Q8R0W1-1]
DR UCSC; uc007oid.4; mouse. [Q8R0W1-2]
DR CTD; 85457; -.
DR MGI; MGI:1919185; Cipc.
DR VEuPathDB; HostDB:ENSMUSG00000034157; -.
DR eggNOG; ENOG502RJ2N; Eukaryota.
DR GeneTree; ENSGT00510000048522; -.
DR InParanoid; Q8R0W1; -.
DR OrthoDB; 1183035at2759; -.
DR PhylomeDB; Q8R0W1; -.
DR BioGRID-ORCS; 217732; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cipc; mouse.
DR PRO; PR:Q8R0W1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R0W1; protein.
DR Bgee; ENSMUSG00000034157; Expressed in right colon and 249 other tissues.
DR ExpressionAtlas; Q8R0W1; baseline and differential.
DR Genevisible; Q8R0W1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR031602; CIPC.
DR PANTHER; PTHR34648; PTHR34648; 1.
DR Pfam; PF15800; CiPC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Coiled coil;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..432
FT /note="CLOCK-interacting pacemaker"
FT /id="PRO_0000256134"
FT REGION 71..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..395
FT /evidence="ECO:0000255"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0C6"
FT VAR_SEQ 1..17
FT /note="MRLLTRRAGHGAATLAL -> MLQVMTSYVIVVFH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_055396"
FT CONFLICT 8
FT /note="A -> T (in Ref. 4; AAH26384)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="I -> L (in Ref. 3; BAE32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="A -> S (in Ref. 3; BAE32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> I (in Ref. 3; BAE32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="T -> S (in Ref. 3; BAC36322)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> R (in Ref. 3; BAE35935)"
FT /evidence="ECO:0000305"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:5VJI"
FT HELIX 362..396
FT /evidence="ECO:0007829|PDB:5VJI"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5VJX"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:5VJI"
SQ SEQUENCE 432 AA; 46320 MW; E304D1F0D8D70D9A CRC64;
MRLLTRRAGH GAATLALRVI HMQRVPVLRL PAILDMERKI PSRESPRRLS AKPGRGTEMK
KLARPLGVVA ADSDKDSGFS DGSSECLSSA EQMESEDMLS ALGCKREDKR RQPSKAADTA
LPTLPPMVVM KSVLVKQGSS SSQLQSWTVQ PSFEVISAQP QLFVLHPPVP SPVSSCQTGE
KKSESRNYLP ILNSYTKIAP HPGKRGLNSE DRGTSGVSKK LCTERPGPSL SSSEPAKTGR
VLSSPSTPAP PSSKLTEDST LQGVPSLGAG GSPQTLQPVS SSHVAKAPSL TLASPASPVC
ASDSTLHGLE SSSPLSPLSA SYTSPLWAAE HLCRSPDIFS EQRQNKHRRF QNTLVVLHKS
GLLEITLKTK ELIRQNQATQ AELDQLKEQT QMFIEATKSR APQAWAKLQA SLTSGSSHSG
SDLDTLSDHP DV
