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Circadian locomoter output cycles protein kaput (dCLOCK) (dPAS1)

 CLOCK_DROME             Reviewed;        1027 AA.
O61735; A4V1L9; A4V1M0; O76342; O77137; Q59E25; Q9VSB0;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 3.
28-MAR-2018, entry version 176.
RecName: Full=Circadian locomoter output cycles protein kaput;
AltName: Full=dCLOCK;
AltName: Full=dPAS1;
Name=Clk; Synonyms=CLOCK, jrk, PAS1; ORFNames=CG7391;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
TISSUE=Head;
PubMed=9630223; DOI=10.1016/S0092-8674(00)81440-3;
Allada R., White N.E., So W.V., Hall J.C., Rosbash M.;
"A mutant Drosophila homolog of mammalian Clock disrupts circadian
rhythms and transcription of period and timeless.";
Cell 93:791-804(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
STRAIN=Canton-S;
PubMed=9742131; DOI=10.1128/MCB.18.10.6142;
Bae K., Lee C., Sidote D., Chuang K.-Y., Edery I.;
"Circadian regulation of a Drosophila homolog of the mammalian clock
gene: PER and TIM function as positive regulators.";
Mol. Cell. Biol. 18:6142-6151(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Head;
PubMed=9616122; DOI=10.1126/science.280.5369.1599;
Darlington T.K., Wager-Smith K., Ceriani M.F., Staknis D., Gekakis N.,
Steeves T.D.L., Weitz C.J., Takahashi J.S., Kay S.A.;
"Closing the circadian loop: CLOCK-induced transcription of its own
inhibitors per and tim.";
Science 280:1599-1603(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
-!- FUNCTION: Circadian regulator that acts as a transcription factor
and generates a rhythmic output with a period of about 24 hours.
Oscillates in antiphase to the cycling observed for period (PER)
and timeless (TIM). According to PubMed:9742131, reaches peak
abundance within several hours of the dark-light transition at ZT0
(zeitgeber 0), whereas PubMed:9616122 describes bimodal
oscillating expression with maximum at ZT5 and ZT23. Clock-cycle
heterodimers activate cycling transcription of PER and TIM by
binding to the E-box (5'-CACGTG-3') present in their promoters.
Once induced, Period and Timeless block Clock's ability to
transactivate their promoters. {ECO:0000269|PubMed:9630223}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Forms a heterodimer with Cycle.
-!- INTERACTION:
P08181:CkIIalpha; NbExp=2; IntAct=EBI-143834, EBI-93115;
O61734:cyc; NbExp=3; IntAct=EBI-143834, EBI-87683;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=D;
IsoId=O61735-1; Sequence=Displayed;
Name=A;
IsoId=O61735-2; Sequence=VSP_010320;
Name=F;
IsoId=O61735-3; Sequence=VSP_026493;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Found in head, body, and
appendage fractions.
-!- DOMAIN: Contains three polyglutamine repeats which could
correspond to the transactivation domain. The length of the
repeats is polymorphic. In the arrhythmic mutant JRK, deletion of
this region leads to the loss of circadian rhythmicity and altered
light response.
-!- POLYMORPHISM: The variability in length of the polyglutamine
stretch is due to polymorphism of this region. Variant B encodes
two conceptual proteins, the first consists only of the bHLH
domain, the other consists of the PAS-1 and all C-terminal
domains. Variant B is expressed weakly at all the times of the
day, and it cycles in phase with the full-length form.
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EMBL; AF065133; AAC39101.1; -; mRNA.
EMBL; AF069997; AAC62234.1; -; mRNA.
EMBL; AF067207; AAD10630.1; -; mRNA.
EMBL; AE014296; AAF50516.1; -; Genomic_DNA.
EMBL; AE014296; AAX52753.1; -; Genomic_DNA.
EMBL; AE014296; AAX52754.1; -; Genomic_DNA.
PIR; T13062; T13062.
PIR; T13068; T13068.
PIR; T13071; T13071.
RefSeq; NP_001014574.1; NM_001014574.2. [O61735-3]
RefSeq; NP_001014576.1; NM_001014576.2. [O61735-1]
RefSeq; NP_523964.2; NM_079240.3. [O61735-2]
UniGene; Dm.7596; -.
ProteinModelPortal; O61735; -.
SMR; O61735; -.
BioGrid; 64302; 24.
DIP; DIP-46595N; -.
IntAct; O61735; 20.
MINT; O61735; -.
STRING; 7227.FBpp0099478; -.
iPTMnet; O61735; -.
PaxDb; O61735; -.
PRIDE; O61735; -.
EnsemblMetazoa; FBtr0076785; FBpp0076500; FBgn0023076. [O61735-2]
EnsemblMetazoa; FBtr0100132; FBpp0099478; FBgn0023076. [O61735-1]
EnsemblMetazoa; FBtr0100134; FBpp0099480; FBgn0023076. [O61735-3]
EnsemblMetazoa; FBtr0334647; FBpp0306709; FBgn0023076.
GeneID; 38872; -.
KEGG; dme:Dmel_CG7391; -.
UCSC; CG7391-RA; d. melanogaster. [O61735-1]
CTD; 38872; -.
FlyBase; FBgn0023076; Clk.
eggNOG; KOG3561; Eukaryota.
eggNOG; ENOG410Y7Z8; LUCA.
GeneTree; ENSGT00760000118788; -.
InParanoid; O61735; -.
KO; K02223; -.
OMA; SYMQMAT; -.
OrthoDB; EOG091G11CV; -.
PhylomeDB; O61735; -.
Reactome; R-DME-432395; Degradation of TIM.
Reactome; R-DME-432408; Transcription regulation of cwo gene.
Reactome; R-DME-432501; Transcription repression by PER and activation by PDP1.
Reactome; R-DME-432524; Degradation of PER.
Reactome; R-DME-432560; Transcription activation by CLK:CYC and repression by VRI.
Reactome; R-DME-432620; Dephosphorylation of PER.
Reactome; R-DME-538848; Degradation of CLK.
Reactome; R-DME-538909; Dephosphorylation of CLK.
GenomeRNAi; 38872; -.
PRO; PR:O61735; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0023076; -.
ExpressionAtlas; O61735; differential.
Genevisible; O61735; DM.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:FlyBase.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IDA:FlyBase.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0048148; P:behavioral response to cocaine; TAS:FlyBase.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:FlyBase.
GO; GO:0003053; P:circadian regulation of heart rate; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
GO; GO:0008062; P:eclosion rhythm; TAS:FlyBase.
GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:UniProtKB.
GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
GO; GO:0009266; P:response to temperature stimulus; IMP:FlyBase.
GO; GO:0007622; P:rhythmic behavior; TAS:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001067; Nuc_translocat.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
Pfam; PF00010; HLH; 1.
PRINTS; PR00785; NCTRNSLOCATR.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
Alternative splicing; Biological rhythms; Complete proteome;
DNA-binding; Nucleus; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 1027 Circadian locomoter output cycles protein
kaput.
/FTId=PRO_0000127162.
DOMAIN 15 65 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 88 160 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 255 321 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 780 1027 Implicated in the circadian rhythmicity.
COMPBIAS 552 575 Poly-Gln.
COMPBIAS 770 773 Poly-Gln.
COMPBIAS 798 840 Poly-Gln.
COMPBIAS 878 881 Poly-Asn.
COMPBIAS 889 899 Poly-Asn.
COMPBIAS 957 967 Poly-Gln.
SITE 20 20 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
SITE 24 24 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
SITE 28 28 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
VAR_SEQ 2 67 Missing (in isoform F). {ECO:0000305}.
/FTId=VSP_026493.
VAR_SEQ 13 16 Missing (in isoform A).
{ECO:0000303|PubMed:9616122,
ECO:0000303|PubMed:9630223}.
/FTId=VSP_010320.
VARIANT 802 809 Missing (in variant B).
CONFLICT 36 36 N -> D (in Ref. 2; AAC62234).
{ECO:0000305}.
CONFLICT 132 132 N -> K (in Ref. 1; AAC39101).
{ECO:0000305}.
CONFLICT 559 559 N -> S (in Ref. 3; AAD10630).
{ECO:0000305}.
CONFLICT 609 609 L -> I (in Ref. 1; AAC39101 and 3;
AAD10630). {ECO:0000305}.
CONFLICT 827 834 Missing (in Ref. 1; AAC39101).
{ECO:0000305}.
CONFLICT 916 916 C -> Y (in Ref. 1; AAC39101 and 3;
AAD10630). {ECO:0000305}.
SEQUENCE 1027 AA; 116142 MW; B4AAC80DBF6F954B CRC64;
MDDESDDKDD TKSFLCRKSR NLSEKKRRDQ FNSLVNDLSA LISTSSRKMD KSTVLKSTIA
FLKNHNEATD RSKVFEIQQD WKPAFLSNDE YTHLMLESLD GFMMVFSSMG SIFYASESIT
SQLGYLPQDL YNMTIYDLAY EMDHEALLNI FMNPTPVIEP RQTDISSSNQ ITFYTHLRRG
GMEKVDANAY ELVKFVGYFR NDTNTSTGSS SEVSNGSNGQ PAVLPRIFQQ NPNAEVDKKL
VFVGTGRVQN PQLIREMSII DPTSNEFTSK HSMEWKFLFL DHRAPPIIGY MPFEVLGTSG
YDYYHFDDLD SIVACHEELR QTGEGKSCYY RFLTKGQQWI WLQTDYYVSY HQFNSKPDYV
VCTHKVVSYA EVLKDSRKEG QKSGNSNSIT NNGSSKVIAS TGTSSKSASA TTTLRDFELS
SQNLDSTLLG NSLASLGTET AATSPAVDSS PMWSASAVQP SGSCQINPLK TSRPASSYGN
ISSTGISPKA KRKCYFYNNR GNDSDSTSMS TDSVTSRQSM MTHVSSQSQR QRSHHREHHR
ENHHNQSHHH MQQQQQHQNQ QQQHQQHQQL QQQLQHTVGT PKMVPLLPIA STQIMAGNAC
QFPQPAYPLA SPQLVAPTFL EPPQYLTAIP MQPVIAPFPV APVLSPLPVQ SQTDMLPDTV
VMTPTQSQLQ DQLQRKHDEL QKLILQQQNE LRIVSEQLLL SRYTYLQPMM SMGFAPGNMT
AAAVGNLGAS GQRGLNFTGS NAVQPQFNQY GFALNSEQML NQQDQQMMMQ QQQNLHTQHQ
HNLQQQHQSH SQLQQHTQQQ HQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQLQLQQQ
NDILLREDID DIDAFLNLSP LHSLGSQSTI NPFNSSSNNN NQSYNGGSNL NNGNQNNNNR
SSNPPQNNNE DSLLSCMQMA TESSPSINFH MGISDDGSET QSEDNKMMHT SGSNLVQQQQ
QQQQQQQILQ QHQQQSNSFF SSNPFLNSQN QNQNQLPNDL EILPYQMSQE QSQNLFNSPH
TAPGSSQ


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