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Circadian locomoter output cycles protein kaput (EC 2.3.1.48)

 CLOCK_PONAB             Reviewed;         846 AA.
Q5RAK8;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
20-JUN-2018, entry version 97.
RecName: Full=Circadian locomoter output cycles protein kaput;
EC=2.3.1.48;
Name=CLOCK;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Transcriptional activator which forms a core component
of the circadian clock. The circadian clock, an internal time-
keeping system, regulates various physiological processes through
the generation of approximately 24 hour circadian rhythms in gene
expression, which are translated into rhythms in metabolism and
behavior. It is derived from the Latin roots 'circa' (about) and
'diem' (day) and acts as an important regulator of a wide array of
physiological functions including metabolism, sleep, body
temperature, blood pressure, endocrine, immune, cardiovascular,
and renal function. Consists of two major components: the central
clock, residing in the suprachiasmatic nucleus (SCN) of the brain,
and the peripheral clocks that are present in nearly every tissue
and organ system. Both the central and peripheral clocks can be
reset by environmental cues, also known as Zeitgebers (German for
'timegivers'). The predominant Zeitgeber for the central clock is
light, which is sensed by retina and signals directly to the SCN.
The central clock entrains the peripheral clocks through neuronal
and hormonal signals, body temperature and feeding-related cues,
aligning all clocks with the external light/dark cycle. Circadian
rhythms allow an organism to achieve temporal homeostasis with its
environment at the molecular level by regulating gene expression
to create a peak of protein expression once every 24 hours to
control when a particular physiological process is most active
with respect to the solar day. Transcription and translation of
core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2,
PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm
generation, whereas delays imposed by post-translational
modifications (PTMs) are important for determining the period
(tau) of the rhythms (tau refers to the period of a rhythm and is
the length, in time, of one complete cycle). A diurnal rhythm is
synchronized with the day/night cycle, while the ultradian and
infradian rhythms have a period shorter and longer than 24 hours,
respectively. Disruptions in the circadian rhythms contribute to
the pathology of cardiovascular diseases, cancer, metabolic
syndromes and aging. A transcription/translation feedback loop
(TTFL) forms the core of the molecular circadian clock mechanism.
Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or
ARNTL2/BMAL2, form the positive limb of the feedback loop, act in
the form of a heterodimer and activate the transcription of core
clock genes and clock-controlled genes (involved in key metabolic
processes), harboring E-box elements (5'-CACGTG-3') within their
promoters. The core clock genes: PER1/2/3 and CRY1/2 which are
transcriptional repressors form the negative limb of the feedback
loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2
heterodimer inhibiting its activity and thereby negatively
regulating their own expression. This heterodimer also activates
nuclear receptors NR1D1/2 and RORA/B/G, which form a second
feedback loop and which activate and repress ARNTL/BMAL1
transcription, respectively. Regulates the circadian expression of
ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of
the transactivation potential of NF-kappaB. Plays an important
role in the homeostatic regulation of sleep. The CLOCK-ARNTL/BMAL1
heterodimer regulates the circadian expression of SERPINE1/PAI1,
VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1,
GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also
genes implicated in glucose and lipid metabolism. Promotes
rhythmic chromatin opening, regulating the DNA accessibility of
other transcription factors. The CLOCK-ARNTL2/BMAL2 heterodimer
activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The
preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is
5'-CACGTGA-3', which contains a flanking Ala residue in addition
to the canonical 6-nucleotide E-box sequence. CLOCK specifically
binds to the half-site 5'-CAC-3', while ARNTL binds to the half-
site 5'-GTGA-3'. The CLOCK-ARNTL/BMAL1 heterodimer also recognizes
the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'.
CLOCK has an intrinsic acetyltransferase activity, which enables
circadian chromatin remodeling by acetylating histones and
nonhistone proteins, including its own partner ARNTL/BMAL1.
Represses glucocorticoid receptor NR3C1/GR-induced transcriptional
activity by reducing the association of NR3C1/GR to glucocorticoid
response elements (GREs) via the acetylation of multiple lysine
residues located in its hinge region. The acetyltransferase
activity of CLOCK is as important as its transcription activity in
circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9
in a circadian manner. Facilitated by BMAL1, rhythmically
interacts and acetylates argininosuccinate synthase 1 (ASS1)
leading to enzymatic inhibition of ASS1 as well as the circadian
oscillation of arginine biosynthesis and subsequent ureagenesis.
{ECO:0000250|UniProtKB:O08785, ECO:0000250|UniProtKB:O15516}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBUNIT: Component of the circadian clock oscillator which
includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or
ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins.
Forms a heterodimer with ARNTL/BMAL1. The CLOCK-ARNTL/BMAL1
heterodimer is required for E-box-dependent transactivation, for
CLOCK nuclear translocation and degradation, and for
phosphorylation of both CLOCK and ARNTL/BMAL1. Interacts with
NR3C1 in a ligand-dependent fashion. Interacts with ESR1 and
estrogen stimulates this interaction. Interacts with the complex
p35/CDK5. Interacts with RELA/p65. Interacts with KAT2B, CREBBP
and EP300. Interacts with ID1 and ID3. Interacts with ID2.
Interacts with MTA1. Interacts with MGEA5. Interacts with SIRT1.
Interacts with CIPC. Interacts with EZH2. Interacts with EIF4E,
PIWIL1 and DDX4. Interacts with PER1, PER2, CRY1 and CRY2 and this
interaction requires a translocation to the nucleus. Interaction
of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits
transcription activation. Interaction of the CLOCK-ARNTL/BMAL1
with CRY1 is independent of DNA but with PER2 is off DNA. The
CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B. Interacts with
KDM5A. Interacts with KMT2A; in a circadian manner. Interacts with
MYBBP1A. Interacts with THRAP3. Interacts with MED1; this
interaction requires the presence of THRAP3. Interacts with NCOA2.
The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1. Interacts
with ASS1 and IMPDH2; in a circadian manner. Interacts with
NDUFA9. {ECO:0000250|UniProtKB:O08785,
ECO:0000250|UniProtKB:O15516}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O08785}.
Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O15516}. Note=Localizes to sites of DNA
damage in a H2AX-independent manner. Shuffling between the
cytoplasm and the nucleus is under circadian regulation and is
ARNTL/BMAL1-dependent. Phosphorylated form located in the nucleus
while the nonphosphorylated form found only in the cytoplasm.
Sequestered to the cytoplasm in the presence of ID2.
{ECO:0000250|UniProtKB:O08785}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250|UniProtKB:O08785}.
-!- PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT
prevents protein degradation by inhibiting ubiquitination. It also
stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing
CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2/3
and CRY1/2. {ECO:0000250|UniProtKB:O08785}.
-!- PTM: Phosphorylation is dependent on the CLOCK-ARNTL/BMAL1
heterodimer formation. Phosphorylation enhances the
transcriptional activity, alters the subcellular localization and
decreases the stability of the heterodimer by promoting its
degradation. Phosphorylation shows circadian variations in the
liver. May be phosphorylated by CSNK1D and CKSN1E (By similarity).
{ECO:0000250|UniProtKB:O08785}.
-!- PTM: Sumoylation enhances its transcriptional activity and
interaction with ESR1, resulting in up-regulation of ESR1
activity. Estrogen stimulates sumoylation. Desumoylation by SENP1
negatively regulates its transcriptional activity.
{ECO:0000250|UniProtKB:O08785}.
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EMBL; CR859007; CAH91202.1; -; mRNA.
RefSeq; NP_001125706.1; NM_001132234.1.
UniGene; Pab.7567; -.
ProteinModelPortal; Q5RAK8; -.
SMR; Q5RAK8; -.
STRING; 9601.ENSPPYP00000016487; -.
GeneID; 100172630; -.
KEGG; pon:100172630; -.
CTD; 9575; -.
eggNOG; ENOG410IQ5V; Eukaryota.
eggNOG; ENOG410Y7Z8; LUCA.
HOVERGEN; HBG050997; -.
InParanoid; Q5RAK8; -.
KO; K02223; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
GO; GO:0042634; P:regulation of hair cycle; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:2000074; P:regulation of type B pancreatic cell development; ISS:UniProtKB.
GO; GO:0051775; P:response to redox state; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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.
InterPro; IPR013767; PAS_fold.
Pfam; PF00010; HLH; 1.
Pfam; PF00989; PAS; 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; 2.
2: Evidence at transcript level;
Activator; Biological rhythms; Complete proteome; Cytoplasm;
DNA damage; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation.
CHAIN 1 846 Circadian locomoter output cycles protein
kaput.
/FTId=PRO_0000262637.
DOMAIN 34 84 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 107 177 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 262 332 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 336 379 PAC.
REGION 371 845 Interaction with NR3C1.
{ECO:0000250|UniProtKB:O08785}.
REGION 450 570 Interaction with SIRT1.
{ECO:0000250|UniProtKB:O08785}.
REGION 514 564 Implicated in the circadian rhythmicity.
{ECO:0000250}.
MOTIF 32 47 Nuclear localization signal.
{ECO:0000250|UniProtKB:O08785}.
COMPBIAS 483 828 Gln-rich.
SITE 39 39 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
SITE 43 43 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
SITE 47 47 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O15516}.
SITE 84 84 Important for interaction with
ARNTL/BMAL1.
{ECO:0000250|UniProtKB:O15516}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:O08785}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:O08785}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:O08785}.
MOD_RES 427 427 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:O08785}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000250|UniProtKB:O08785}.
MOD_RES 451 451 Phosphothreonine; by CDK5.
{ECO:0000250|UniProtKB:O15516}.
MOD_RES 461 461 Phosphothreonine; by CDK5.
{ECO:0000250|UniProtKB:O15516}.
CROSSLNK 67 67 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:O08785}.
CROSSLNK 67 67 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O08785}.
CROSSLNK 842 842 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:O08785}.
SEQUENCE 846 AA; 95354 MW; F7119E879F2C41E2 CRC64;
MLFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF NVLIKELGSM
LPGNARKMDK STVLQKSIDF LRKHKEITAQ SDASEIRQDW KPTFLSNEEF TQLMLEALDG
FFLAIMTDGS IIYVSESVTS LLEHLPSDLV DQSIFNFIPE GEHSEVYKIL STHLLESDSL
TPEYLKSKNQ LEFCCHMLRG TIDPKEPSTY EYVKFIGNFK SLNSVSSSAH NGFEGTIQRT
HRPSYEDRVC FVATVRLATP QFIKEMCTVE EPNEEFASRH SLEWKFLFLD HRAPPIIGYL
PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW LQTHYYITYH
QWNSRPEFIV CTHTVVSYAE VRAERRRELS IEESLPEIAA DKSQDSGSDN RINTVSLKEA
LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMVQRRSSF
SSQSINSQSV GSSLTQPVMS QATNLPIPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN
IHRQQEELRK IQEQLQMVHG QGLQMFLQQP NPGLNFGSVQ LSSGNSSNIQ QLAPINMQGQ
VVPTNQIQSG MNTGHIGTTQ HMIQQQTLQS TSTQSQQNVL SGHSQQTSLP SQTQSTLTAP
LYNTMVISQP AAGSMVQIPS SMPQNSTQSA AVTTFTQDRQ IRFSQGQQLV TKLVTAPVAC
GAVMVPSTML MGQVVTAYPT FATQQQQSQT LSVTQQRQQQ SSQEQQLTSV QQPSQAQLTQ
PPQQFLQTSR LLHGNPSTQL ILSAAFPLQQ STFPQSHHQQ HQSQQQQQLS RHRTDSLPDP
SKVQPQ


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