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Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Brain and muscle ARNT-like 1)

 BMAL1_HORSE             Reviewed;         626 AA.
A0MLS5;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
12-SEP-2018, entry version 81.
RecName: Full=Aryl hydrocarbon receptor nuclear translocator-like protein 1;
AltName: Full=Brain and muscle ARNT-like 1;
Name=ARNTL; Synonyms=BMAL1;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16479406; DOI=10.1007/s00359-006-0108-7;
Murphy B.A., Vick M.M., Sessions D.R., Cook R.F., Fitzgerald B.P.;
"Evidence of an oscillating peripheral clock in an equine fibroblast
cell line and adipose tissue but not in peripheral blood.";
J. Comp. Physiol. A 192:743-751(2006).
-!- 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, NR1D2, RORA, RORB and RORG, which form a
second feedback loop and which activate and repress ARNTL/BMAL1
transcription, respectively. ARNTL/BMAL1 positively regulates
myogenesis and negatively regulates adipogenesis via the
transcriptional control of the genes of the canonical Wnt
signaling pathway. Plays a role in normal pancreatic beta-cell
function; regulates glucose-stimulated insulin secretion via the
regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2,
PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling
pathway; regulates the expression of MTOR and DEPTOR. Controls
diurnal oscillations of Ly6C inflammatory monocytes; rhythmic
recruitment of the PRC2 complex imparts diurnal variation to
chemokine expression that is necessary to sustain Ly6C monocyte
rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1,
CYP19A1 and LHCGR in the ovary and also the genes involved in hair
growth. Plays an important role in adult hippocampal neurogenesis
by regulating the timely entry of neural stem/progenitor cells
(NSPCs) into the cell cycle and the number of cell divisions that
take place prior to cell-cycle exit. Regulates the circadian
expression of CIART. 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 and also genes implicated in
glucose and lipid metabolism. Promotes rhythmic chromatin opening,
regulating the DNA accessibility of other transcription factors.
The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the
expression of MAOA, F7 and LDHA and modulates the circadian rhythm
of daytime contrast sensitivity by regulating the rhythmic
expression of adenylate cyclase type 1 (ADCY1) in the retina. 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'.
Essential for the rhythmic interaction of CLOCK with ASS1 and
plays a critical role in positively regulating CLOCK-mediated
acetylation of ASS1. {ECO:0000250|UniProtKB:O00327,
ECO:0000250|UniProtKB:Q9WTL8}.
-!- SUBUNIT: Component of the circadian clock oscillator which
includes the CRY1/2 proteins, CLOCK or NPAS2, ARNTL/BMAL1 or
ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER1/2/3
proteins. Efficient DNA binding requires dimerization with another
bHLH protein. 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. Part of a
nuclear complex which also includes RACK1 and PRKCA; RACK1 and
PRKCA are recruited to the complex in a circadian manner.
Interacts with NPAS2, HSP90, AHR, CIART, DDX4, SUMO3, OGT, EED,
EZH2, SUZ12, KAT2B, EP300, BHLHE40/DEC1, BHLHE41/DEC2, ID1, ID2,
ID3, MTA1 and SIRT1. Interacts with RELB and the interaction is
enhanced in the presence of CLOCK. 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 UBE3A and PRKCG. Interacts with MAGEL2. Interacts
with NCOA2. Interacts with THRAP3. The CLOCK-ARNTL/BMAL1
heterodimer interacts with PASD1. Interacts with PASD1.
{ECO:0000250|UniProtKB:O00327, ECO:0000250|UniProtKB:Q9WTL8}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981}. Cytoplasm {ECO:0000250}. Nucleus, PML body
{ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm
and this nucleocytoplasmic shuttling is essential for the nuclear
accumulation of CLOCK, target gene transcription and the
degradation of the CLOCK-ARNTL/BMAL1 heterodimer. The sumoylated
form localizes in the PML body (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250}.
-!- 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 transcription of genes in the negative
loop of the circadian clock such as PER1/2/3 and CRY1/2 (By
similarity). {ECO:0000250}.
-!- PTM: Acetylated on Lys-538 upon dimerization with CLOCK.
Acetylation facilitates CRY1-mediated repression (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated upon dimerization with CLOCK. Phosphorylation
enhances the transcriptional activity, alters the subcellular
localization and decreases the stability of the CLOCK-ARNTL/BMAL1
heterodimer by promoting its degradation. Phosphorylation shows
circadian variations in the liver with a peak between CT10 to
CT14. Phosphorylation at Ser-90 by CK2 is essential for its
nuclear localization, its interaction with CLOCK and controls
CLOCK nuclear entry. Dephosphorylation at Ser-78 is important for
dimerization with CLOCK and transcriptional activity.
{ECO:0000250|UniProtKB:O00327, ECO:0000250|UniProtKB:Q9WTL8}.
-!- PTM: Sumoylated on Lys-259 upon dimerization with CLOCK.
Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the
level of these conjugates undergo rhythmic variation, peaking at
CT9-CT12. Sumoylation localizes it exclusively to the PML body and
promotes its ubiquitination in the PML body, ubiquitin-dependent
proteasomal degradation and the transcriptional activity of the
CLOCK-ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; DQ988038; ABJ90473.1; -; mRNA.
RefSeq; NP_001075390.1; NM_001081921.2.
RefSeq; XP_014596969.1; XM_014741483.1.
UniGene; Eca.20470; -.
UniGene; Eca.2805; -.
ProteinModelPortal; A0MLS5; -.
SMR; A0MLS5; -.
STRING; 9796.ENSECAP00000010490; -.
PaxDb; A0MLS5; -.
PRIDE; A0MLS5; -.
GeneID; 100034115; -.
KEGG; ecb:100034115; -.
CTD; 406; -.
eggNOG; KOG3561; Eukaryota.
eggNOG; ENOG410XRJI; LUCA.
HOGENOM; HOG000234379; -.
HOVERGEN; HBG107503; -.
InParanoid; A0MLS5; -.
KO; K02296; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0070888; F:E-box binding; 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:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0090403; P:oxidative stress-induced premature senescence; ISS:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:1901985; P:positive regulation of protein acetylation; ISS:UniProtKB.
GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; 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:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
GO; GO:0042634; P:regulation of hair cycle; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; 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: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; 3.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
2: Evidence at transcript level;
Acetylation; Activator; Biological rhythms; Complete proteome;
Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 626 Aryl hydrocarbon receptor nuclear
translocator-like protein 1.
/FTId=PRO_0000278842.
DOMAIN 72 125 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 143 215 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 326 396 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 401 444 PAC.
REGION 508 588 Interaction with CIART. {ECO:0000250}.
MOTIF 36 41 Nuclear localization signal.
{ECO:0000250}.
MOTIF 142 152 Nuclear export signal 1. {ECO:0000250}.
MOTIF 361 369 Nuclear export signal 2. {ECO:0000250}.
SITE 77 77 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O00327}.
SITE 80 80 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O00327}.
SITE 81 81 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O00327}.
SITE 85 85 Interaction with E-box DNA.
{ECO:0000250|UniProtKB:O00327}.
SITE 125 125 Important for interaction with CLOCK.
{ECO:0000250|UniProtKB:O00327}.
MOD_RES 17 17 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 21 21 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:O00327}.
MOD_RES 90 90 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 538 538 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WTL8}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2 and
SUMO3). {ECO:0000250}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O00327}.
SEQUENCE 626 AA; 68758 MW; 51B28896154F4DEB CRC64;
MADQRMDISS TISDFMSPGA TDLLSSPLGT SGMDCNRKRK GSSTDYQESM DTDKDDPHGR
LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ
HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL
NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC
SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE
DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI
LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW
FSFMNPWTKE VEYIVSTNTV VLANVLEGGD PTFPQLTASP HSMDSMLPSG EGGPKRTHPT
VPGIPGGTRA GAGKIGRMIA EEVMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI
LNGGTPDIPS SGLPPGQAQE NPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM
AVIMSLLEAD AGLGGPVDFS DLPWPL


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