BMAL2_CHICK
ID BMAL2_CHICK Reviewed; 622 AA.
AC Q8QGQ7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator-like protein 2;
DE AltName: Full=Brain and muscle ARNT-like 2;
DE Short=cBMAL2;
GN Name=ARNTL2; Synonyms=BMAL2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH CLOCK AND
RP ARNTL, AND INDUCTION.
RC TISSUE=Pineal gland;
RX PubMed=11554928; DOI=10.1046/j.1365-2443.2001.00462.x;
RA Okano T., Yamamoto K., Okano K., Hirota T., Kasahara T., Sasaki M.,
RA Takanaka Y., Fukada Y.;
RT "Chicken pineal clock genes: implication of BMAL2 as a bidirectional
RT regulator in circadian clock oscillation.";
RL Genes Cells 6:825-836(2001).
CC -!- FUNCTION: Transcriptional activator which forms a core component of the
CC circadian clock. The circadian clock, an internal time-keeping system,
CC regulates various physiological processes through the generation of
CC approximately 24 hour circadian rhythms in gene expression, which are
CC translated into rhythms in metabolism and behavior. It is derived from
CC the Latin roots 'circa' (about) and 'diem' (day) and acts as an
CC important regulator of a wide array of physiological functions
CC including metabolism, sleep, body temperature, blood pressure,
CC endocrine, immune, cardiovascular, and renal function. Consists of two
CC major components: the central clock, residing in the suprachiasmatic
CC nucleus (SCN) of the brain, and the peripheral clocks that are present
CC in nearly every tissue and organ system. Both the central and
CC peripheral clocks can be reset by environmental cues, also known as
CC Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the
CC central clock is light, which is sensed by retina and signals directly
CC to the SCN. The central clock entrains the peripheral clocks through
CC neuronal and hormonal signals, body temperature and feeding-related
CC cues, aligning all clocks with the external light/dark cycle. Circadian
CC rhythms allow an organism to achieve temporal homeostasis with its
CC environment at the molecular level by regulating gene expression to
CC create a peak of protein expression once every 24 hours to control when
CC a particular physiological process is most active with respect to the
CC solar day. Transcription and translation of core clock components
CC (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and
CC CRY2) plays a critical role in rhythm generation, whereas delays
CC imposed by post-translational modifications (PTMs) are important for
CC determining the period (tau) of the rhythms (tau refers to the period
CC of a rhythm and is the length, in time, of one complete cycle). A
CC diurnal rhythm is synchronized with the day/night cycle, while the
CC ultradian and infradian rhythms have a period shorter and longer than
CC 24 hours, respectively. Disruptions in the circadian rhythms contribute
CC to the pathology of cardiovascular diseases, cancer, metabolic
CC syndromes and aging. A transcription/translation feedback loop (TTFL)
CC forms the core of the molecular circadian clock mechanism.
CC Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2,
CC form the positive limb of the feedback loop, act in the form of a
CC heterodimer and activate the transcription of core clock genes and
CC clock-controlled genes (involved in key metabolic processes), harboring
CC E-box elements (5'-CACGTG-3') within their promoters. The core clock
CC genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form
CC the negative limb of the feedback loop and interact with the
CC CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its
CC activity and thereby negatively regulating their own expression. This
CC heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G,
CC which form a second feedback loop and which activate and repress
CC ARNTL/BMAL1 transcription, respectively. The preferred binding motif
CC for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains
CC a flanking Ala residue in addition to the canonical 6-nucleotide E-box
CC sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while
CC ARNTL binds to the half-site 5'-GTGA-3'. {ECO:0000250|UniProtKB:O00327,
CC ECO:0000250|UniProtKB:Q2VPD4, ECO:0000250|UniProtKB:Q8WYA1}.
CC -!- SUBUNIT: Component of the circadian core oscillator, which includes the
CC CRY proteins, CLOCK, or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D
CC and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with
CC CLOCK to form the ARNTL2/BMAL2-CLOCK transactivator. Can form
CC heterodimers or homodimers which interact directly with CLOCK to form
CC the transcription activator. {ECO:0000269|PubMed:11554928}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expressed in the pineal gland.
CC {ECO:0000269|PubMed:11554928}.
CC -!- INDUCTION: Expression in the pineal gland exhibits circadian rhythm.
CC Maximum levels expressed at CT14, and between ZT14 and ZT18.
CC {ECO:0000269|PubMed:11554928}.
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DR EMBL; AF246958; AAL98707.1; -; mRNA.
DR RefSeq; NP_989464.1; NM_204133.1.
DR AlphaFoldDB; Q8QGQ7; -.
DR SMR; Q8QGQ7; -.
DR STRING; 9031.ENSGALP00000022780; -.
DR PaxDb; Q8QGQ7; -.
DR PRIDE; Q8QGQ7; -.
DR GeneID; 373925; -.
DR KEGG; gga:373925; -.
DR CTD; 56938; -.
DR VEuPathDB; HostDB:geneid_373925; -.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; Q8QGQ7; -.
DR OrthoDB; 331262at2759; -.
DR PhylomeDB; Q8QGQ7; -.
DR PRO; PR:Q8QGQ7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..622
FT /note="Aryl hydrocarbon receptor nuclear translocator-like
FT protein 2"
FT /id="PRO_0000273633"
FT DOMAIN 92..145
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 163..235
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 342..412
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 417..460
FT /note="PAC"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 97
FT /note="Interaction with E-box DNA"
FT /evidence="ECO:0000250|UniProtKB:O00327"
FT SITE 101
FT /note="Interaction with E-box DNA"
FT /evidence="ECO:0000250|UniProtKB:O00327"
FT SITE 105
FT /note="Interaction with E-box DNA"
FT /evidence="ECO:0000250|UniProtKB:O00327"
FT SITE 145
FT /note="Important for interaction with CLOCK"
FT /evidence="ECO:0000250|UniProtKB:O00327"
SQ SEQUENCE 622 AA; 69132 MW; 25CF08318CECD6C1 CRC64;
MAEAGVGSAE GAEEERRAVE ENFPVDGNSC IASGVPSLMN PITKPATTSF NNSVVEIPRK
RKGSDSDNQD TVEVDGDPQK RNEDEEHLKI KDFREAHSQT EKRRRDKMNN LIEELSAMIP
QCNPMARKLD KLTVLRMAVQ HLKSLKGSTS SYTEVRYKPS FLKDDELRQL ILRAADGFLF
VVGCNRGKIL FVSESVCKIL NYDQTSLIGQ SLFDYLHPKD VAKVKEQLSS SDVSPREKLV
DGKTGLQVHT DFQAGPARLN SGARRSFFCR IKCSRTTVKE EKECLPNPKK KDHRKYCTIH
CTGYMKNWPP SEVGVEEEND VEKNSSNFNC LVAIGRLHPY IVPQKSGEIK VKATEFVTRF
AMDGKFVYVD QRATAILGYL PQELLGTSCY EYCHQDDHNH LAEKHKEVLQ NKEKVFTNSY
KFRAKDGSFI TLKSQWFSFM NPWTKELEYI VSNNTVVLGH NESAEEQVSY GSQPAEGAVK
QSLVSVPGMS SGTVLGAGSI GTEIANEILE LQRLHSSPPG ELSPSHLLRK SPSPALTVNC
SNVPNKELIQ LCPSEAEVLE TSEQNQGAIP FPSNEPLLGG NSQLDFAICE NDDTAMTALM
NYLEADGGLG DPAELSDIQW AL
