PER2_CHICK
ID PER2_CHICK Reviewed; 1344 AA.
AC Q8QGQ8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Period circadian protein homolog 2;
DE Short=cPER2;
DE AltName: Full=Circadian clock protein PERIOD 2;
GN Name=PER2;
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], FUNCTION, 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 repressor 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 syndrome
CC and aging. A transcription/translation feedback loop (TTFL) forms the
CC core of the molecular circadian clock mechanism. Transcription factors,
CC CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb
CC of the feedback loop, act in the form of a heterodimer and activate the
CC transcription of core clock genes and clock-controlled genes (involved
CC in key metabolic processes), harboring E-box elements (5'-CACGTG-3')
CC within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which
CC are transcriptional repressors form the negative limb of the feedback
CC loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2
CC heterodimer inhibiting its activity and thereby negatively regulating
CC their own expression. This heterodimer also activates nuclear receptors
CC NR1D1/2 and RORA/B/G, which form a second feedback loop and which
CC activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and
CC PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate
CC circadian timing, but also contribute directly to repression of clock-
CC controlled target genes through interaction with several classes of
CC RNA-binding proteins, helicases and others transcriptional repressors.
CC PER appears to regulate circadian control of transcription by at least
CC three different modes. First, interacts directly with the CLOCK-
CC ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit
CC complexes containing the SIN3-HDAC that remodel chromatin to repress
CC transcription. Second, brings H3K9 methyltransferases such as SUV39H1
CC and SUV39H2 to the E-box elements of the circadian target genes, like
CC PER2 itself or PER1. The recruitment of each repressive modifier to the
CC DNA seems to be very precisely temporally orchestrated by the large PER
CC complex, the deacetylases acting before than the methyltransferases.
CC Additionally, large PER complexes are also recruited to the target
CC genes 3' termination site through interactions with RNA-binding
CC proteins and helicases that may play a role in transcription
CC termination to regulate transcription independently of CLOCK-
CC ARTNL/BMAL1 interactions (By similarity).
CC {ECO:0000250|UniProtKB:O54943, ECO:0000269|PubMed:11554928}.
CC -!- SUBUNIT: Component of the circadian clock oscillator which includes the
CC CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1E, and
CC the PER proteins. Interacts directly with PER3, and through a C-
CC terminal domain, with CRY1 and CRY2. {ECO:0000250|UniProtKB:O54943}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54943}. Cytoplasm
CC {ECO:0000250|UniProtKB:O54943}. Note=Mainly nuclear. Nucleocytoplasmic
CC shuttling is effected by interaction with other circadian core
CC oscillator proteins and/or by phosphorylation. Retention of PER1 in the
CC cytoplasm occurs through PER1-PER2 heterodimer formation or by
CC interaction with CSNK1E and/or phosphorylation which appears to mask
CC the PER1 nuclear localization signal. Also translocated to the nucleus
CC by CRY1 or CRY2 (By similarity). {ECO:0000250|UniProtKB:O54943}.
CC -!- INDUCTION: Exhibits circadian rhythm expression. Peak levels in early
CC morning and low levels at early night. {ECO:0000269|PubMed:11554928}.
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DR EMBL; AF246956; AAL98705.1; -; mRNA.
DR RefSeq; NP_989593.1; NM_204262.1.
DR AlphaFoldDB; Q8QGQ8; -.
DR SMR; Q8QGQ8; -.
DR STRING; 9031.ENSGALP00000008844; -.
DR PaxDb; Q8QGQ8; -.
DR PRIDE; Q8QGQ8; -.
DR GeneID; 374116; -.
DR KEGG; gga:374116; -.
DR CTD; 8864; -.
DR VEuPathDB; HostDB:geneid_374116; -.
DR eggNOG; KOG3753; Eukaryota.
DR InParanoid; Q8QGQ8; -.
DR PhylomeDB; Q8QGQ8; -.
DR PRO; PR:Q8QGQ8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR022728; Period_circadian-like_C.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12114; Period_C; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50112; PAS; 1.
PE 2: Evidence at transcript level;
KW Biological rhythms; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1344
FT /note="Period circadian protein homolog 2"
FT /id="PRO_0000261154"
FT DOMAIN 231..298
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 371..437
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 445..488
FT /note="PAC"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1344
FT /note="CRY binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q9Z301"
FT MOTIF 161..170
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250|UniProtKB:O54943"
FT MOTIF 358..362
FT /note="LXXLL"
FT MOTIF 512..521
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250|UniProtKB:O54943"
FT MOTIF 851..865
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O54943"
FT MOTIF 1138..1142
FT /note="LXXLL"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 147942 MW; A34EC8265066A2A0 CRC64;
MDCIEVRGFY SSTEEQNPEQ QADISENISS LFSLKEQQKM SEYSGLASNH SQMIAEDSEI
QPKPEHSPEV LQEDIEMSSG SSGNDFSGNE TNENYSSGHD SHGHESDENG KDSAMLMESS
DCHKSSSSNA FSLMIANSEH NQSSSGCSSE QSTKAKTQKE LLKTLQELKA HLPAEKRIKG
KSSVLTTLKY ALKSIKQVKA NEEYYQLLMI NESQPSGLNV SSYTVEEVET ITSEYIMKNA
DMFAVAVSLI TGKIVYISDQ AAAILRCKRS YFKNAKFVEL LAPQDVSVFY TSTTPYRLPS
WNICSRAESS TQDCMEEKSF FCRISAGKER ENEICYHPFR MTPYLIKVQD PEVAEDQLCC
VLLAEKVHSG YEAPRIPPDK RIFTTTHTPT CLFQDVDERA VPLLGYLPQD LIGTPVLVHL
HPNDRPLMLA IHKKILQYGG QPFDYSPIRF CTRNGDYITM DTSWSSFINP WSRKVSFIIG
RHKVRTGPLN EDVFAAPNYT EDRILHPSVQ EITEQIYRLL LQPVHNSGSS GYGSLGSNGS
HEHLMSVASS SDSTGNNNDD TQKDKTISQD ARKVKTKGQH IFTENKGKLE YKREPSAEKQ
NGPGGQVKDV IGKDTTATAA PKNVATEELA WKEQPVYSYQ QISCLDSVIR YLESCNVPGT
AKRKCEPSSS VNSSVHEQKA SVNAIQPLGD STVLKSSGKS SGPPVVGAHL TSLALPGKPE
SVVSLTSQCS YSSTIVHVGD KKPQPELEMI EDGPSGAEVL DTQLPAPPPS STHVNQEKES
FKKLGLTKEV LAVHTQKEEQ SFLNKFKEIK RFNIFQSHCN YYLQDKPKGR PGERGGRGQR
NGTSGMDQPW KKSGKNRKSK RIKPQESSDS TTSGTKFPHR FPLQGLNTTA WSPSDTSQAS
YSAMSFPTVM PAYPLPVFPA AAGTVPPAPE TSVSGFNQLP DSGNTCSMQP SQFSAPLMTP
VVALVLPNYV YPEMNNSLPQ TLYHSQANFP THPAFSSQTV FPAQPPFTTP SPFPQQAFFP
MQPFHYNPPA EIEKVPVTET RNEPSRSCTP QSVGPQDQAS PPLFQSRCSS PLNLLQLEEN
TKTVESGAPA GLHGALNEEG TIGKIMTTDA GSGKGSLPAE SPMDAQNSDA LSMSSVLLDI
LLQEDACSGT GSASSGSGVS AAAESLGSGS NGCDMSGSRT GSSETSHTSK YFGSIDSSEN
HHKTKMKAEI EESEHFIKYV LQDPIWLLMA NTDDTVMMTY QLPSRDLETV LKEDKLKLKQ
MQKLQPKFTE DQKRELIEVH PWIQQGGLPK TVANSECIFC EDNIQSNFYT SYDEEIHEMD
LNEMIEDSGE NNLVPLSQVN EEQT
