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PER3_RAT
ID   PER3_RAT                Reviewed;        1119 AA.
AC   Q8CJE2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Period circadian protein homolog 3;
DE            Short=rPER3;
DE   AltName: Full=Circadian clock protein PERIOD 3;
GN   Name=Per3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Suzuki S., Oishi K., Sakamoto K., Ishida N.;
RT   "Cloning and circadian expression of rat period3 gene.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Originally described as a core component of the circadian
CC       clock. The circadian clock, an internal time-keeping system, regulates
CC       various physiological processes through the generation of approximately
CC       24 hour circadian rhythms in gene expression, which are translated into
CC       rhythms in metabolism and behavior. It is derived from the Latin roots
CC       'circa' (about) and 'diem' (day) and acts as an important regulator of
CC       a wide array of physiological functions including metabolism, sleep,
CC       body temperature, blood pressure, endocrine, immune, cardiovascular,
CC       and renal function. Consists of two major components: the central
CC       clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and
CC       the peripheral clocks that are present in nearly every tissue and organ
CC       system. Both the central and peripheral clocks can be reset by
CC       environmental cues, also known as Zeitgebers (German for 'timegivers').
CC       The predominant Zeitgeber for the central clock is light, which is
CC       sensed by retina and signals directly to the SCN. The central clock
CC       entrains the peripheral clocks through neuronal and hormonal signals,
CC       body temperature and feeding-related cues, aligning all clocks with the
CC       external light/dark cycle. Circadian rhythms allow an organism to
CC       achieve temporal homeostasis with its environment at the molecular
CC       level by regulating gene expression to create a peak of protein
CC       expression once every 24 hours to control when a particular
CC       physiological process is most active with respect to the solar day.
CC       Transcription and translation of core clock components (CLOCK, NPAS2,
CC       ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a
CC       critical role in rhythm generation, whereas delays imposed by post-
CC       translational modifications (PTMs) are important for determining the
CC       period (tau) of the rhythms (tau refers to the period of a rhythm and
CC       is the length, in time, of one complete cycle). A diurnal rhythm is
CC       synchronized with the day/night cycle, while the ultradian and
CC       infradian rhythms have a period shorter and longer than 24 hours,
CC       respectively. Disruptions in the circadian rhythms contribute to the
CC       pathology of cardiovascular diseases, cancer, metabolic syndromes and
CC       aging. A transcription/translation feedback loop (TTFL) forms the core
CC       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, NR1D2, RORA, RORB and RORG, which form a second feedback loop
CC       and which activate and repress ARNTL/BMAL1 transcription, respectively.
CC       Has a redundant role with the other PER proteins PER1 and PER2 and is
CC       not essential for the circadian rhythms maintenance. In contrast, plays
CC       an important role in sleep-wake timing and sleep homeostasis probably
CC       through the transcriptional regulation of sleep homeostasis-related
CC       genes, without influencing circadian parameters. Can bind heme.
CC       {ECO:0000250|UniProtKB:O70361, ECO:0000250|UniProtKB:P56645}.
CC   -!- SUBUNIT: Homodimer. Component of the circadian core oscillator, which
CC       includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2,
CC       CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly
CC       with PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and
CC       CRY2 is weak and not rhythmic. Interacts with FBXW11 and BTRC.
CC       {ECO:0000250|UniProtKB:O70361, ECO:0000250|UniProtKB:P56645}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O70361}. Nucleus
CC       {ECO:0000250|UniProtKB:O70361}. Note=Mainly cytoplasmic. Translocates
CC       to the nucleus through binding PER1, PER2, CRY1 or CRY2, but not
CC       TIMELESS. {ECO:0000250|UniProtKB:O70361}.
CC   -!- PTM: Phosphorylation by CSNK1E is weak and appears to require
CC       association with PER1 and translocation to the nucleus.
CC       {ECO:0000250|UniProtKB:O70361}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O70361}.
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DR   EMBL; AB092512; BAC16806.1; -; mRNA.
DR   RefSeq; NP_076468.2; NM_023978.2.
DR   AlphaFoldDB; Q8CJE2; -.
DR   SMR; Q8CJE2; -.
DR   STRING; 10116.ENSRNOP00000024932; -.
DR   PaxDb; Q8CJE2; -.
DR   PRIDE; Q8CJE2; -.
DR   GeneID; 78962; -.
DR   KEGG; rno:78962; -.
DR   UCSC; RGD:621581; rat.
DR   CTD; 8863; -.
DR   RGD; 621581; Per3.
DR   eggNOG; KOG3753; Eukaryota.
DR   InParanoid; Q8CJE2; -.
DR   OrthoDB; 331262at2759; -.
DR   PhylomeDB; Q8CJE2; -.
DR   PRO; PR:Q8CJE2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; ISO:RGD.
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:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; ISO:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
DR   CDD; cd00130; PAS; 1.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR015524; Per_circ_prot_3.
DR   InterPro; IPR022728; Period_circadian-like_C.
DR   PANTHER; PTHR11269:SF13; PTHR11269:SF13; 1.
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; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..1119
FT                   /note="Period circadian protein homolog 3"
FT                   /id="PRO_0000261155"
FT   DOMAIN          120..187
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          259..325
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          334..377
FT                   /note="PAC"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..750
FT                   /note="CSNK1E binding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          718..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1037..1119
FT                   /note="CRY binding domain"
FT                   /evidence="ECO:0000250"
FT   MOTIF           54..63
FT                   /note="Nuclear export signal 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           400..409
FT                   /note="Nuclear export signal 3"
FT                   /evidence="ECO:0000250"
FT   MOTIF           720..739
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           913..920
FT                   /note="Nuclear export signal 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         907
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P56645"
SQ   SEQUENCE   1119 AA;  122686 MW;  38FD286377CD234E CRC64;
     MDPCGNPAVP GGDCPQTRGP GLQGSSGQEG PLQGICVDSS HSEHEDRNRM SEELIMVVQE
     MKKYFPAERH TKPSTLDALN YALRCVHSVQ ANSEFFQSLS PRGARQAEAT VYNLEELTSL
     ASEHTSKNTD TFVAVFSFLS GRLVHISEQA AWILNSKKGF LKSLHFVDLL APRDVRVFYA
     HTAPTQLPFW NTWTQRASQY ECAPVKPFFC RICGGGDREQ KRHYSPFRIL PYLVHVHSPA
     QPEPEPCCLT LVEKIHSGYE APRIPVDKRV FTTTHTPGCV FLEVDERAVP LLGFLPQDLI
     GTSILTYLHP EDRPLMVAVH QKVLKYVGHP PFEHSPIRFC TQNGDYVILD SSWSSFVNPW
     SRKVSFIIGR HKVRTSPLNE DVFATRIKKA TSHDEDITEL QEQIHRLLLQ PVHASASSGY
     GSLGSSGSQE QHISVTSSSE SSGHCVEEAQ QEQMTLQQVY ASVNKIKNVG QQLYIESMAR
     SSVKPVMETC TEPQGSDEQK DFSSSQTLKN KSTDTGSGGD LRPEQHSSSY QQMNCIDSVI
     RYLTSYSFPA LKRKCISCTN TSSSSEEAKP NPEADGSLRD TEQLLDIPEQ ETTTPSADAE
     GGVARTLSTA ALSMASGVSQ CSCSSTTDHV PPLQSESVAG ACEPWALRTK AHVTAEGFKP
     VGLTAAVLSA HTQKEEQNYV DRFREKILTS PYGCYLQQEG RNHAKYACVV GAGATPKHSR
     CAGSERRKHK RKKLPTPVDS SSSSAHLCPH VRGLLPDVQH WSASVTSPCA TGLALPSALV
     VPNQTPYLLS SFPLQDMAPH GVGDSAPWGA AAECPPLSAG PHPVSTFPSA YMGTFMTVLL
     HNSPLFPLWP ASFSPYPFLG ATGPSQMAPL VPAMAPDLEP TPSDHGPRRV EENWETHSEE
     EHPFISSRSS SPLQLNLLQE EMPAPSEYAD ALRRGACPDA KQLCVTGNSG SRSPPCATGE
     LATASVQQES PSAAASGSSA SSVHGSGSDY TSEVSENGQR SQDTHRDRAF SGAAEESIWR
     MIERTPQCVL MTYQVPERGR DTVLREDLEK LHSMERQRPQ FSSAQKEELA KVRSWIHSHP
     APEERQLQRA MSPVKTEVQL VTLQRPVNSV QQKTPVEQL
 
 
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