PER_DROSE
ID PER_DROSE Reviewed; 661 AA.
AC Q03354; Q26285;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Period circadian protein;
DE Flags: Fragments;
GN Name=per;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558.
RX PubMed=8436278; DOI=10.1093/genetics/133.2.375;
RA Kliman R.M., Hey J.;
RT "DNA sequence variation at the period locus within and among species of the
RT Drosophila melanogaster complex.";
RL Genetics 133:375-387(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 559-661.
RX PubMed=1487825; DOI=10.1007/bf00171819;
RA Peixoto A.A., Costa R., Wheeler D.A., Hall J.C., Kyriacou C.P.;
RT "Evolution of the threonine-glycine repeat region of the period gene in the
RT melanogaster species subgroup of Drosophila.";
RL J. Mol. Evol. 35:411-419(1992).
CC -!- FUNCTION: Essential for biological clock functions. Determines the
CC period length of circadian and ultradian rhythms; an increase in PER
CC dosage leads to shortened circadian rhythms and a decrease leads to
CC lengthened circadian rhythms. Essential for the circadian rhythmicity
CC of locomotor activity, eclosion behavior, and for the rhythmic
CC component of the male courtship song that originates in the thoracic
CC nervous system. The biological cycle depends on the rhythmic formation
CC and nuclear localization of the TIM-PER complex. Light induces the
CC degradation of TIM, which promotes elimination of PER. Nuclear activity
CC of the heterodimer coordinatively regulates PER and TIM transcription
CC through a negative feedback loop. Behaves as a negative element in
CC circadian transcriptional loop. Does not appear to bind DNA, suggesting
CC indirect transcriptional inhibition (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with timeless (TIM); the complex then
CC translocates into the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Note=Nuclear at specific periods of the day.
CC First accumulates in the perinuclear region about one hour before
CC translocation into the nucleus. Interaction with Tim is required for
CC nuclear localization (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The run of Gly-Thr is implicated in the maintenance of
CC circadian period at different temperatures. Deletion of the repeat
CC leads to a shortening of the courtship song cycle period, and thus
CC could be important for determining features of species-specific mating
CC behavior (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated with a circadian rhythmicity, probably by the
CC double-time protein (dbt). Phosphorylation could be implicated in the
CC stability of per monomer and in the formation of heterodimer per-tim
CC (By similarity). {ECO:0000250}.
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DR EMBL; L07820; AAA28774.1; -; Genomic_DNA.
DR EMBL; L07822; AAA28772.1; -; Genomic_DNA.
DR EMBL; L07824; AAA28770.1; -; Genomic_DNA.
DR EMBL; L07827; AAA28767.1; -; Genomic_DNA.
DR EMBL; S53297; AAB25028.2; -; Genomic_DNA.
DR PIR; S52944; S52944.
DR PIR; S52951; S52951.
DR AlphaFoldDB; Q03354; -.
DR SMR; Q03354; -.
DR EnsemblMetazoa; FBtr0202223; FBpp0200715; FBgn0012799.
DR GO; GO:0044297; C:cell body; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0060086; P:circadian temperature homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0007620; P:copulation; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0008062; P:eclosion rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IEA:EnsemblMetazoa.
DR GO; GO:0045475; P:locomotor rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0007616; P:long-term memory; IEA:EnsemblMetazoa.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:EnsemblMetazoa.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00989; PAS; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50112; PAS; 2.
PE 3: Inferred from homology;
KW Biological rhythms; Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT CHAIN <1..>661
FT /note="Period circadian protein"
FT /id="PRO_0000162608"
FT DOMAIN 223..358
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 376..482
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REPEAT 591..592
FT /note="1"
FT REPEAT 593..594
FT /note="2"
FT REPEAT 595..596
FT /note="3"
FT REPEAT 597..598
FT /note="4"
FT REPEAT 599..600
FT /note="5"
FT REPEAT 601..602
FT /note="6"
FT REPEAT 603..604
FT /note="7"
FT REPEAT 605..606
FT /note="8"
FT REPEAT 607..608
FT /note="9"
FT REPEAT 609..610
FT /note="10"
FT REPEAT 611..612
FT /note="11"
FT REPEAT 613..614
FT /note="12"
FT REPEAT 615..616
FT /note="13"
FT REPEAT 617..618
FT /note="14"
FT REPEAT 619..620
FT /note="15"
FT REPEAT 621..622
FT /note="16"
FT REPEAT 623..624
FT /note="17"
FT REPEAT 625..626
FT /note="18"
FT REPEAT 627..628
FT /note="19"
FT REPEAT 629..630
FT /note="20"
FT REPEAT 631..632
FT /note="21"
FT REPEAT 633..634
FT /note="22"
FT REPEAT 635..636
FT /note="23; approximate"
FT REPEAT 637..638
FT /note="24"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..638
FT /note="24 X 2 AA approximate tandem repeats of G-[TN]"
FT MOTIF 53..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 85
FT /note="L -> M (in clone SE-P4)"
FT NON_CONS 558..559
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 661
SQ SEQUENCE 661 AA; 69678 MW; C0680E5198B6A209 CRC64;
KVSDSAYSNS CSNSQSQRSG SSKSRLSGSH SSGSSGYGGK PSTQASSSDM IIKRNKDKSR
KKKKNKGAGQ GAGQAQTLIS ASTSLEGRDE EKPRPSGTGC VEQQICRELQ DQQHGEDHSE
PQAAEQLQQE EDQSGSESEA DRVEGVAKSE AVQSFPIPSP LSVTIVPPSM GGCGGVGHAA
GLDSGLAKFD KTWEAGPGKL ESMTGVGAAA AGTGQRGERV KEDSFCCVIS MHDGIVLYTT
PSITDVLGYP RDMWLGRSFI DFVHLKDRAT FASQITTGIP IAESRGSVPK DAKSTFCVML
RRYRGLKSGG FGVIGRPVSY EPFRLGLTFR EAPEEARPDN YMVSNGTNML LVICATPIKS
SYKVPDEILS QKSPKFAIRH TATGIISHVD SAAVSALGYL PQDLIGRSIM DFYHHEDLSV
MKETYETVMK KGQTAGASFC SKPYRFLIQN GCYVLLETEW TSFVNPWSRK LEFVVGHHRV
FQGPKQCNVF EAAPTCKLKI SEEAQSRNTR IKEDIVKRLA ETVSRPSDTV KQEVSRRCQA
LASFMETLMD EVSRADLKEG SGGSGSSGNF TTASNIHMSS VTNTSIAGTG GTGTGTGTGT
GTGTGTGTGT GTGTGTGTGT GTGTGTGTGT GNGTNSGTTS SSRGGSAAAP PVTLTESLLN
K
