PER_DROVI
ID PER_DROVI Reviewed; 1087 AA.
AC P12349;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Period circadian protein;
GN Name=per;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3208754; DOI=10.1002/j.1460-2075.1988.tb03279.x;
RA Colot H.V., Hall J.C., Rosbash M.;
RT "Interspecific comparison of the period gene of Drosophila reveals large
RT blocks of non-conserved coding DNA.";
RL EMBO J. 7:3929-3937(1988).
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 -!- 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; X13877; CAA32081.1; -; Genomic_DNA.
DR PIR; S02035; S02035.
DR AlphaFoldDB; P12349; -.
DR SMR; P12349; -.
DR STRING; 7244.FBpp0231099; -.
DR eggNOG; KOG3753; Eukaryota.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; 2.
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..1087
FT /note="Period circadian protein"
FT /id="PRO_0000162613"
FT DOMAIN 220..355
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 373..479
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 65..78
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 118081 MW; 3585A3A581E5124D CRC64;
MEGESTESTH NTKVSDSAYS NSCSNSQSQR SGSSKSRLSG SHSSGSSGYG GKPSTQASSS
DMAVKRNKDK SRKKKKAKSP AQATAATTTT IKSLEQTEEP LLVKPNNGSC EQQLELQDAQ
QLGAPTPSDA HDAHGDKPQL DVDEQQDDPQ AEQIQQLETA TAATISPDTM SASVTVTIDG
CTSMEKTCEW TDRPGRLEAH AACIGKQHVQ QQQHDRVKED SFCCVISMHD GVVLFTTANL
NEMLGYPREM WLGRSFIDFV HIKDRATFAS QITTGIPIAE SRCSQSKDAR TTFCVMLRRY
RGLASGGFGI IGRPVSYAPF RLGLTFREAP EEVQPDGCTL SNATSMLLVI SATPIKSCYK
EPDEFLSPKG PKFAIQHTAA GIISHVDTAA VSALGYLPQD LIGRSILDFY HHEDLSDIKD
IYEKVVKKGQ TVGATFCSKP FRFLIQNGCY ILLETEWTSF VNPWSRKLEF VVGHHRVFQG
PKQCDVFEMS PNVTPNIPED EQNRNACIKE DILKMMTETV TRPSDTVKQE VSRRCQALAS
FMETLMDEVA RGDLKLDLPH ETELTVSERD SVMLGEISPH HDYYDSKSST ETPPSYNQLN
YNENLLRFFN SKPVTAPVDT DPPKMDSSYV SSAREDALSP VHGFEGSGGS GSSGNLTTAS
NVRMSSVTNT SNTGTGTSGG ENSASGSSNP LPVNMTLTEI LLNKHNDEME KCMLKKHRES
RGRTGDKTKK SVIEKMPEYS GPGHGQTMKR GGSHSWEGDA NKPKQQLTLS AVVVAPTVSV
SPAEDSQTTA KWQAPMTGSH LFQSSYNFPQ SINLWPPFSL GLTTPTVHTT HTSMAQKSFS
PQHNLFPAFY YIPAPLATAT AGSAAAQTSV SSASAAQHSP KSSENPSTSQ PEATAATAMP
MPYMAGVMYP HPSLFYAYQP MPFPSVSGAV QMSVQSSGSQ SNNNNKSIYT MAPASTTTQK
PGAFHSITPA ELNKPDAPDT LLHTETSPKI SVQEAPKKEL SDLPSTSARR GSSSDQRNNS
NNPKKYTDSN GNSDDMDGSS FSSFYSSFIK TTDGSESPPD NEKETKVHKL KPIVEHPEED
QTQHGDG
