PER_DROME
ID PER_DROME Reviewed; 1224 AA.
AC P07663; O17483; O76882; O76883; O76884; O76885; Q24446; Q24447; Q24448;
AC Q24449; Q6PVA3; Q8MLY0; Q9GN20; Q9GN51; Q9GQH9; Q9GV48; Q9GV53; Q9GV54;
AC Q9GV55; Q9W4X0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Period circadian protein;
DE AltName: Full=Protein clock-6;
DE Short=CLK-6;
GN Name=per; ORFNames=CG2647;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R;
RX PubMed=3102970; DOI=10.1038/326042a0;
RA Citri Y., Colot H.V., Jacquier A.C., Yu Q., Hall J.C., Baltimore D.,
RA Rosbash M.;
RT "A family of unusually spliced biologically active transcripts encoded by a
RT Drosophila clock gene.";
RL Nature 326:42-47(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PER-A-LONG).
RC STRAIN=Canton-S;
RA Baylies M.K., Weiner L., Vosshall L.B., Saez L., Young M.W.;
RT "Genetic, molecular and cellular studies of the period locus and its
RT products in Drosophila melanogaster.";
RL (In) Young M.W. (eds.);
RL Molecular genetics of biological rhythms, pp.123-153, Marcel Dekker, New
RL York (1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=3081818; DOI=10.1038/320185a0;
RA Jackson F.R., Bargiello T.A., Yun S.-H., Young M.W.;
RT "Product of per locus of Drosophila shares homology with proteoglycans.";
RL Nature 320:185-188(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT (GLY-THR)20.
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-609.
RC STRAIN=Oregon-R;
RX PubMed=15288072; DOI=10.1016/j.ympev.2004.03.013;
RA Dean M.D., Ballard J.W.O.;
RT "Linking phylogenetics with population genetics to reconstruct the
RT geographic origin of a species.";
RL Mol. Phylogenet. Evol. 32:998-1009(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-573.
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-400; 744-926 AND 1076-1218.
RC STRAIN=L18, SP1, and U79;
RA Horio A.T., Date A., Noda R., Tajima F., Chigusa S.I., Kondo R.;
RT "Population structure and founder effect in the colonization of D.simulans
RT based on DNA sequence variation in the Drosophila clock gene period.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-1075, AND VARIANT (GLY-THR)20.
RC STRAIN=Oregon-R;
RX PubMed=3087625; DOI=10.1016/0092-8674(86)90859-7;
RA Reddy P., Jacquier A.C., Abovich N., Petersen G., Rosbash M.;
RT "The period clock locus of D. melanogaster codes for a proteoglycan.";
RL Cell 46:53-61(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 683-932, AND VARIANT (GLY-THR)20.
RX PubMed=11007323; DOI=10.1098/rspb.2000.1169;
RA Lachaise D., Harry M., Solignac M., Lemeunier F., Benassi V., Cariou M.L.;
RT "Evolutionary novelties in islands: Drosophila santomea, a new melanogaster
RT sister species from Sao Tome.";
RL Proc. R. Soc. B 267:1487-1495(2000).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1155-1224.
RC STRAIN=AF1, AF2, AF3, AF4, K1, K11, K13, K14, K16, K17, K2, K20, K21, K3,
RC K5, K7, K9, Wi1, Wi10, Wi12, Wi13, Wi14, Wi15, Wi16, Wi17, Wi18, Wi19, Wi2,
RC Wi21, Wi22, Wi23, Wi24, Wi25, Wi27, Wi28, Wi29, Wi3, Wi30, Wi31, Wi32,
RC Wi33, Wi4, Wi5, Wi6, Wi7, Wi8, Wi9, ZH1, ZH13, ZH16, ZH18, ZH19, ZH2, ZH20,
RC ZH21, ZH23, ZH25, ZH29, ZH31, ZH33, ZH35, and ZH36;
RX PubMed=12351680; DOI=10.1073/pnas.202336899;
RA Harr B., Kauer M., Schloetterer C.;
RT "Hitchhiking mapping: a population-based fine-mapping strategy for adaptive
RT mutations in Drosophilamelanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12949-12954(2002).
RN [13]
RP PHOSPHORYLATION.
RX PubMed=8134384; DOI=10.1073/pnas.91.6.2260;
RA Edery I., Zwiebel L.J., Dembinska M.E., Rosbash M.;
RT "Temporal phosphorylation of the Drosophila period protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2260-2264(1994).
RN [14]
RP FUNCTION.
RX PubMed=27814361; DOI=10.1371/journal.pgen.1006430;
RA Zhou J., Yu W., Hardin P.E.;
RT "CLOCKWORK ORANGE enhances PERIOD mediated rhythms in transcriptional
RT repression by antagonizing E-box binding by CLOCK-CYCLE.";
RL PLoS Genet. 12:E1006430-E1006430(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 232-599, AND SUBUNIT.
RX PubMed=15629718; DOI=10.1016/j.molcel.2004.11.022;
RA Yildiz O., Doi M., Yujnovsky I., Cardone L., Berndt A., Hennig S.,
RA Schulze S., Urbanke C., Sassone-Corsi P., Wolf E.;
RT "Crystal structure and interactions of the PAS repeat region of the
RT Drosophila clock protein PERIOD.";
RL Mol. Cell 17:69-82(2005).
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. Required for binding of cwo to the
CC E box regions in the promoters of target genes of the transcriptional
CC activator Clock, probably by binding to Clock-cycle heterodimers,
CC reducing their affinity for E box binding and allowing cwo to bind
CC instead (PubMed:27814361). {ECO:0000269|PubMed:27814361}.
CC -!- SUBUNIT: Forms a heterodimer with timeless (TIM); the complex then
CC translocates into the nucleus. A proportion of the protein exists as
CC homodimer. {ECO:0000269|PubMed:15629718}.
CC -!- INTERACTION:
CC P07663-1; P07663-1: per; NbExp=3; IntAct=EBI-15718452, EBI-15718452;
CC P07663-1; P49021: tim; NbExp=2; IntAct=EBI-15718452, EBI-266295;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, perinuclear region.
CC Note=Nuclear at specific periods of the day. First accumulates in the
CC perinuclear region about one hour before translocation into the
CC nucleus. Interaction with Tim is required for nuclear localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=PER-A-long; Synonyms=perA;
CC IsoId=P07663-1; Sequence=Displayed;
CC Name=PER-A-short;
CC IsoId=P07663-2; Sequence=VSP_004657;
CC Name=PER-B;
CC IsoId=P07663-3; Sequence=VSP_004658;
CC Name=PER-C;
CC IsoId=P07663-4; Sequence=VSP_004660;
CC Name=PER-D;
CC IsoId=P07663-5; Sequence=VSP_004659;
CC Name=PER-E;
CC IsoId=P07663-6; Sequence=VSP_004659, VSP_004661;
CC -!- TISSUE SPECIFICITY: Expressed in neural tissues and in several
CC nonneural tissues of the abdomen. Malpighian tubules contain a
CC circadian pacemaker that functions independently of the brain.
CC Expression oscillates in all tissues studied except for the ovary. PER-
CC A isoforms are mainly expressed in adult's head.
CC -!- INDUCTION: Expression is sensitive to temperature but not to light.
CC -!- DOMAIN: Contains a remarkable run of alternating Gly-Thr residues which
CC is polymorphic in length. At least three types of Gly-Thr length exist
CC in the natural population, (Gly-Thr)23 (shown here), and two major
CC variants (Gly-Thr)17 and (Gly-Thr)20. This Gly-Thr stretch is
CC implicated in the maintenance of circadian period at different
CC temperatures. Deletion of the repeat leads to a shortening of the
CC courtship song cycle period, and thus could be important for
CC determining features of species-specific mating behavior.
CC -!- DOMAIN: Mutations in the PAS domain result in longer circadian rhythms
CC and courtship song (PERL mutation) or makes the flies arrhythmic (PER01
CC mutation).
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 {ECO:0000269|PubMed:8134384}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27285.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The tale of a love song
CC - Issue 6 of January 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/006";
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DR EMBL; M30114; AAA28752.1; -; Genomic_DNA.
DR EMBL; M30114; AAA28753.1; -; Genomic_DNA.
DR EMBL; M30114; AAA28754.1; -; Genomic_DNA.
DR EMBL; AF033029; AAB87476.1; -; mRNA.
DR EMBL; X03636; CAA27285.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014298; AAF45804.1; -; Genomic_DNA.
DR EMBL; AL024485; CAA19677.1; -; Genomic_DNA.
DR EMBL; AL024485; CAA19678.1; -; Genomic_DNA.
DR EMBL; AL024485; CAA19679.1; -; Genomic_DNA.
DR EMBL; AL024485; CAA19680.1; -; Genomic_DNA.
DR EMBL; AY575847; AAS89667.1; -; Genomic_DNA.
DR EMBL; L07817; AAA28777.1; -; Genomic_DNA.
DR EMBL; L07818; AAA28776.1; -; Genomic_DNA.
DR EMBL; L07819; AAA28775.1; -; Genomic_DNA.
DR EMBL; L07821; AAA28773.1; -; Genomic_DNA.
DR EMBL; L07823; AAA28771.1; -; Genomic_DNA.
DR EMBL; L07825; AAA28769.1; -; Genomic_DNA.
DR EMBL; AB029194; BAB15868.1; -; Genomic_DNA.
DR EMBL; AB029195; BAB15869.1; -; Genomic_DNA.
DR EMBL; AB029196; BAB15870.1; -; Genomic_DNA.
DR EMBL; AB029222; BAB15896.1; -; Genomic_DNA.
DR EMBL; AB029223; BAB15897.1; -; Genomic_DNA.
DR EMBL; AB029224; BAB15898.1; -; Genomic_DNA.
DR EMBL; AB029250; BAB15924.1; -; Genomic_DNA.
DR EMBL; AB029251; BAB15925.1; -; Genomic_DNA.
DR EMBL; AB029252; BAB15926.1; -; Genomic_DNA.
DR EMBL; D00009; BAA00007.1; -; Genomic_DNA.
DR EMBL; AF251241; AAG44573.1; -; Genomic_DNA.
DR EMBL; AY047980; AAN02289.1; -; Genomic_DNA.
DR EMBL; AY047981; AAN02291.1; -; Genomic_DNA.
DR EMBL; AY047982; AAN02293.1; -; Genomic_DNA.
DR EMBL; AY047983; AAN02295.1; -; Genomic_DNA.
DR EMBL; AY047984; AAN02297.1; -; Genomic_DNA.
DR EMBL; AY047985; AAN02299.1; -; Genomic_DNA.
DR EMBL; AY047986; AAN02301.1; -; Genomic_DNA.
DR EMBL; AY047987; AAN02303.1; -; Genomic_DNA.
DR EMBL; AY047988; AAN02305.1; -; Genomic_DNA.
DR EMBL; AY047989; AAN02307.1; -; Genomic_DNA.
DR EMBL; AY047990; AAN02309.1; -; Genomic_DNA.
DR EMBL; AY047991; AAN02311.1; -; Genomic_DNA.
DR EMBL; AY047992; AAN02313.1; -; Genomic_DNA.
DR EMBL; AY047993; AAN02315.1; -; Genomic_DNA.
DR EMBL; AY047994; AAN02317.1; -; Genomic_DNA.
DR EMBL; AY047995; AAN02319.1; -; Genomic_DNA.
DR EMBL; AY047996; AAN02321.1; -; Genomic_DNA.
DR EMBL; AY047997; AAN02323.1; -; Genomic_DNA.
DR EMBL; AY047998; AAN02325.1; -; Genomic_DNA.
DR EMBL; AY047999; AAN02327.1; -; Genomic_DNA.
DR EMBL; AY048000; AAN02329.1; -; Genomic_DNA.
DR EMBL; AY048001; AAN02331.1; -; Genomic_DNA.
DR EMBL; AY048002; AAN02333.1; -; Genomic_DNA.
DR EMBL; AY048003; AAN02335.1; -; Genomic_DNA.
DR EMBL; AY048004; AAN02337.1; -; Genomic_DNA.
DR EMBL; AY048005; AAN02339.1; -; Genomic_DNA.
DR EMBL; AY048006; AAN02341.1; -; Genomic_DNA.
DR EMBL; AY048007; AAN02343.1; -; Genomic_DNA.
DR EMBL; AY048008; AAN02345.1; -; Genomic_DNA.
DR EMBL; AY048009; AAN02347.1; -; Genomic_DNA.
DR EMBL; AY048010; AAN02349.1; -; Genomic_DNA.
DR EMBL; AY048011; AAN02351.1; -; Genomic_DNA.
DR EMBL; AY048012; AAN02353.1; -; Genomic_DNA.
DR EMBL; AY048013; AAN02355.1; -; Genomic_DNA.
DR EMBL; AY048014; AAN02357.1; -; Genomic_DNA.
DR EMBL; AY048015; AAN02359.1; -; Genomic_DNA.
DR EMBL; AY048016; AAN02361.1; -; Genomic_DNA.
DR EMBL; AY048017; AAN02363.1; -; Genomic_DNA.
DR EMBL; AY048018; AAN02365.1; -; Genomic_DNA.
DR EMBL; AY048019; AAN02367.1; -; Genomic_DNA.
DR EMBL; AY048020; AAN02369.1; -; Genomic_DNA.
DR EMBL; AY048021; AAN02371.1; -; Genomic_DNA.
DR EMBL; AY048022; AAN02373.1; -; Genomic_DNA.
DR EMBL; AY048023; AAN02375.1; -; Genomic_DNA.
DR EMBL; AY048024; AAN02377.1; -; Genomic_DNA.
DR EMBL; AY048025; AAN02379.1; -; Genomic_DNA.
DR EMBL; AY048026; AAN02381.1; -; Genomic_DNA.
DR EMBL; AY048027; AAN02383.1; -; Genomic_DNA.
DR EMBL; AY048028; AAN02385.1; -; Genomic_DNA.
DR EMBL; AY048029; AAN02387.1; -; Genomic_DNA.
DR EMBL; AY048030; AAN02389.1; -; Genomic_DNA.
DR EMBL; AY048031; AAN02391.1; -; Genomic_DNA.
DR EMBL; AY048032; AAN02393.1; -; Genomic_DNA.
DR EMBL; AY048033; AAN02395.1; -; Genomic_DNA.
DR EMBL; AY048034; AAN02397.1; -; Genomic_DNA.
DR EMBL; AY048035; AAN02399.1; -; Genomic_DNA.
DR EMBL; AY048036; AAN02401.1; -; Genomic_DNA.
DR EMBL; AY048037; AAN02403.1; -; Genomic_DNA.
DR EMBL; AY048038; AAN02405.1; -; Genomic_DNA.
DR EMBL; AY048040; AAN02407.1; -; Genomic_DNA.
DR EMBL; AY048041; AAN02409.1; -; Genomic_DNA.
DR EMBL; AY048042; AAN02411.1; -; Genomic_DNA.
DR PIR; A23932; UMFF.
DR PIR; A26427; A26427.
DR PIR; A26588; A26588.
DR PIR; B26427; B26427.
DR PIR; C26427; C26427.
DR PIR; S52943; S52943.
DR RefSeq; NP_001259194.1; NM_001272265.1.
DR RefSeq; NP_525056.2; NM_080317.2.
DR PDB; 1WA9; X-ray; 3.15 A; A/B=232-599.
DR PDB; 3GEC; X-ray; 4.00 A; A=232-538.
DR PDB; 3RTY; X-ray; 2.85 A; A/B/C/D/E/F/G/H=236-574.
DR PDBsum; 1WA9; -.
DR PDBsum; 3GEC; -.
DR PDBsum; 3RTY; -.
DR AlphaFoldDB; P07663; -.
DR SMR; P07663; -.
DR BioGRID; 57782; 38.
DR DIP; DIP-29426N; -.
DR IntAct; P07663; 4.
DR STRING; 7227.FBpp0070455; -.
DR iPTMnet; P07663; -.
DR PaxDb; P07663; -.
DR EnsemblMetazoa; FBtr0070477; FBpp0070455; FBgn0003068.
DR GeneID; 31251; -.
DR KEGG; dme:Dmel_CG2647; -.
DR CTD; 31251; -.
DR FlyBase; FBgn0003068; per.
DR VEuPathDB; VectorBase:FBgn0003068; -.
DR eggNOG; KOG3753; Eukaryota.
DR GeneTree; ENSGT00940000174107; -.
DR HOGENOM; CLU_002704_0_0_1; -.
DR InParanoid; P07663; -.
DR Reactome; R-DME-432395; Degradation of TIM.
DR Reactome; R-DME-432490; Nuclear import of PER and TIM.
DR Reactome; R-DME-432501; Transcription repression by PER and activation by PDP1.
DR Reactome; R-DME-432524; Degradation of PER.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-432620; Dephosphorylation of PER.
DR Reactome; R-DME-538898; Dephosphorylation of TIM.
DR SignaLink; P07663; -.
DR BioGRID-ORCS; 31251; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P07663; -.
DR GenomeRNAi; 31251; -.
DR PRO; PR:P07663; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003068; Expressed in VUM neuron (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P07663; baseline and differential.
DR Genevisible; P07663; DM.
DR GO; GO:0044297; C:cell body; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; NAS:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:FlyBase.
DR GO; GO:0001222; F:transcription corepressor binding; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:FlyBase.
DR GO; GO:0048148; P:behavioral response to cocaine; NAS:FlyBase.
DR GO; GO:0048512; P:circadian behavior; IMP:FlyBase.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0042745; P:circadian sleep/wake cycle; TAS:FlyBase.
DR GO; GO:0060086; P:circadian temperature homeostasis; IMP:FlyBase.
DR GO; GO:0007620; P:copulation; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; NAS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0008062; P:eclosion rhythm; IMP:FlyBase.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0045433; P:male courtship behavior, veined wing generated song production; TAS:FlyBase.
DR GO; GO:0007617; P:mating behavior; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IMP:FlyBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; TAS:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0009266; P:response to temperature stimulus; TAS:FlyBase.
DR GO; GO:0007622; P:rhythmic behavior; TAS:FlyBase.
DR CDD; cd00130; PAS; 2.
DR IDEAL; IID50270; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1224
FT /note="Period circadian protein"
FT /id="PRO_0000162596"
FT DOMAIN 238..373
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 391..497
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REPEAT 694..695
FT /note="1"
FT REPEAT 697..698
FT /note="2"
FT REPEAT 699..700
FT /note="3"
FT REPEAT 701..702
FT /note="4"
FT REPEAT 703..704
FT /note="5"
FT REPEAT 705..706
FT /note="6"
FT REPEAT 707..708
FT /note="7"
FT REPEAT 709..710
FT /note="8"
FT REPEAT 711..712
FT /note="9"
FT REPEAT 713..714
FT /note="10"
FT REPEAT 715..716
FT /note="11"
FT REPEAT 717..718
FT /note="12"
FT REPEAT 719..720
FT /note="13"
FT REPEAT 721..722
FT /note="14"
FT REPEAT 723..724
FT /note="15"
FT REPEAT 725..726
FT /note="16"
FT REPEAT 727..728
FT /note="17"
FT REPEAT 729..730
FT /note="18"
FT REPEAT 731..732
FT /note="19"
FT REPEAT 733..734
FT /note="20"
FT REPEAT 735..736
FT /note="21"
FT REPEAT 737..738
FT /note="22"
FT REPEAT 739..740
FT /note="23"
FT REPEAT 741..742
FT /note="24"
FT REPEAT 743..744
FT /note="25"
FT REPEAT 745..746
FT /note="26"
FT REPEAT 747..748
FT /note="27; approximate"
FT REPEAT 749..750
FT /note="28"
FT REPEAT 751..752
FT /note="29"
FT REPEAT 753..754
FT /note="30"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..754
FT /note="30 X 2 AA approximate tandem repeats of G-[TN]"
FT REGION 749..868
FT /note="Regulates the rhythm of species-specific courtship
FT song"
FT REGION 788..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 66..79
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform PER-A-short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004657"
FT VAR_SEQ 863..958
FT /note="Missing (in isoform PER-D and isoform PER-E)"
FT /evidence="ECO:0000305"
FT /id="VSP_004659"
FT VAR_SEQ 868..963
FT /note="Missing (in isoform PER-B)"
FT /evidence="ECO:0000305"
FT /id="VSP_004658"
FT VAR_SEQ 1076..1224
FT /note="TTPASMTKKVPGAFHSVTTPAQVQRPSSQSASVKTEPGSSAAVSDPCKKEVP
FT DSSPIPSVMGDYNSDPPCSSSNPANNKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSE
FT SPPDTEKDPKHRKLKSMSTSESKIMEHPEEDQTQHGDG -> VSQWPVVPHRTVLTPTP
FT TPYSSIDHAGVHDEEGAGCIPLGHHSCPGAASLLAERIRQDGAGLQCSGIRSLQEGGAG
FT LLAHSLRDGRLQLRPALQQQQSRQQQGMLYE (in isoform PER-C)"
FT /evidence="ECO:0000305"
FT /id="VSP_004660"
FT VAR_SEQ 1155..1224
FT /note="KYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDPKHRKLKSMSTS
FT ESKIMEHPEEDQTQHGDG -> VCYTNEVHW (in isoform PER-E)"
FT /evidence="ECO:0000305"
FT /id="VSP_004661"
FT VARIANT 697..708
FT /note="Missing (in (Gly-Thr)17)"
FT VARIANT 697..702
FT /note="Missing (in (Gly-Thr)20)"
FT VARIANT 748
FT /note="S -> F (in strain: U79)"
FT VARIANT 762
FT /note="T -> S (in strain: Berkeley, L18, Oregon-R, SP1 and
FT U79)"
FT VARIANT 846
FT /note="A -> T (in strain: U79)"
FT VARIANT 858
FT /note="V -> A (in strain: L18 and U79)"
FT VARIANT 1176
FT /note="S -> P (in strain: L18)"
FT CONFLICT 211
FT /note="G -> V (in Ref. 8; AAA28777)"
FT /evidence="ECO:0000305"
FT CONFLICT 498..499
FT /note="GP -> A (in Ref. 8; AAA28777)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="E -> A (in Ref. 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 733..767
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 762..764
FT /note="TAA -> RR (in Ref. 3 and 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="L -> V (in Ref. 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="A -> P (in Ref. 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="T -> TVSQWPV (in Ref. 6; CAA19677)"
FT /evidence="ECO:0000305"
FT CONFLICT 1114
FT /note="S -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1215
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3RTY"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1WA9"
FT STRAND 335..346
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 433..446
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 468..479
FT /evidence="ECO:0007829|PDB:3RTY"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 485..497
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:3RTY"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 516..535
FT /evidence="ECO:0007829|PDB:3RTY"
FT TURN 544..550
FT /evidence="ECO:0007829|PDB:3RTY"
FT HELIX 554..573
FT /evidence="ECO:0007829|PDB:3RTY"
SQ SEQUENCE 1224 AA; 127852 MW; 71FA54ECF3E90F4A CRC64;
MEGGESTEST HNTKVSDSAY SNSCSNSQSQ RSGSSKSRLS GSHSSGSSGY GGKPSTQASS
SDMIIKRNKD KSRKKKKNKG AGQGAGQAQT LISASTSLEG RDEEKPRPSG TGCVEQQICR
ELQDQQHGED HSEPQAIEQL QQEEEEDQSG SESEADRVEG VAKSEAAQSF PIPSPLSVTI
VPPSMGGCGG VGHAAGLDSG LAKFDKTWEA GPGKLESMTG VGAAAAGTGQ RGERVKEDSF
CCVISMHDGI VLYTTPSITD VLGYPRDMWL GRSFIDFVHL KDRATFASQI TTGIPIAESR
GSVPKDAKST FCVMLRRYRG LKSGGFGVIG RPVSYEPFRL GLTFREAPEE ARPDNYMVSN
GTNMLLVICA TPIKSSYKVP DEILSQKSPK FAIRHTATGI ISHVDSAAVS ALGYLPQDLI
GRSIMDFYHH EDLSVMKETY ETVMKKGQTA GASFCSKPYR FLIQNGCYVL LETEWTSFVN
PWSRKLEFVV GHHRVFQGPK QCNVFEAAPT CKLKISEEAQ SRNTRIKEDI VKRLAETVSR
PSDTVKQEVS RRCQALASFM ETLMDEVSRA DLKLELPHEN ELTVSERDSV MLGEISPHHD
YYDSKSSTET PPSYNQLNYN ENLLRFFNSK PVTAPAELDP PKTEPPEPRG TCVSGASGPM
SPVHEGSGGS GSSGNFTTAS NIHMSSVTNT SIAGTGGTGT GTGTGTGTGT GTGTGTGTGT
GTGTGTGTGT GTGTGTGTGT GTGNGTNSGT GTGTASSSKG GTAAIPPVTL TESLLNKHND
EMEKFMLKKH RESRGRTGEK SKKSANDTLK MLEYSGPGHG IKRGGSHSWE GEANKPKQQL
TLGTDAIKGA AGSAGGAVGT GGVGSGGAGV AGGGGSGTGV AGTPEGRATT TSGTGTPGGA
GGGGGAGAAA AAGASSSVGS STPGPSSYPT CTQNINLWPP FSVGITPPVH STHTAMAQSS
FSSAGLFPTF YYIPASLTPT SPTRSPRMHK HPHKGGTDMP TTSQQAAAAA AQAMPLQYMA
GVMYPHPSLF YTHPAAAAAT AMMYQPMPFP GMANALQIPE RPLGSQSAYN KSVYTTTPAS
MTKKVPGAFH SVTTPAQVQR PSSQSASVKT EPGSSAAVSD PCKKEVPDSS PIPSVMGDYN
SDPPCSSSNP ANNKKYTDSN GNSDDMDGSS FSSFYSSFIK TTDGSESPPD TEKDPKHRKL
KSMSTSESKI MEHPEEDQTQ HGDG
