ID   PER_DROTP               Reviewed;         390 AA.
AC   P91716;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Period circadian protein;
DE   Flags: Fragment;
GN   Name=per;
OS   Drosophila tropicalis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=0801.0 San Salvador / El Salvador;
RX   PubMed=9214747; DOI=10.1093/oxfordjournals.molbev.a025814;
RA   Gleason J.M., Powell J.R.;
RT   "Interspecific and intraspecific comparisons of the period locus in the
RT   Drosophila willistoni sibling species.";
RL   Mol. Biol. Evol. 14:741-753(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U51087; AAB41395.1; -; Genomic_DNA.
DR   AlphaFoldDB; P91716; -.
DR   FlyBase; FBgn0017841; Dtro\per.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Biological rhythms; Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN           <1..>390
FT                   /note="Period circadian protein"
FT                   /id="PRO_0000162612"
FT   REGION          27..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         390
SQ   SEQUENCE   390 AA;  39544 MW;  A40C4242BD33DD93 CRC64;
     SSTETPPSYN QLNYNENLLR FFNSKPVTAP VELDPPKVES SYVSSARGED ARSTLSPVQG
     FEGSGGSGSS GNFTTGSNLH MSSVTNTSNA GTGTSGTGNS GDGGGGGGAD GTGSGAAPPV
     TLTESLLNKH NDEMEKFMLK KHRESRGRSG EKNKKSANEA MKMLEYSGPG PGHGHGIKRG
     GSHSWEGEAN KPKQQLTLNP SGGGGGMPLL LDITHTSSST QNKGLAGVGV GGAGGGVGGG
     GSGTGLGGNG NVGSGNGNNN QASTNQYTQS GLPCTQNINL WPPFSVGITT PTSVLSSHTA
     VAQSSFSPQH SLFPTFYYIP ASIAASSPSG TNPSPNRPHK HAHVHSSSEK PSTSQAAAAT
     MPLQYMTGVM YPHPSLFYTH PAAAAATAMV