PER_DROSC
ID PER_DROSC Reviewed; 375 AA.
AC P91705;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Period circadian protein;
DE Flags: Fragment;
GN Name=per;
OS Drosophila sucinea (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46791;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=0791.3;
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}.
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DR EMBL; U51091; AAB41394.1; -; Genomic_DNA.
DR AlphaFoldDB; P91705; -.
DR FlyBase; FBgn0017934; Dsuc\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..>375
FT /note="Period circadian protein"
FT /id="PRO_0000162607"
FT REGION 27..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 375
SQ SEQUENCE 375 AA; 38358 MW; 5C0111511ABAF63A CRC64;
SSTETPPSYN QLNYNENLLR FFNSKPVTAP VELDPPKVEP SYVSSAREDA RSTLSPVQGF
EGSGGTGSSG NFTTGSNLHM SSVTNTSNAG TGTSGTGNSG GGGGGGGGAG PGNGAVPPVT
LTESLLNKHN DEMEKFMLKK HRESRGRSGE KNKKSANDTL KMVEYSGPGP GPGHGHGIKR
GGSHSWEGEA NKPKQLLTLN TGGMPPLLDI HTSSASLSKC QASGAGGGGS GSVGGTGNIG
SGGSNAQPST NQYTQSGLSC TQNINLWPPF SVGITTPTSV LSTHTAVAQS SFSTQHNLFP
TFYYIPASIA ASSPSGTSPN PRPHKHTLVH KSAEQPSTSQ AAAATMPLQY MTGLMYPHPS
LFYTHPAAAA ATAMV