PER_DROMA
ID PER_DROMA Reviewed; 676 AA.
AC Q03353; Q26283;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Period circadian protein;
DE Flags: Fragments;
GN Name=per;
OS Drosophila mauritiana (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-559.
RC STRAIN=MA-1, MA-2, MA-3, MA-4, MA-5, and MA-6;
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 560-676.
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}.
CC -!- MISCELLANEOUS: The sequence shown here is that of clones MA-1, MA-2,
CC MA-4 and MA-5.
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DR EMBL; L07811; AAA28778.1; -; Genomic_DNA.
DR EMBL; L07812; AAA28784.1; -; Genomic_DNA.
DR EMBL; L07813; AAA28783.1; -; Genomic_DNA.
DR EMBL; L07814; AAA28782.1; -; Genomic_DNA.
DR EMBL; L07815; AAA28781.1; -; Genomic_DNA.
DR EMBL; L07816; AAA28780.1; -; Genomic_DNA.
DR EMBL; S53294; AAB25026.2; -; Genomic_DNA.
DR PIR; S52935; S52935.
DR PIR; S52937; S52937.
DR PIR; S52938; S52938.
DR PIR; S52940; S52940.
DR AlphaFoldDB; Q03353; -.
DR SMR; Q03353; -.
DR FlyBase; FBgn0012516; Dmau\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: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; 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..>676
FT /note="Period circadian protein"
FT /id="PRO_0000162595"
FT DOMAIN 224..359
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 377..483
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REPEAT 589..590
FT /note="1"
FT REPEAT 592..593
FT /note="2"
FT REPEAT 594..595
FT /note="3"
FT REPEAT 596..597
FT /note="4"
FT REPEAT 598..599
FT /note="5"
FT REPEAT 600..601
FT /note="6"
FT REPEAT 602..603
FT /note="7"
FT REPEAT 604..605
FT /note="8"
FT REPEAT 606..607
FT /note="9"
FT REPEAT 608..609
FT /note="10"
FT REPEAT 610..611
FT /note="11"
FT REPEAT 612..613
FT /note="12"
FT REPEAT 614..615
FT /note="13"
FT REPEAT 616..617
FT /note="14"
FT REPEAT 618..619
FT /note="15"
FT REPEAT 620..621
FT /note="16"
FT REPEAT 622..623
FT /note="17"
FT REPEAT 624..625
FT /note="18"
FT REPEAT 626..627
FT /note="19"
FT REPEAT 628..629
FT /note="20"
FT REPEAT 630..631
FT /note="21"
FT REPEAT 632..633
FT /note="22"
FT REPEAT 634..635
FT /note="23"
FT REPEAT 636..637
FT /note="24"
FT REPEAT 638..639
FT /note="25"
FT REPEAT 640..641
FT /note="26"
FT REPEAT 642..643
FT /note="27; approximate"
FT REPEAT 644..645
FT /note="28"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..645
FT /note="28 X 2 AA approximate tandem repeats of G-T"
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 24
FT /note="S -> C (in strain: MA-6)"
FT VARIANT 57
FT /note="D -> N (in strain: MA-3)"
FT NON_CONS 559..560
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 676
SQ SEQUENCE 676 AA; 71004 MW; 11E55FEE28B705A9 CRC64;
KVSDSAYSNS CSNSQSQRSG SSKSRLSGSH SSGSSGYGGK PSTQASSSDM IIKRNKDKSR
KKKKNKGAGQ GAGQAQTLIS ASTSLEGRDE EKPRPSGTGC VEQQICRELQ DQQHGEDHSE
PQATEQLQQE EEDQSGSESE ADRVEGVAKS EAAQSFPIPS PLSVTIVPPS MGGCGGVGHA
AGLDSGLAKF DKTWEAGPGK LESMTGVGAA AAGTGQRGER VKEDSFCCVI SMHDGIVLYT
TPSITDVLGY PRDMWLGRSF IDFVHLKDRA TFASQITTGI PIAESRGSVP KDAKSTFCVM
LRRYRGLKSG GFGVIGRPVS YEPFRLGLTF REAPEEARPD NYMVSNGTNM LLVICATPIK
SSYKVPDEIL SQKSPKFAIR HTATGIISHV DSAAVSALGY LPQDLIGRSI MDFYHHEDLS
VMKETYETVM KKGQTAGASF CSKPYRFLIQ NGCYVLLETE WTSFVNPWSR KLEFVVGHHR
VFQGPKQCNV FEAAPTCKLK ISEEAQSRNT RIKEDIVKRL AETVSRPSDT VKQEVSRRCQ
ALASFMETLM DEVSRADLKE GSGGSGSSGN FTTASNIHMS SVTNTSIAGT GGTGTGTGTG
TGTGTGTGTG TGTGTGTGTG TGTGTGTGTG TGTGTGTGTG TGNGTNSCTG TGTTSSSRGG
SAAIPPVTLT ESLLNK
