ID   PER_MANSE               Reviewed;         354 AA.
AC   Q25478;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Period circadian protein;
DE   Flags: Fragment;
GN   Name=per;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7946353; DOI=10.1016/0896-6273(94)90054-x;
RA   Reppert S.M., Tsai T., Roca A.L., Sauman I.;
RT   "Cloning of a structural and functional homolog of the circadian clock gene
RT   period from the giant silkmoth Antheraea pernyi.";
RL   Neuron 13:1167-1176(1994).
CC   -!- FUNCTION: Involved in the generation of biological rhythms. The
CC       biological cycle depends on the rhythmic formation and nuclear
CC       localization of the tim-per complex. Light induces the degradation of
CC       tim, which promotes elimination of per. Nuclear activity of the
CC       heterodimer coordinatively regulates per and tim transcription negative
CC       feedback loop. Behaves as a negative element in circadian
CC       transcriptional loop. Does not appear to bind DNA, suggesting indirect
CC       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. Note=Nuclear at specific periods of the
CC       day. Interaction with TIM is required for nuclear localization (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated with a circadian rhythmicity. {ECO:0000250}.
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DR   EMBL; U12773; AAA64678.1; -; mRNA.
DR   AlphaFoldDB; Q25478; -.
DR   SMR; Q25478; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048856; P:anatomical structure development; 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; IPR013655; PAS_fold_3.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN           <1..>354
FT                   /note="Period circadian protein"
FT                   /id="PRO_0000162621"
FT   DOMAIN          <1..55
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          133..235
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          318..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         354
SQ   SEQUENCE   354 AA;  40303 MW;  E2AE4567BA1F8017 CRC64;
     GIVMYTTSSL TTTLGFPKDM WIGRSFIDFV HPRDRNTFAS QITSGLAVPK IVNGQSPGNP
     ASTMVCRIRR YRGLTTGFGV KDRVVTFMPF LLKFTFKNVS DEEGKVIYLV IQATQFFSAF
     RIPSEVVSKA VPFVMRHAAN GNLEYIDPES VPYLGYLPQD VTDKDALQLY HPEDLDYLQQ
     VYETIVKEGG VPRTKAYRMM AQNGDYLKLE TEWSSFINPW SKRLDFVIGK HHIIEGPSNP
     DVFQSPDPEK AVAMSEEEKA KEQKYRRDII RTMNEVLTKP AEVAKQQMTK RCQDLASFME
     SLMEEQQPKV DEDLRLDIQD PDHSYYQRDS VMLGGISPHH DYNDSKSSTG TPLS