ID   PER_HYACE               Reviewed;         358 AA.
AC   Q25020;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Period circadian protein;
DE   Flags: Fragment;
GN   Name=per;
OS   Hyalophora cecropia (Cecropia moth) (Samia cecropia).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Attacini; Hyalophora.
OX   NCBI_TaxID=7123;
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; U12771; AAA64676.1; -; mRNA.
DR   AlphaFoldDB; Q25020; -.
DR   SMR; Q25020; -.
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   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..>358
FT                   /note="Period circadian protein"
FT                   /id="PRO_0000162619"
FT   DOMAIN          <1..120
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          138..240
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   NON_TER         1
FT   NON_TER         358
SQ   SEQUENCE   358 AA;  40930 MW;  8E212B9114885EC4 CRC64;
     GVVMYTTSSI TATLGFPKDM WIGRSFIDFL HPKDANTFAS QITNGLAIPK IVNDTQEKAQ
     IFGTQGSTMV CRIRRYRGLS SGFGVKDTSV SYMPFLLKFR FRNISDDKGL VVYLVIQTVP
     FFSAYKTPNE ILTQEVSFIM RHSANGNLEY IDPDCVPYLG YIPQDITNRN ALVLYHPGDL
     PFLQEVYQAI VKEGSVTRSK SYRMVTQNGH FIKVETEWSA FINPWSRKLE FVNGKYYIIE
     GPANPDVFES PDPEKTPKLT EERKNQAQIC RDDIIRIMNE VLTNPAEIAK QQMSKRCQEL
     ALFMEILQEE QPKAEEEFHL QTQDVDHTYY ERDSVMLGGI SPHHEYNDIK SSAETSLS