PER3_HUMAN
ID PER3_HUMAN Reviewed; 1201 AA.
AC P56645; Q5H8X4; Q5H8X5; Q969K6; Q96S77; Q96S78; Q9C0J3; Q9NSP9; Q9UGU8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Period circadian protein homolog 3;
DE Short=hPER3;
DE AltName: Full=Cell growth-inhibiting gene 13 protein;
DE AltName: Full=Circadian clock protein PERIOD 3;
GN Name=PER3; ORFNames=GIG13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 44-91 AND 724-882 (ISOFORMS 1/2), AND VARIANTS GLY-639; PRO-827;
RP ALA-856; 1001-SER--PRO-1018; THR-1028 AND ARG-1149.
RX PubMed=11306557; DOI=10.1093/embo-reports/kve070;
RA Ebisawa T., Uchiyama M., Kajimura N., Mishima K., Kamei Y., Katoh M.,
RA Watanabe T., Sekimoto M., Shibui K., Kim K., Kudo Y., Ozeki Y.,
RA Sugishita M., Toyoshima R., Inoue Y., Yamada N., Nagase T., Ozaki N.,
RA Ohara O., Ishida N., Okawa M., Takahashi K., Yamauchi T.;
RT "Association of structural polymorphisms in the human period3 gene with
RT delayed sleep phase syndrome.";
RL EMBO Rep. 2:342-346(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S., Huckle E.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a growth inhibition gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919; SER-994 AND SER-1053,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP IDENTIFICATION OF VARIANT 1001-SER--PRO-1018 DEL ASSOCIATED WITH DIURNAL
RP PREFERENCE.
RX PubMed=12841365; DOI=10.1093/sleep/26.4.413;
RA Archer S.N., Robilliard D.L., Skene D.J., Smits M., Williams A., Arendt J.,
RA von Schantz M.;
RT "A length polymorphism in the circadian clock gene Per3 is linked to
RT delayed sleep phase syndrome and extreme diurnal preference.";
RL Sleep 26:413-415(2003).
RN [7]
RP INTERACTION WITH FBXW11 AND BTRC.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [8]
RP FUNCTION IN SLEEP HOMEOSTASIS, AND CHARACTERIZATION OF VARIANT
RP 1001-SER--PRO-1018 DEL.
RX PubMed=17346965; DOI=10.1016/j.cub.2007.01.073;
RA Viola A.U., Archer S.N., James L.M., Groeger J.A., Lo J.C., Skene D.J.,
RA von Schantz M., Dijk D.J.;
RT "PER3 polymorphism predicts sleep structure and waking performance.";
RL Curr. Biol. 17:613-618(2007).
RN [9]
RP FUNCTION IN SLEEP HOMEOSTASIS, CHARACTERIZATION OF VARIANT
RP 1001-SER--PRO-1018 DEL, AND REVIEW.
RX PubMed=19716732; DOI=10.1016/j.smrv.2009.07.002;
RA Dijk D.J., Archer S.N.;
RT "PERIOD3, circadian phenotypes, and sleep homeostasis.";
RL Sleep Med. Rev. 14:151-160(2010).
RN [10]
RP REVIEW.
RX PubMed=23303907; DOI=10.1152/physrev.00016.2012;
RA Eckel-Mahan K., Sassone-Corsi P.;
RT "Metabolism and the circadian clock converge.";
RL Physiol. Rev. 93:107-135(2013).
RN [11]
RP FUNCTION IN SLEEP HOMEOSTASIS, AND CHARACTERIZATION OF VARIANT
RP 1001-SER--PRO-1018 DEL.
RX PubMed=24439663; DOI=10.1016/j.cortex.2013.11.008;
RA Maire M., Reichert C.F., Gabel V., Viola A.U., Strobel W., Krebs J.,
RA Landolt H.P., Bachmann V., Cajochen C., Schmidt C.;
RT "Sleep ability mediates individual differences in the vulnerability to
RT sleep loss: evidence from a PER3 polymorphism.";
RL Cortex 52:47-59(2014).
RN [12]
RP FUNCTION IN SLEEP HOMEOSTASIS, AND CHARACTERIZATION OF VARIANT
RP 1001-SER--PRO-1018 DEL.
RX PubMed=24577121; DOI=10.1096/fj.13-240135;
RA Hasan S., van der Veen D.R., Winsky-Sommerer R., Hogben A., Laing E.E.,
RA Koentgen F., Dijk D.J., Archer S.N.;
RT "A human sleep homeostasis phenotype in mice expressing a primate-specific
RT PER3 variable-number tandem-repeat coding-region polymorphism.";
RL FASEB J. 28:2441-2454(2014).
RN [13]
RP REVIEW.
RX PubMed=23916625; DOI=10.1016/j.tcb.2013.07.002;
RA Partch C.L., Green C.B., Takahashi J.S.;
RT "Molecular architecture of the mammalian circadian clock.";
RL Trends Cell Biol. 24:90-99(2014).
RN [14]
RP VARIANT GLY-639.
RX PubMed=12655319; DOI=10.1038/sj.npp.1300121;
RA Johansson C., Willeit M., Smedh C., Ekholm J., Paunio T., Kieseppa T.,
RA Lichtermann D., Praschak-Rieder N., Neumeister A., Nilsson L.G., Kasper S.,
RA Peltonen L., Adolfsson R., Schalling M., Partonen T.;
RT "Circadian clock-related polymorphisms in seasonal affective disorder and
RT their relevance to diurnal preference.";
RL Neuropsychopharmacology 28:734-739(2003).
RN [15]
RP INVOLVEMENT IN FASPS3, VARIANT FASPS3 414-ALA--ARG-416, VARIANTS ALA-414
RP AND ARG-416, CHARACTERIZATION OF VARIANT FASPS3 414-ALA--ARG-416, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=26903630; DOI=10.1073/pnas.1600039113;
RA Zhang L., Hirano A., Hsu P.K., Jones C.R., Sakai N., Okuro M., McMahon T.,
RA Yamazaki M., Xu Y., Saigoh N., Saigoh K., Lin S.T., Kaasik K., Nishino S.,
RA Ptacek L.J., Fu Y.H.;
RT "A PERIOD3 variant causes a circadian phenotype and is associated with a
RT seasonal mood trait.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1536-E1544(2016).
CC -!- FUNCTION: Originally described as a core component of the circadian
CC clock. The circadian clock, an internal time-keeping system, regulates
CC various physiological processes through the generation of approximately
CC 24 hour circadian rhythms in gene expression, which are translated into
CC rhythms in metabolism and behavior. It is derived from the Latin roots
CC 'circa' (about) and 'diem' (day) and acts as an important regulator of
CC a wide array of physiological functions including metabolism, sleep,
CC body temperature, blood pressure, endocrine, immune, cardiovascular,
CC and renal function. Consists of two major components: the central
CC clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and
CC the peripheral clocks that are present in nearly every tissue and organ
CC system. Both the central and peripheral clocks can be reset by
CC environmental cues, also known as Zeitgebers (German for 'timegivers').
CC The predominant Zeitgeber for the central clock is light, which is
CC sensed by retina and signals directly to the SCN. The central clock
CC entrains the peripheral clocks through neuronal and hormonal signals,
CC body temperature and feeding-related cues, aligning all clocks with the
CC external light/dark cycle. Circadian rhythms allow an organism to
CC achieve temporal homeostasis with its environment at the molecular
CC level by regulating gene expression to create a peak of protein
CC expression once every 24 hours to control when a particular
CC physiological process is most active with respect to the solar day.
CC Transcription and translation of core clock components (CLOCK, NPAS2,
CC ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a
CC critical role in rhythm generation, whereas delays imposed by post-
CC translational modifications (PTMs) are important for determining the
CC period (tau) of the rhythms (tau refers to the period of a rhythm and
CC is the length, in time, of one complete cycle). A diurnal rhythm is
CC synchronized with the day/night cycle, while the ultradian and
CC infradian rhythms have a period shorter and longer than 24 hours,
CC respectively. Disruptions in the circadian rhythms contribute to the
CC pathology of cardiovascular diseases, cancer, metabolic syndromes and
CC aging. A transcription/translation feedback loop (TTFL) forms the core
CC of the molecular circadian clock mechanism. Transcription factors,
CC CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb
CC of the feedback loop, act in the form of a heterodimer and activate the
CC transcription of core clock genes and clock-controlled genes (involved
CC in key metabolic processes), harboring E-box elements (5'-CACGTG-3')
CC within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which
CC are transcriptional repressors form the negative limb of the feedback
CC loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2
CC heterodimer inhibiting its activity and thereby negatively regulating
CC their own expression. This heterodimer also activates nuclear receptors
CC NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop
CC and which activate and repress ARNTL/BMAL1 transcription, respectively.
CC Has a redundant role with the other PER proteins PER1 and PER2 and is
CC not essential for the circadian rhythms maintenance. In contrast, plays
CC an important role in sleep-wake timing and sleep homeostasis probably
CC through the transcriptional regulation of sleep homeostasis-related
CC genes, without influencing circadian parameters. Can bind heme.
CC {ECO:0000269|PubMed:17346965, ECO:0000269|PubMed:19716732,
CC ECO:0000269|PubMed:24439663, ECO:0000269|PubMed:24577121,
CC ECO:0000269|PubMed:26903630}.
CC -!- SUBUNIT: Homodimer. Component of the circadian core oscillator, which
CC includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2,
CC CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly
CC with PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and
CC CRY2 is weak and not rhythmic. Interacts with FBXW11 and BTRC.
CC {ECO:0000269|PubMed:15917222}.
CC -!- INTERACTION:
CC P56645; O96017: CHEK2; NbExp=2; IntAct=EBI-2827813, EBI-1180783;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26903630}. Nucleus
CC {ECO:0000269|PubMed:26903630}. Note=Mainly cytoplasmic. Translocates to
CC the nucleus through binding PER1, PER2, CRY1 or CRY2, but not TIMELESS.
CC {ECO:0000250|UniProtKB:O70361}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56645-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56645-2; Sequence=VSP_040326, VSP_040327, VSP_040328;
CC -!- PTM: Phosphorylation by CSNK1E is weak and appears to require
CC association with PER1 and translocation to the nucleus.
CC {ECO:0000250|UniProtKB:O70361}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O70361}.
CC -!- POLYMORPHISM: The number of repeats of 18 amino acids in positions 966
CC to 1055 is polymorphic and varies among at least 2 different alleles.
CC Alleles corresponding in size to a 4 (PER3.4) and 5 (PER3.5) repeats
CC have been described. The sequence shown is that of allele PER3.5. In
CC most populations around 10% of individuals are homozygous for the 5-
CC repeat (PER3.5), whereas approximately 50% are homozygous for the 4-
CC repeat (PER3.4). In some populations in Papua New Guinea the prevalence
CC of the various genotypes appears to be reversed. These repeats and
CC polymorphism are not present in non-primate mammals. Homozygosity for
CC PER3.5 is more likely to show morning preference, whereas homozygosity
CC for the PER3.4 associates with evening preferences. PER3.5 homozygous
CC show vulnerability to sleep loss with a greater cognitive decline in
CC response to total sleep deprivation (PubMed:11306557, PubMed:17346965,
CC PubMed:19716732, PubMed:24439663, PubMed:24577121).
CC {ECO:0000269|PubMed:11306557, ECO:0000269|PubMed:17346965,
CC ECO:0000269|PubMed:19716732, ECO:0000269|PubMed:24439663,
CC ECO:0000269|PubMed:24577121}.
CC -!- DISEASE: Advanced sleep phase syndrome, familial, 3 (FASPS3)
CC [MIM:616882]: A disorder characterized by very early sleep onset and
CC offset. Individuals are 'morning larks' with a 4 hours advance of the
CC sleep, temperature and melatonin rhythms.
CC {ECO:0000269|PubMed:26903630}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB32925.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB047521; BAB63250.1; -; Genomic_DNA.
DR EMBL; AB047530; BAB63251.1; -; Genomic_DNA.
DR EMBL; AB047531; BAB63252.1; -; Genomic_DNA.
DR EMBL; AB047532; BAB63253.1; -; Genomic_DNA.
DR EMBL; AB047533; BAB63254.1; -; Genomic_DNA.
DR EMBL; AB047534; BAB63255.1; -; Genomic_DNA.
DR EMBL; AB047686; BAB32925.2; ALT_INIT; mRNA.
DR EMBL; AL157954; CAB76084.1; -; mRNA.
DR EMBL; AY493418; AAS72879.1; -; mRNA.
DR EMBL; Z98884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS72695.1; -. [P56645-2]
DR CCDS; CCDS89.1; -. [P56645-1]
DR RefSeq; NP_001276790.1; NM_001289861.1.
DR RefSeq; NP_001276791.1; NM_001289862.1. [P56645-2]
DR RefSeq; NP_001276792.1; NM_001289863.1.
DR RefSeq; NP_001276793.1; NM_001289864.1.
DR RefSeq; NP_058515.1; NM_016831.2. [P56645-1]
DR AlphaFoldDB; P56645; -.
DR SMR; P56645; -.
DR BioGRID; 114386; 17.
DR ComplexPortal; CPX-3223; Cry1-Per3 complex.
DR ComplexPortal; CPX-3224; Cry2-Per3 complex.
DR IntAct; P56645; 12.
DR MINT; P56645; -.
DR STRING; 9606.ENSP00000482093; -.
DR iPTMnet; P56645; -.
DR PhosphoSitePlus; P56645; -.
DR BioMuta; PER3; -.
DR DMDM; 317373535; -.
DR EPD; P56645; -.
DR jPOST; P56645; -.
DR MassIVE; P56645; -.
DR MaxQB; P56645; -.
DR PaxDb; P56645; -.
DR PeptideAtlas; P56645; -.
DR PRIDE; P56645; -.
DR ProteomicsDB; 56931; -. [P56645-1]
DR ProteomicsDB; 56932; -. [P56645-2]
DR Antibodypedia; 13182; 212 antibodies from 32 providers.
DR DNASU; 8863; -.
DR Ensembl; ENST00000361923.2; ENSP00000355031.2; ENSG00000049246.15. [P56645-1]
DR Ensembl; ENST00000377532.8; ENSP00000366755.3; ENSG00000049246.15. [P56645-2]
DR Ensembl; ENST00000613533.4; ENSP00000482093.1; ENSG00000049246.15. [P56645-2]
DR GeneID; 8863; -.
DR KEGG; hsa:8863; -.
DR MANE-Select; ENST00000377532.8; ENSP00000366755.3; NM_001377275.1; NP_001364204.1. [P56645-2]
DR UCSC; uc001aop.5; human. [P56645-1]
DR CTD; 8863; -.
DR DisGeNET; 8863; -.
DR GeneCards; PER3; -.
DR HGNC; HGNC:8847; PER3.
DR HPA; ENSG00000049246; Low tissue specificity.
DR MalaCards; PER3; -.
DR MIM; 603427; gene.
DR MIM; 616882; phenotype.
DR neXtProt; NX_P56645; -.
DR OpenTargets; ENSG00000049246; -.
DR Orphanet; 164736; Familial advanced sleep-phase syndrome.
DR PharmGKB; PA33186; -.
DR VEuPathDB; HostDB:ENSG00000049246; -.
DR eggNOG; KOG3753; Eukaryota.
DR GeneTree; ENSGT00940000160817; -.
DR HOGENOM; CLU_006667_0_1_1; -.
DR InParanoid; P56645; -.
DR OMA; EQVLMTY; -.
DR OrthoDB; 331262at2759; -.
DR PhylomeDB; P56645; -.
DR TreeFam; TF318445; -.
DR PathwayCommons; P56645; -.
DR SignaLink; P56645; -.
DR SIGNOR; P56645; -.
DR BioGRID-ORCS; 8863; 16 hits in 1084 CRISPR screens.
DR ChiTaRS; PER3; human.
DR GeneWiki; PER3; -.
DR GenomeRNAi; 8863; -.
DR Pharos; P56645; Tbio.
DR PRO; PR:P56645; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P56645; protein.
DR Bgee; ENSG00000049246; Expressed in sural nerve and 196 other tissues.
DR ExpressionAtlas; P56645; baseline and differential.
DR Genevisible; P56645; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR015524; Per_circ_prot_3.
DR InterPro; IPR022728; Period_circadian-like_C.
DR PANTHER; PTHR11269:SF13; PTHR11269:SF13; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12114; Period_C; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Disease variant;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1201
FT /note="Period circadian protein homolog 3"
FT /id="PRO_0000162633"
FT DOMAIN 121..188
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 262..328
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 337..380
FT /note="PAC"
FT REPEAT 965..982
FT /note="1"
FT REPEAT 983..1000
FT /note="2"
FT REPEAT 1001..1018
FT /note="3"
FT REPEAT 1019..1036
FT /note="4"
FT REPEAT 1037..1054
FT /note="5"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..760
FT /note="CSNK1E binding domain"
FT /evidence="ECO:0000250"
FT REGION 717..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1054
FT /note="5 X 18 AA tandem repeats of S-[HP]-[AP]-T-[AT]-
FT [GST]-[ATV]-L-S-[MT]-G-[LS]-P-P-[MRS]-[EKR]-[NST]-P"
FT REGION 1123..1201
FT /note="CRY binding domain"
FT /evidence="ECO:0000250"
FT MOTIF 55..64
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 403..412
FT /note="Nuclear export signal 3"
FT /evidence="ECO:0000250"
FT MOTIF 729..745
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 925..932
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 197
FT /note="R -> RA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11306557"
FT /id="VSP_040326"
FT VAR_SEQ 499
FT /note="G -> GGESANGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11306557"
FT /id="VSP_040327"
FT VAR_SEQ 954
FT /note="Y -> YQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11306557"
FT /id="VSP_040328"
FT VARIANT 414..416
FT /note="PVH -> AVR (in FASPS3; decreased stability;
FT decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:26903630"
FT /id="VAR_076416"
FT VARIANT 414
FT /note="P -> A (in dbSNP:rs150812083)"
FT /evidence="ECO:0000269|PubMed:26903630"
FT /id="VAR_076417"
FT VARIANT 416
FT /note="H -> R (in dbSNP:rs139315125)"
FT /evidence="ECO:0000269|PubMed:26903630"
FT /id="VAR_076418"
FT VARIANT 639
FT /note="V -> G (associated with delayed sleep phase syndrome
FT (DSPS); dbSNP:rs10462020)"
FT /evidence="ECO:0000269|PubMed:11306557,
FT ECO:0000269|PubMed:12655319"
FT /id="VAR_025532"
FT VARIANT 827
FT /note="L -> P (in dbSNP:rs228696)"
FT /evidence="ECO:0000269|PubMed:11306557"
FT /id="VAR_022428"
FT VARIANT 856
FT /note="P -> A (in dbSNP:rs228697)"
FT /evidence="ECO:0000269|PubMed:11306557"
FT /id="VAR_015514"
FT VARIANT 1001..1018
FT /note="Missing (associated with eveningness and better
FT cognitive performance during sleep deprivation experiments;
FT dbSNP:rs57875989)"
FT /evidence="ECO:0000269|PubMed:17346965,
FT ECO:0000269|PubMed:19716732, ECO:0000269|PubMed:24439663,
FT ECO:0000269|PubMed:24577121"
FT /id="VAR_071049"
FT VARIANT 1007
FT /note="A -> T (in dbSNP:rs1776342)"
FT /id="VAR_028728"
FT VARIANT 1010
FT /note="T -> I (in dbSNP:rs12033719)"
FT /id="VAR_028729"
FT VARIANT 1028
FT /note="M -> T (only found in PER3.4 allele;
FT dbSNP:rs2640909)"
FT /evidence="ECO:0000269|PubMed:11306557"
FT /id="VAR_025533"
FT VARIANT 1081
FT /note="S -> C (in dbSNP:rs2640905)"
FT /id="VAR_028730"
FT VARIANT 1149
FT /note="H -> R (in dbSNP:rs10462021)"
FT /evidence="ECO:0000269|PubMed:11306557"
FT /id="VAR_025534"
FT CONFLICT 943
FT /note="Q -> R (in Ref. 1; BAB32925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1201 AA; 131888 MW; 8129C4246EDD1816 CRC64;
MPRGEAPGPG RRGAKDEALG EESGERWSPE FHLQRKLADS SHSEQQDRNR VSEELIMVVQ
EMKKYFPSER RNKPSTLDAL NYALRCVHSV QANSEFFQIL SQNGAPQADV SMYSLEELAT
IASEHTSKNT DTFVAVFSFL SGRLVHISEQ AALILNRKKD VLASSHFVDL LAPQDMRVFY
AHTARAQLPF WNNWTQRAAR YECAPVKPFF CRIRGGEDRK QEKCHSPFRI IPYLIHVHHP
AQPELESEPC CLTVVEKIHS GYEAPRIPVN KRIFTTTHTP GCVFLEVDEK AVPLLGYLPQ
DLIGTSILSY LHPEDRSLMV AIHQKVLKYA GHPPFEHSPI RFCTQNGDYI ILDSSWSSFV
NPWSRKISFI IGRHKVRTSP LNEDVFATKI KKMNDNDKDI TELQEQIYKL LLQPVHVSVS
SGYGSLGSSG SQEQLVSIAS SSEASGHRVE ETKAEQMTLQ QVYASVNKIK NLGQQLYIES
MTKSSFKPVT GTRTEPNGGG ECKTFTSFHQ TLKNNSVYTE PCEDLRNDEH SPSYQQINCI
DSVIRYLKSY NIPALKRKCI SCTNTTSSSS EEDKQNHKAD DVQALQAGLQ IPAIPKSEMP
TNGRSIDTGG GAPQILSTAM LSLGSGISQC GYSSTIVHVP PPETARDATL FCEPWTLNMQ
PAPLTSEEFK HVGLTAAVLS AHTQKEEQNY VDKFREKILS SPYSSYLQQE SRSKAKYSYF
QGDSTSKQTR SAGCRKGKHK RKKLPEPPDS SSSNTGSGPR RGAHQNAQPC CPSAASSPHT
SSPTFPPAAM VPSQAPYLVP AFPLPAATSP GREYAAPGTA PEGLHGLPLS EGLQPYPAFP
FPYLDTFMTV FLPDPPVCPL LSPSFLPCPF LGATASSAIS PSMSSAMSPT LDPPPSVTSQ
RREEEKWEAQ SEGHPFITSR SSSPLQLNLL QEEMPRPSES PDQMRRNTCP QTEYCVTGNN
GSESSPATTG ALSTGSPPRE NPSHPTASAL STGSPPMKNP SHPTASALST GSPPMKNPSH
PTASTLSMGL PPSRTPSHPT ATVLSTGSPP SESPSRTGSA ASGSSDSSIY LTSSVYSSKI
SQNGQQSQDV QKKETFPNVA EEPIWRMIRQ TPERILMTYQ VPERVKEVVL KEDLEKLESM
RQQQPQFSHG QKEELAKVYN WIQSQTVTQE IDIQACVTCE NEDSADGAAT SCGQVLVEDS
C
