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PER_DROYA
ID   PER_DROYA               Reviewed;        1208 AA.
AC   Q24767; Q26286;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Period circadian protein;
GN   Name=per;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1702156; DOI=10.1007/bf02106054;
RA   Thackeray J.R., Kyriacou C.P.;
RT   "Molecular evolution in the Drosophila yakuba period locus.";
RL   J. Mol. Evol. 31:389-401(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 669-766.
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}.
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DR   EMBL; X61127; CAA43439.1; -; Genomic_DNA.
DR   EMBL; S53298; AAB25029.2; -; Genomic_DNA.
DR   PIR; S17286; S17286.
DR   AlphaFoldDB; Q24767; -.
DR   SMR; Q24767; -.
DR   STRING; 7245.FBpp0261279; -.
DR   eggNOG; KOG3753; Eukaryota.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:EnsemblMetazoa.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:EnsemblMetazoa.
DR   GO; GO:0017022; F:myosin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR   GO; GO:0007420; P:brain development; IEA:EnsemblMetazoa.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:EnsemblMetazoa.
DR   GO; GO:0008347; P:glial cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0045676; P:regulation of R7 cell differentiation; IEA:EnsemblMetazoa.
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..1208
FT                   /note="Period circadian protein"
FT                   /id="PRO_0000162615"
FT   DOMAIN          242..377
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          395..501
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REPEAT          698..699
FT                   /note="1"
FT   REPEAT          701..702
FT                   /note="2"
FT   REPEAT          703..704
FT                   /note="3"
FT   REPEAT          705..706
FT                   /note="4"
FT   REPEAT          707..708
FT                   /note="5"
FT   REPEAT          709..710
FT                   /note="6"
FT   REPEAT          711..712
FT                   /note="7"
FT   REPEAT          713..714
FT                   /note="8"
FT   REPEAT          715..716
FT                   /note="9"
FT   REPEAT          717..718
FT                   /note="10"
FT   REPEAT          719..720
FT                   /note="11"
FT   REPEAT          721..722
FT                   /note="12"
FT   REPEAT          723..724
FT                   /note="13"
FT   REPEAT          725..726
FT                   /note="14"
FT   REPEAT          727..728
FT                   /note="15"
FT   REPEAT          729..730
FT                   /note="16"
FT   REPEAT          731..732
FT                   /note="17"
FT   REPEAT          734..735
FT                   /note="18; approximate"
FT   REPEAT          737..738
FT                   /note="19"
FT   REPEAT          739..740
FT                   /note="20"
FT   REPEAT          741..742
FT                   /note="21; approximate"
FT   REGION          1..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..742
FT                   /note="21 X 2 AA approximate tandem repeats of G-[TN]"
FT   REGION          802..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          961..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1076..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           66..79
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        742
FT                   /note="S -> T (in Ref. 2; AAB25029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        751
FT                   /note="S -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        762
FT                   /note="A -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1208 AA;  126820 MW;  EE54A35E473B8483 CRC64;
     MEGGESAEST HNTKVSDSAY SNSCSNSQSQ RSGSSKSRLS GSHSSGSSGY GGKPSTQASS
     SDMIIKRNKD KSRKKKKNKG AGQGAGQAGQ SLISASTSLE GGAEEKPRPS GSGCGVEQQS
     CRELLQDQQH GEDHSEPKAT EQLQQEEGDR SGSESEAERV ENAAKSEAAQ SFPIPSPLSV
     TIVPPSMGGC AGVGHAASLD SGLAKLDKTW EAGGPGKVEP VPGVPGTAAA GTGQRGERLK
     EESFCCVISM HDGIVLYTTP SITDVLGYPR DMWLGRSFID FVHLKDRATF ASQITTGIPI
     AESRGSVPKD TKSTFCVMLR RYRGLKSGGF GVIGRPVSYE PFRLGLTFRE APEEARPDNY
     MVSNGTNMLL VICATPIKSS YKIPDEILSQ KSPKFAIRHT ATGIISHVDS AAVSALGYLP
     QDLIGRSIMD FYHQEDLSVM KETYEMVMKK GQTAGASFCS KPYRFLIQNG CYVLLETEWT
     SFVNPWSRKL EFVVGHHRVF QGPKSCNVFE AAPTCKLKMS EEAQSRNTRI KEDIVKRLAE
     TVSRPSDTVK QEVSRRCQAL ASFMETLMDE VSRADLKLEL PHENELTVSE RDSVMLGEIS
     PHHDYYDSKS STETPPSYNQ LNYNENLLRF FNSKPVTAPA ELDPPKTEPP EPRGTCVSGA
     SGPMSPVHEG SGGSGSSGNF TTASNIHMSS VTNTSIAGTG GTGTGTGTGT GTGTGTGTGT
     GTGTGTGTGT GNGTNSGTGT GSASSNYRGG SVAIQPVTLT EALLNKHNDE MEKFMLKKHR
     ESRGRSGEKS KKSATDTLKM LEYSGPGHGI KRGGSHSWEG EANKPKQQLT LGTDAIKGVV
     GGSGGVVGTG GGAGVAGGGG TGTGLAGTSD GRLTMSSGAG GVVGGPGGAA AAAGVISSVG
     SSMPGPSSYP TCTQNINLWP PFSVGITPPV HSTHTAMAQS SFSSAGLFPT FYYIPASLTP
     TSPTRSPRMH KHPHKGGPEM PTTSQQAAAA AAQAAQAMPL QYMAGVMYPH PSLFYTHPAA
     AAATAMMYQP MPFTGMTNAL QIPERPLGSQ SAYNKSMYTT TPPSMAKKVP GAFHSVTTPS
     QVQRSSSQSA SVNAEPGCSA SVSDPCKKEA PGSSPIPSVM GDYNSELPCS SSNPANNKKY
     TDSNGNSDDM DGSSFSSFYS SFIKTTDGSE SPPDIEKDPK HRKLKSMSPS DSKIMEHPEE
     DQTQHGDG
 
 
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