FRQ_NEUCR
ID FRQ_NEUCR Reviewed; 989 AA.
AC P19970; Q01276; Q7RVB1; V5IKG2; V5IL36;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Frequency clock protein;
GN Name=frq; ORFNames=B13D24.170, NCU02265;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLU-364; GLY-459; GLY-482
RP AND ALA-895.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8052643; DOI=10.1073/pnas.91.16.7683;
RA Aronson B.D., Johnson K.A., Dunlap J.C.;
RT "Circadian clock locus frequency: protein encoded by a single open reading
RT frame defines period length and temperature compensation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7683-7687(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-989.
RX PubMed=2525233; DOI=10.1038/339558a0;
RA McClung C.R., Fox B.A., Dunlap J.C.;
RT "The Neurospora clock gene frequency shares a sequence element with the
RT Drosophila clock gene period.";
RL Nature 339:558-562(1989).
RN [5]
RP PHOSPHORYLATION AT THR-501; SER-513 AND SER-519, AND MUTAGENESIS OF
RP 501-THR--SER-503; 513-SER-THR-514 AND SER-519.
RX PubMed=10618401; DOI=10.1073/pnas.97.1.234;
RA Liu Y., Loros J., Dunlap J.C.;
RT "Phosphorylation of the Neurospora clock protein frequency determines its
RT degradation rate and strongly influences the period length of the circadian
RT clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:234-239(2000).
RN [6]
RP PHOSPHORYLATION BY CK2.
RX PubMed=11959847; DOI=10.1101/gad.965102;
RA Yang Y., Cheng P., Liu Y.;
RT "Regulation of the Neurospora circadian clock by casein kinase II.";
RL Genes Dev. 16:994-1006(2002).
CC -!- FUNCTION: Circadian clock component involved in the generation of
CC biological rhythms, in particular in rhythm stability, period length,
CC and temperature compensation. Oscillates in abundance with a daily peak
CC early in the morning. Behaves as a negative element in circadian
CC transcriptional loop. May bind to wc-2 protein. The complex frq-wc-2
CC may turn off the expression of frq.
CC -!- INTERACTION:
CC P19970; Q873J5: B9B11.040; Xeno; NbExp=2; IntAct=EBI-6995022, EBI-15874858;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P19970-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P19970-2; Sequence=VSP_018781;
CC -!- INDUCTION: By light; perhaps through white collar-1 (wc-1) and white
CC collar-2 (wc-2). Also activated directly by wc-1 and wc-2.
CC -!- PTM: Progressive phosphorylation during the late circadian day and
CC early night. Phosphorylation is also involved in regulating frq
CC degradation. Phosphorylation by CKII may have at least three functions;
CC it decreases the stability of frq, reduces the protein complex
CC formation between frq and the white collar proteins, and is important
CC for the closing of the Neurospora circadian negative feedback loop.
CC {ECO:0000269|PubMed:10618401, ECO:0000269|PubMed:11959847}.
CC -!- MISCELLANEOUS: [Isoform Long]: Maintains rhythms at high temperature
CC (30 degrees Celsius).
CC -!- MISCELLANEOUS: [Isoform Short]: Maintains rhythms at lower temperature
CC (18 degrees Celsius). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FRQ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.4; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U17073; AAA57121.1; -; mRNA.
DR EMBL; BX908789; CAF05882.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA42013.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA42014.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA42015.1; -; Genomic_DNA.
DR PIR; T46659; T46659.
DR RefSeq; XP_011395124.1; XM_011396822.1. [P19970-2]
DR RefSeq; XP_011395125.1; XM_011396823.1. [P19970-1]
DR RefSeq; XP_011395126.1; XM_011396824.1. [P19970-1]
DR AlphaFoldDB; P19970; -.
DR DIP; DIP-41987N; -.
DR IntAct; P19970; 2.
DR MINT; P19970; -.
DR STRING; 5141.EFNCRP00000003120; -.
DR iPTMnet; P19970; -.
DR PRIDE; P19970; -.
DR EnsemblFungi; ESA42013; ESA42013; NCU02265. [P19970-1]
DR EnsemblFungi; ESA42014; ESA42014; NCU02265. [P19970-1]
DR EnsemblFungi; ESA42015; ESA42015; NCU02265. [P19970-2]
DR GeneID; 3876095; -.
DR KEGG; ncr:NCU02265; -.
DR VEuPathDB; FungiDB:NCU02265; -.
DR HOGENOM; CLU_007103_1_0_1; -.
DR InParanoid; P19970; -.
DR OMA; PYYLPSE; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR018554; FRQ.
DR Pfam; PF09421; FRQ; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Biological rhythms; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..989
FT /note="Frequency clock protein"
FT /id="PRO_0000021288"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 564..568
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..885
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10618401"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10618401"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10618401"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018781"
FT MUTAGEN 364
FT /note="E->K: In FRQ3; lengthened period."
FT /evidence="ECO:0000269|PubMed:8052643"
FT MUTAGEN 459
FT /note="G->D: In FRQ7; lengthened period."
FT /evidence="ECO:0000269|PubMed:8052643"
FT MUTAGEN 482
FT /note="G->S: In FRQ1; shortened period."
FT /evidence="ECO:0000269|PubMed:8052643"
FT MUTAGEN 501..503
FT /note="TPS->APG: In FRQ10; no effect."
FT /evidence="ECO:0000269|PubMed:10618401"
FT MUTAGEN 513..514
FT /note="ST->RA: In FRQ10; strong reduction in the
FT degradation rate; lengthened period."
FT /evidence="ECO:0000269|PubMed:10618401"
FT MUTAGEN 513
FT /note="S->D: In FRQ10; reduces phosphorylation; slight
FT reduction in the degradation rate; loss of rhythmicity."
FT MUTAGEN 513
FT /note="S->I: In FRQ10; reduces phosphorylation; strong
FT reduction in the degradation rate; lengthened period."
FT MUTAGEN 519
FT /note="S->A: In FRQ10; no effect."
FT /evidence="ECO:0000269|PubMed:10618401"
FT MUTAGEN 663..989
FT /note="Missing: In FRQ9; loss of rhythmicity."
FT MUTAGEN 895
FT /note="A->T: In FRQ2; shortened period."
FT /evidence="ECO:0000269|PubMed:8052643"
FT CONFLICT 146
FT /note="S -> T (in Ref. 1; AAA57121)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..207
FT /note="EATLRD -> MGGNRP (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="D -> H (in Ref. 1; AAA57121)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="H -> Y (in Ref. 1; AAA57121)"
FT /evidence="ECO:0000305"
FT CONFLICT 962..963
FT /note="ML -> IV (in Ref. 1; AAA57121 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 989 AA; 108200 MW; EC4E984FAD39F095 CRC64;
MADSGDKSQG MRPPPFDSRG HPLPRRASPD KSITLENHRL ARDTSSRVTS SSALGVTESQ
PQLKSSPTRR NSSGESEPTN WFNQSNRNPA AAFHDESHIM EVDPPFYQKE TDSSNEESRY
PPGRNPVHPP GGVQLPGFRP VAAHSSAADD YRSVIDDLTV ENKRLKEELK RYKQFGSDVM
RKEKLFEIKV HGLPRRKKRE LEATLRDFAA SLGDSSESTS QRRKTGRHGT AVHSSGVSLS
KHDSSSSSRS RPVDSAYNSM STGRSSHAPH SSGPSLGRPS LTRAKSVGTQ KVENYLRDTP
DGLLPHHIVM TDKEKKKLVV RRLEQLFTGK ISGRNMQRNQ SMPSMDAPLA PEGTNMAPPR
PPPEGLREAC IQLQDGDNPR KNRSSKDNGS ASNSGGDQTE LGGTGTGSGD GSGSGGRTGN
NTSPPGAIAP DQRPTRPRDL DPDRVQIPSE NMDYIRHLGL VSPEFLQGSR TSYQDVAPDA
EGWVYLNLLC NLAQLHMVNV TPSFIRQAVS EKSTKFQLSA DGRKIRWRGG TDGTKFSSDS
SEDKSQQSPM TEDTEDGSDK NGRRKKRKTQ QASSEIGRFG PSRSPSDTFH YKPMFVHRNS
SSIETSLEES MSQGSEDAVD ESNMGNSKWD FSGSGTTQQR RKRRYDGAIV YYTGAPFCTD
LSGDPGDMSP TAQMTAGREV EGSGSGDEVE HVLQRTLSGS SLPIRPLSDD RARVAEVLDF
DPGNPPELVA DDGSSPNDED FVFPWCEDPA KVRIQPIAKE VMEPSGLGGV LPDDHFVMLV
TTRRVVRPIL QRQLSRSTTS EDTAEFIAER LAAIRTSSPL PPRSHRLTVA PLQVEYVSGQ
FRRLNPAPLP PPAIFYPPFS TDSSWDDGDD LASDDEEVEE VEEDSYSEGQ ISRRANPHFS
DNNTYMRKDD LAFDTETDVR MDSDDNRLSD SGHNMRAMMP RAEAVDGDDS PLAAVTGKEV
DMLHTGSSVA TAGGAESGYS SSMEDVSSS
