ADO1_ARATH
ID ADO1_ARATH Reviewed; 609 AA.
AC Q94BT6; Q9LDF6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Adagio protein 1;
DE AltName: Full=Clock-associated PAS protein ZTL;
DE AltName: Full=F-box only protein 2b;
DE Short=FBX2b;
DE AltName: Full=Flavin-binding kelch repeat F-box protein 1-like protein 2;
DE Short=FKF1-like protein 2;
DE AltName: Full=LOV kelch protein 1;
DE AltName: Full=Protein ZEITLUPE;
GN Name=ADO1; Synonyms=FKL2, LKP1, ZTL; OrderedLocusNames=At5g57360;
GN ORFNames=MSF19.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND MUTAGENESIS OF ASP-320
RP AND ASP-425.
RX PubMed=10847686; DOI=10.1016/s0092-8674(00)80841-7;
RA Somers D.E., Schultz T.F., Milnamow M., Kay S.A.;
RT "ZEITLUPE encodes a novel clock-associated PAS protein from Arabidopsis.";
RL Cell 101:319-329(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10847687; DOI=10.1016/s0092-8674(00)80842-9;
RA Nelson D.C., Lasswell J.E., Rogg L.E., Cohen M.A., Bartel B.;
RT "FKF1, a clock-controlled gene that regulates the transition to flowering
RT in Arabidopsis.";
RL Cell 101:331-340(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=10998191; DOI=10.1046/j.1365-313x.2000.00850.x;
RA Kiyosue T., Wada M.;
RT "LKP1 (LOV kelch protein 1): a factor involved in the regulation of
RT flowering time in Arabidopsis.";
RL Plant J. 23:807-815(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CRY1 AND PHYB.
RX PubMed=11260718; DOI=10.1038/35068589;
RA Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R.,
RA Cashmore A.R.;
RT "An Arabidopsis circadian clock component interacts with both CRY1 and
RT phyB.";
RL Nature 410:487-490(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11077244; DOI=10.1016/s1360-1385(00)01769-6;
RA Xiao W., Jang J.-C.;
RT "F-box proteins in Arabidopsis.";
RL Trends Plant Sci. 5:454-457(2000).
RN [9]
RP INTERACTION WITH SKP1A; SKP1B; SKP1D; SKP1K AND SKP1S.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
RN [10]
RP INDUCTION.
RX PubMed=12665620; DOI=10.1073/pnas.0736949100;
RA Kim W.-Y., Geng R., Somers D.E.;
RT "Circadian phase-specific degradation of the F-box protein ZTL is mediated
RT by the proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4933-4938(2003).
RN [11]
RP INTERACTION WITH SKP1A; SKP1B; SKP1D; SKP1K; SKP1N; ADO2; APRR1 AND APRR5.
RX PubMed=15310821; DOI=10.1093/jxb/erh226;
RA Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N.,
RA Komatsu A., Seki M., Shinozaki K., Kiyosue T.;
RT "Identification of ASK and clock-associated proteins as molecular partners
RT of LKP2 (LOV kelch protein 2) in Arabidopsis.";
RL J. Exp. Bot. 55:2015-2027(2004).
RN [12]
RP FUNCTION.
RX PubMed=14973171; DOI=10.1105/tpc.016808;
RA Somers D.E., Kim W.-Y., Geng R.;
RT "The F-box protein ZEITLUPE confers dosage-dependent control on the
RT circadian clock, photomorphogenesis, and flowering time.";
RL Plant Cell 16:769-782(2004).
RN [13]
RP FUNCTION, MUTAGENESIS OF LEU-200 AND LEU-213, AND IDENTIFICATION IN A
RP SCF(ADO1) COMPLEX.
RX PubMed=15447654; DOI=10.1111/j.1365-313x.2004.02207.x;
RA Han L., Mason M., Risseeuw E.P., Crosby W.L., Somers D.E.;
RT "Formation of an SCF(ZTL) complex is required for proper regulation of
RT circadian timing.";
RL Plant J. 40:291-301(2004).
RN [14]
RP FUNCTION, MUTAGENESIS OF GLY-119; GLU-203; GLY-287; PRO-317; ASP-320;
RP GLY-347; ASP-372; ASP-425; GLY-452 AND GLY-564, AND INTERACTION WITH SKP1A;
RP APRR1 AND PHYB.
RX PubMed=16428597; DOI=10.1104/pp.105.074864;
RA Kevei E., Gyula P., Hall A., Kozma-Bognar L., Kim W.Y., Eriksson M.E.,
RA Toth R., Hanano S., Feher B., Southern M.M., Bastow R.M., Viczian A.,
RA Hibberd V., Davis S.J., Somers D.E., Nagy F., Millar A.J.;
RT "Forward genetic analysis of the circadian clock separates the multiple
RT functions of ZEITLUPE.";
RL Plant Physiol. 140:933-945(2006).
RN [15]
RP FUNCTION, MUTAGENESIS OF GLY-46; CYS-82; GLY-119; LEU-200; GLU-203;
RP LEU-213; ASP-425 AND GLY-452, INTERACTION WITH GI AND APRR1, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17704763; DOI=10.1038/nature06132;
RA Kim W.Y., Fujiwara S., Suh S.S., Kim J., Kim Y., Han L., David K.,
RA Putterill J., Nam H.G., Somers D.E.;
RT "ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue
RT light.";
RL Nature 449:356-360(2007).
RN [16]
RP INTERACTION WITH APRR5.
RX PubMed=18562312; DOI=10.1074/jbc.m803471200;
RA Fujiwara S., Wang L., Han L., Suh S.-S., Salome P.A., McClung C.R.,
RA Somers D.E.;
RT "Post-translational regulation of the Arabidopsis circadian clock through
RT selective proteolysis and phosphorylation of pseudo-response regulator
RT proteins.";
RL J. Biol. Chem. 283:23073-23083(2008).
RN [17]
RP FUNCTION, INTERACTION WITH ADO3, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21518052; DOI=10.1111/j.1365-313x.2011.04618.x;
RA Takase T., Nishiyama Y., Tanihigashi H., Ogura Y., Miyazaki Y., Yamada Y.,
RA Kiyosue T.;
RT "LOV KELCH PROTEIN2 and ZEITLUPE repress Arabidopsis photoperiodic
RT flowering under non-inductive conditions, dependent on FLAVIN-BINDING KELCH
RT REPEAT F-BOX1.";
RL Plant J. 67:608-621(2011).
RN [18]
RP INTERACTION WITH NFXL2, AND INDUCTION.
RX PubMed=21300918; DOI=10.1104/pp.110.167155;
RA Johansson M., McWatters H.G., Bako L., Takata N., Gyula P., Hall A.,
RA Somers D.E., Millar A.J., Eriksson M.E.;
RT "Partners in time: EARLY BIRD associates with ZEITLUPE and regulates the
RT speed of the Arabidopsis clock.";
RL Plant Physiol. 155:2108-2122(2011).
CC -!- FUNCTION: Component of an E3 ubiquitin ligase complex that plays a
CC central role in blue light-dependent circadian cycles. Acts as a blue
CC light photoreceptor, due to the presence of FMN, that mediates light-
CC regulated protein degradation of critical clock components by targeting
CC them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase
CC complex is involved in the regulation of circadian clock-dependent
CC processes including the transition to flowering time, hypocotyl
CC elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5,
CC but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase
CC complex. Blue light enhances cooperative stabilization of 'GIGANTEA'
CC and ADO1/ZTL, leading to amplification and sharpening of the expression
CC profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the
CC interaction of ADO3 with CDF1. {ECO:0000269|PubMed:10847686,
CC ECO:0000269|PubMed:10847687, ECO:0000269|PubMed:10998191,
CC ECO:0000269|PubMed:11260718, ECO:0000269|PubMed:14973171,
CC ECO:0000269|PubMed:15447654, ECO:0000269|PubMed:16428597,
CC ECO:0000269|PubMed:17704763, ECO:0000269|PubMed:21518052}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with NFXL2. Interacts (via N-terminus) with GI and
CC (via Kelch repeats) with ADO3. Component of an E3 ubiquitin ligase
CC SCF(ADO1) complex composed of SKP1A/ASK1 (or SKP1B/ASK2), CUL1, RBX1
CC and ADO1. Also interacts with SKP1D/ASK4, SKP1K/ASK11, CRY1, PHYB,
CC APRR1 and APRR5, and probably with SKP1N/ASK14 and SKP1S/ASK19.
CC {ECO:0000269|PubMed:11260718, ECO:0000269|PubMed:12795696,
CC ECO:0000269|PubMed:15310821, ECO:0000269|PubMed:15447654,
CC ECO:0000269|PubMed:16428597, ECO:0000269|PubMed:17704763,
CC ECO:0000269|PubMed:18562312, ECO:0000269|PubMed:21300918,
CC ECO:0000269|PubMed:21518052}.
CC -!- INTERACTION:
CC Q94BT6; Q9LKL2: APRR1; NbExp=7; IntAct=EBI-300691, EBI-618423;
CC Q94BT6; O49484: ASK11; NbExp=3; IntAct=EBI-300691, EBI-401185;
CC Q94BT6; Q9SQI2: GI; NbExp=6; IntAct=EBI-300691, EBI-446380;
CC Q94BT6; Q39255: SKP1A; NbExp=9; IntAct=EBI-300691, EBI-532357;
CC Q94BT6; Q9FHW7: SKP1B; NbExp=5; IntAct=EBI-300691, EBI-604076;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear after 9 hours of
CC illumination (afternoon of long days). Cytoplasmic when plant have been
CC subsequently grown 16 hours in light and 5 hours in dark (early morning
CC of long days).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94BT6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
CC cotyledons and leaves. {ECO:0000269|PubMed:10847687,
CC ECO:0000269|PubMed:10998191}.
CC -!- DEVELOPMENTAL STAGE: Mainly present during the light phase, and
CC degraded in a proteasome-dependent manner in dark (at protein level).
CC -!- INDUCTION: Not regulated at the transcript level, but circadian-
CC regulation at the protein level with a peak at the end of the
CC subjective day. {ECO:0000269|PubMed:10847686,
CC ECO:0000269|PubMed:10998191, ECO:0000269|PubMed:12665620,
CC ECO:0000269|PubMed:17704763, ECO:0000269|PubMed:21300918}.
CC -!- PTM: May be ubiquitinated. Degraded in a proteasome-dependent manner.
CC -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC is reversed in the dark. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of ADO3 protein during the morning
CC period and early flowering time. {ECO:0000269|PubMed:21518052}.
CC -!- MISCELLANEOUS: 'Zeitlupe' means slow motion in German.
CC -!- MISCELLANEOUS: 'Adagio' means slowly in Italian.
CC -!- SIMILARITY: Belongs to the ADAGIO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK64006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF254413; AAF70288.1; -; mRNA.
DR EMBL; AF216525; AAF32300.1; -; mRNA.
DR EMBL; AB038796; BAB18914.1; -; mRNA.
DR EMBL; AF252294; AAK27433.1; -; mRNA.
DR EMBL; AB016891; BAB08473.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96891.1; -; Genomic_DNA.
DR EMBL; AY039902; AAK64006.1; ALT_FRAME; mRNA.
DR EMBL; BT008772; AAP68211.1; -; mRNA.
DR RefSeq; NP_568855.1; NM_125119.4. [Q94BT6-1]
DR PDB; 5SVG; X-ray; 2.50 A; A/B/C/D=29-165.
DR PDB; 5SVU; X-ray; 2.60 A; A/B/C/D=29-165.
DR PDB; 5SVV; X-ray; 2.10 A; A/B/C/D=29-165.
DR PDB; 5SVW; X-ray; 2.29 A; A/B/C/D=29-165.
DR PDB; 6WLE; X-ray; 3.00 A; A/B/C/D/E/F/G=1-190.
DR PDB; 6WLP; X-ray; 3.00 A; A/B/C/D/E/F/G=1-190.
DR PDBsum; 5SVG; -.
DR PDBsum; 5SVU; -.
DR PDBsum; 5SVV; -.
DR PDBsum; 5SVW; -.
DR PDBsum; 6WLE; -.
DR PDBsum; 6WLP; -.
DR AlphaFoldDB; Q94BT6; -.
DR SASBDB; Q94BT6; -.
DR SMR; Q94BT6; -.
DR BioGRID; 21086; 26.
DR DIP; DIP-32989N; -.
DR IntAct; Q94BT6; 20.
DR MINT; Q94BT6; -.
DR STRING; 3702.AT5G57360.2; -.
DR PaxDb; Q94BT6; -.
DR EnsemblPlants; AT5G57360.1; AT5G57360.1; AT5G57360. [Q94BT6-1]
DR GeneID; 835842; -.
DR Gramene; AT5G57360.1; AT5G57360.1; AT5G57360. [Q94BT6-1]
DR KEGG; ath:AT5G57360; -.
DR Araport; AT5G57360; -.
DR eggNOG; ENOG502QQR1; Eukaryota.
DR HOGENOM; CLU_033494_1_0_1; -.
DR InParanoid; Q94BT6; -.
DR OMA; VGDRNVC; -.
DR PhylomeDB; Q94BT6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94BT6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BT6; baseline and differential.
DR Genevisible; Q94BT6; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009637; P:response to blue light; IBA:GO_Central.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011498; Kelch_2.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Chromophore;
KW Cytoplasm; Flavoprotein; Flowering; FMN; Kelch repeat; Nucleus;
KW Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..609
FT /note="Adagio protein 1"
FT /id="PRO_0000119956"
FT DOMAIN 32..114
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 118..161
FT /note="PAC"
FT DOMAIN 195..241
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 292..342
FT /note="Kelch 1"
FT REPEAT 345..392
FT /note="Kelch 2"
FT REPEAT 397..445
FT /note="Kelch 3"
FT REPEAT 450..501
FT /note="Kelch 4"
FT REPEAT 516..564
FT /note="Kelch 5"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 46
FT /note="G->E: Loss of binding to GI."
FT /evidence="ECO:0000269|PubMed:17704763"
FT MUTAGEN 82
FT /note="C->A: Loss of binding to GI, but no effect on FNM
FT binding."
FT /evidence="ECO:0000269|PubMed:17704763"
FT MUTAGEN 119
FT /note="G->D: In ztl-21; long-period phenotype, decreased
FT interaction with SKP1A/ASK1 and loss of binding to GI,
FT NFXL2 and APRR1/TOC1, but no effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597,
FT ECO:0000269|PubMed:17704763"
FT MUTAGEN 200
FT /note="L->A: No SCF(ADO1) complex formation and reduced
FT cyclic degradation of ADO1, but no effect on binding to GI;
FT when associated with A-213."
FT /evidence="ECO:0000269|PubMed:15447654,
FT ECO:0000269|PubMed:17704763"
FT MUTAGEN 203
FT /note="E->K: In ztl-22; long-period phenotype and loss of
FT binding to NFXL2, but no effect on binding to GI or PHYB."
FT /evidence="ECO:0000269|PubMed:16428597,
FT ECO:0000269|PubMed:17704763"
FT MUTAGEN 213
FT /note="L->A: No SCF(ADO1) complex formation and reduced
FT cyclic degradation of ADO1, but no effect on binding to GI;
FT when associated with A-200."
FT /evidence="ECO:0000269|PubMed:15447654,
FT ECO:0000269|PubMed:17704763"
FT MUTAGEN 287
FT /note="G->D: In ztl-23; long-period phenotype, but no
FT effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597"
FT MUTAGEN 317
FT /note="P->S: In ztl-24; long-period phenotype, but no
FT effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597"
FT MUTAGEN 320
FT /note="D->N: In ztl-2; affects circadian clock by
FT lengthening the free-running period of clock-controlled
FT processes."
FT /evidence="ECO:0000269|PubMed:10847686,
FT ECO:0000269|PubMed:16428597"
FT MUTAGEN 347
FT /note="G->S: In ztl-25; long-period phenotype, but no
FT effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597"
FT MUTAGEN 372
FT /note="D->N: In ztl-26; long-period phenotype, but no
FT effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597"
FT MUTAGEN 425
FT /note="D->N: In ztl-1; affects circadian clock by
FT lengthening the free-running period of clock-controlled
FT processes, but has no effect on binding to GI or NFXL2."
FT /evidence="ECO:0000269|PubMed:10847686,
FT ECO:0000269|PubMed:16428597, ECO:0000269|PubMed:17704763"
FT MUTAGEN 452
FT /note="G->D: In ztl-27; long-period phenotype and loss of
FT binding to APRR1/TOC1, but no effect on binding to GI or
FT PHYB."
FT /evidence="ECO:0000269|PubMed:16428597,
FT ECO:0000269|PubMed:17704763"
FT MUTAGEN 564
FT /note="G->R: In ztl-30; long-period phenotype, but no
FT effect on binding to PHYB."
FT /evidence="ECO:0000269|PubMed:16428597"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:5SVU"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:5SVW"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5SVV"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:5SVV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5SVV"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5SVV"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5SVV"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5SVV"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:5SVV"
SQ SEQUENCE 609 AA; 65906 MW; B25192FCBE019093 CRC64;
MEWDSGSDLS ADDASSLADD EEGGLFPGGG PIPYPVGNLL HTAPCGFVVT DAVEPDQPII
YVNTVFEMVT GYRAEEVLGG NCRFLQCRGP FAKRRHPLVD SMVVSEIRKC IDEGIEFQGE
LLNFRKDGSP LMNRLRLTPI YGDDDTITHI IGIQFFIETD IDLGPVLGSS TKEKSIDGIY
SALAAGERNV SRGMCGLFQL SDEVVSMKIL SRLTPRDVAS VSSVCRRLYV LTKNEDLWRR
VCQNAWGSET TRVLETVPGA KRLGWGRLAR ELTTLEAAAW RKLSVGGSVE PSRCNFSACA
VGNRVVLFGG EGVNMQPMND TFVLDLNSDY PEWQHVKVSS PPPGRWGHTL TCVNGSNLVV
FGGCGQQGLL NDVFVLNLDA KPPTWREISG LAPPLPRSWH SSCTLDGTKL IVSGGCADSG
VLLSDTFLLD LSIEKPVWRE IPAAWTPPSR LGHTLSVYGG RKILMFGGLA KSGPLKFRSS
DVFTMDLSEE EPCWRCVTGS GMPGAGNPGG VAPPPRLDHV AVNLPGGRIL IFGGSVAGLH
SASQLYLLDP TEDKPTWRIL NIPGRPPRFA WGHGTCVVGG TRAIVLGGQT GEEWMLSELH
ELSLASYLT
