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 24-JAN-2024, entry version 168. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q94BT6; -. DR PaxDb; 3702-AT5G57360-2; -. 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 TAIR; AT5G57360; ZTL. DR eggNOG; ENOG502QQR1; Eukaryota. DR HOGENOM; CLU_033494_1_0_1; -. DR InParanoid; Q94BT6; -. DR OMA; ANPPTWR; -. DR PhylomeDB; Q94BT6; -. DR UniPathway; UPA00143; -. DR PRO; PR:Q94BT6; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q94BT6; baseline and differential. 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; cd22154; F-box_AtADO-like; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 1.20.1280.50; -; 1. DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2. DR Gene3D; 3.30.450.20; PAS domain; 1. 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 NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR46175:SF5; ADAGIO PROTEIN 1; 1. DR PANTHER; PTHR46175; BACTERIOOPSIN TRANSCRIPTIONAL ACTIVATOR; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF07646; Kelch_2; 2. DR Pfam; PF13415; Kelch_3; 1. DR Pfam; PF13418; Kelch_4; 1. DR Pfam; PF13426; PAS_9; 1. DR SMART; SM00256; FBOX; 1. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1. DR SUPFAM; SSF117281; Kelch motif; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50181; FBOX; 1. DR PROSITE; PS50112; PAS; 1. DR Genevisible; Q94BT6; AT. 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 //