Q94BT6 (ADO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adagio protein 1

Alternative name(s):
Clock-associated PAS protein ZTL
F-box only protein 2b
Short name=FBX2b
Flavin-binding kelch repeat F-box protein 1-like protein 2
Short name=FKF1-like protein 2
LOV kelch protein 1
Protein ZEITLUPE

Gene names

Name:	ADO1
Synonyms:	FKL2, LKP1, ZTL
Ordered Locus Names:	At5g57360
ORF Names:	MSF19.2

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1. Ref.1 Ref.2 Ref.3 Ref.4 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with NFXL2. Interacts (via N-terminus) with GI and (via Kelch repeats) with ADO3. Component of an E3 ubiquitin ligase SCF(ADO1) complex composed of SKP1A/ASK1 (or SKP1B/ASK2), CUL1, RBX1 and ADO1. Also interacts with SKP1D/ASK4, SKP1K/ASK11, CRY1, PHYB, APRR1 and APRR5, and probably with SKP1N/ASK14 and SKP1S/ASK19. Ref.4 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Nucleus. Cytoplasm. Note: Nuclear after 9 hours of illumination (afternoon of long days). Cytoplasmic when plant have been subsequently grown 16 hours in light and 5 hours in dark (early morning of long days). Ref.3 Ref.15 Ref.16
Tissue specificity	Ubiquitously expressed with higher levels in cotyledons and leaves. Ref.2 Ref.3
Developmental stage	Mainly present during the light phase, and degraded in a proteasome-dependent manner in dark (at protein level).
Induction	Not regulated at the transcript level, but circadian-regulation at the protein level with a peak at the end of the subjective day. Ref.1 Ref.3 Ref.10 Ref.15 Ref.17
Post-translational modification	May be ubiquitinated. Degraded in a proteasome-dependent manner. FMN binds covalently to cysteine after exposure to blue light and is reversed in the dark By similarity.
Disruption phenotype	Accumulation of ADO3 protein during the morning period and early flowering time. Ref.16
Miscellaneous	'Zeitlupe' means slow motion in German. 'Adagio' means slowly in Italian.
Sequence similarities	Belongs to the ADAGIO family. Contains 1 F-box domain. Contains 5 Kelch repeats. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 1 PAS (PER-ARNT-SIM) domain.
Sequence caution	The sequence AAK64006.1 differs from that shown. Reason: Frameshift at positions 462 and 467.

Ontologies

Keywords
Biological process	Biological rhythms Flowering Sensory transduction Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Kelch repeat Repeat
Ligand	Chromophore FMN Flavoprotein
Molecular function	Photoreceptor protein Receptor
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	flower development Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APRR1	Q9LKL2	6	EBI-300691,EBI-618423
ASK11	O49484	3	EBI-300691,EBI-401185
CRY1	Q43125	2	EBI-300691,EBI-300703
GI	Q9SQI2	5	EBI-300691,EBI-446380
PHYB	P14713	2	EBI-300691,EBI-300727
SKP1A	Q39255	9	EBI-300691,EBI-532357
SKP1B	Q9FHW7	5	EBI-300691,EBI-604076

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q94BT6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 609	609	Adagio protein 1		PRO_0000119956
Regions
	Domain	32 – 114	83	PAS
	Domain	118 – 161	44	PAC
	Domain	195 – 241	47	F-box
	Repeat	292 – 342	51	Kelch 1
	Repeat	345 – 392	48	Kelch 2
	Repeat	397 – 445	49	Kelch 3
	Repeat	450 – 501	52	Kelch 4
	Repeat	516 – 564	49	Kelch 5
Amino acid modifications
	Modified residue	82	1	S-4a-FMN cysteine By similarity
Experimental info
	Mutagenesis	46	1	G → E: Loss of binding to GI. Ref.15
	Mutagenesis	82	1	C → A: Loss of binding to GI, but no effect on FNM binding. Ref.15
	Mutagenesis	119	1	G → D in ztl-21; long-period phenotype, decreased interaction with SKP1A/ASK1 and loss of binding to GI, NFXL2 and APRR1/TOC1, but no effect on binding to PHYB. Ref.14 Ref.15
	Mutagenesis	200	1	L → A: No SCF(ADO1) complex formation and reduced cyclic degradation of ADO1, but no effect on binding to GI; when associated with A-213. Ref.13 Ref.15
	Mutagenesis	203	1	E → K in ztl-22; long-period phenotype and loss of binding to NFXL2, but no effect on binding to GI or PHYB. Ref.14 Ref.15
	Mutagenesis	213	1	L → A: No SCF(ADO1) complex formation and reduced cyclic degradation of ADO1, but no effect on binding to GI; when associated with A-200. Ref.13 Ref.15
	Mutagenesis	287	1	G → D in ztl-23; long-period phenotype, but no effect on binding to PHYB. Ref.14
	Mutagenesis	317	1	P → S in ztl-24; long-period phenotype, but no effect on binding to PHYB. Ref.14
	Mutagenesis	320	1	D → N in ztl-2; affects circadian clock by lengthening the free-running period of clock-controlled processes. Ref.1 Ref.14
	Mutagenesis	347	1	G → S in ztl-25; long-period phenotype, but no effect on binding to PHYB. Ref.14
	Mutagenesis	372	1	D → N in ztl-26; long-period phenotype, but no effect on binding to PHYB. Ref.14
	Mutagenesis	425	1	D → N in ztl-1; affects circadian clock by lengthening the free-running period of clock-controlled processes, but has no effect on binding to GI or NFXL2. Ref.1 Ref.14 Ref.15
	Mutagenesis	452	1	G → D in ztl-27; long-period phenotype and loss of binding to APRR1/TOC1, but no effect on binding to GI or PHYB. Ref.14 Ref.15
	Mutagenesis	564	1	G → R in ztl-30; long-period phenotype, but no effect on binding to PHYB. Ref.14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 8, 2005. Version 2. Checksum: B25192FCBE019093	FASTA	609	65,906
	10 20 30 40 50 60 MEWDSGSDLS ADDASSLADD EEGGLFPGGG PIPYPVGNLL HTAPCGFVVT DAVEPDQPII 70 80 90 100 110 120 YVNTVFEMVT GYRAEEVLGG NCRFLQCRGP FAKRRHPLVD SMVVSEIRKC IDEGIEFQGE 130 140 150 160 170 180 LLNFRKDGSP LMNRLRLTPI YGDDDTITHI IGIQFFIETD IDLGPVLGSS TKEKSIDGIY 190 200 210 220 230 240 SALAAGERNV SRGMCGLFQL SDEVVSMKIL SRLTPRDVAS VSSVCRRLYV LTKNEDLWRR 250 260 270 280 290 300 VCQNAWGSET TRVLETVPGA KRLGWGRLAR ELTTLEAAAW RKLSVGGSVE PSRCNFSACA 310 320 330 340 350 360 VGNRVVLFGG EGVNMQPMND TFVLDLNSDY PEWQHVKVSS PPPGRWGHTL TCVNGSNLVV 370 380 390 400 410 420 FGGCGQQGLL NDVFVLNLDA KPPTWREISG LAPPLPRSWH SSCTLDGTKL IVSGGCADSG 430 440 450 460 470 480 VLLSDTFLLD LSIEKPVWRE IPAAWTPPSR LGHTLSVYGG RKILMFGGLA KSGPLKFRSS 490 500 510 520 530 540 DVFTMDLSEE EPCWRCVTGS GMPGAGNPGG VAPPPRLDHV AVNLPGGRIL IFGGSVAGLH 550 560 570 580 590 600 SASQLYLLDP TEDKPTWRIL NIPGRPPRFA WGHGTCVVGG TRAIVLGGQT GEEWMLSELH ELSLASYLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ZEITLUPE encodes a novel clock-associated PAS protein from Arabidopsis." Somers D.E., Schultz T.F., Milnamow M., Kay S.A. Cell 101:319-329(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, MUTAGENESIS OF ASP-320 AND ASP-425.
[2]	"FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis." Nelson D.C., Lasswell J.E., Rogg L.E., Cohen M.A., Bartel B. Cell 101:331-340(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]	"LKP1 (LOV kelch protein 1): a factor involved in the regulation of flowering time in Arabidopsis." Kiyosue T., Wada M. Plant J. 23:807-815(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
[4]	"An Arabidopsis circadian clock component interacts with both CRY1 and phyB." Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R., Cashmore A.R. Nature 410:487-490(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CRY1 AND PHYB.
[5]	"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones." Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S. DNA Res. 5:379-391(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[7]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[8]	"F-box proteins in Arabidopsis." Xiao W., Jang J.-C. Trends Plant Sci. 5:454-457(2000) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis." Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J., Hellmann H., Estelle M., Somers D.E., Crosby W.L. Plant J. 34:753-767(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SKP1A; SKP1B; SKP1D; SKP1K AND SKP1S.
[10]	"Circadian phase-specific degradation of the F-box protein ZTL is mediated by the proteasome." Kim W.-Y., Geng R., Somers D.E. Proc. Natl. Acad. Sci. U.S.A. 100:4933-4938(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[11]	"Identification of ASK and clock-associated proteins as molecular partners of LKP2 (LOV kelch protein 2) in Arabidopsis." Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N., Komatsu A., Seki M., Shinozaki K., Kiyosue T. J. Exp. Bot. 55:2015-2027(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SKP1A; SKP1B; SKP1D; SKP1K; SKP1N; ADO2; APRR1 AND APRR5.
[12]	"The F-box protein ZEITLUPE confers dosage-dependent control on the circadian clock, photomorphogenesis, and flowering time." Somers D.E., Kim W.-Y., Geng R. Plant Cell 16:769-782(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Formation of an SCF(ZTL) complex is required for proper regulation of circadian timing." Han L., Mason M., Risseeuw E.P., Crosby W.L., Somers D.E. Plant J. 40:291-301(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LEU-200 AND LEU-213, IDENTIFICATION IN A SCF(ADO1) COMPLEX.
[14]	"Forward genetic analysis of the circadian clock separates the multiple functions of ZEITLUPE." Kevei E., Gyula P., Hall A., Kozma-Bognar L., Kim W.Y., Eriksson M.E., Toth R., Hanano S., Feher B., Southern M.M., Bastow R.M., Viczian A., Hibberd V., Davis S.J., Somers D.E., Nagy F., Millar A.J. Plant Physiol. 140:933-945(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-119; GLU-203; GLY-287; PRO-317; ASP-320; GLY-347; ASP-372; ASP-425; GLY-452 AND GLY-564, INTERACTION WITH SKP1A; APRR1 AND PHYB.
[15]	"ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light." Kim W.Y., Fujiwara S., Suh S.S., Kim J., Kim Y., Han L., David K., Putterill J., Nam H.G., Somers D.E. Nature 449:356-360(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-46; CYS-82; GLY-119; LEU-200; GLU-203; LEU-213; ASP-425 AND GLY-452, INTERACTION WITH GI AND APRR1, INDUCTION, SUBCELLULAR LOCATION.
[16]	"LOV KELCH PROTEIN2 and ZEITLUPE repress Arabidopsis photoperiodic flowering under non-inductive conditions, dependent on FLAVIN-BINDING KELCH REPEAT F-BOX1." Takase T., Nishiyama Y., Tanihigashi H., Ogura Y., Miyazaki Y., Yamada Y., Kiyosue T. Plant J. 67:608-621(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ADO3, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[17]	"Partners in time: EARLY BIRD associates with ZEITLUPE and regulates the speed of the Arabidopsis clock." Johansson M., McWatters H.G., Bako L., Takata N., Gyula P., Hall A., Somers D.E., Millar A.J., Eriksson M.E. Plant Physiol. 155:2108-2122(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFXL2, INDUCTION.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF254413 mRNA. Translation: AAF70288.1. AF216525 mRNA. Translation: AAF32300.1. AB038796 mRNA. Translation: BAB18914.1. AF252294 mRNA. Translation: AAK27433.1. AB016891 Genomic DNA. Translation: BAB08473.1. CP002688 Genomic DNA. Translation: AED96891.1. AY039902 mRNA. Translation: AAK64006.1. Frameshift. BT008772 mRNA. Translation: AAP68211.1.
IPI	IPI00532449.
RefSeq	NP_568855.1. NM_125119.3.
UniGene	At.21022.
3D structure databases
ProteinModelPortal	Q94BT6.
SMR	Q94BT6. Positions 47-154.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94BT6. 22 interactions.
MINT	MINT-192373.
STRING	3702.AT5G57360.2-P.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G57360.1; AT5G57360.1; AT5G57360.
GeneID	835842.
KEGG	ath:AT5G57360.
Organism-specific databases
GeneFarm	5106. 485.
TAIR	At5g57360.
Phylogenomic databases
eggNOG	COG2202.
HOGENOM	HOG000238789.
InParanoid	Q94BT6.
KO	K12115.
PhylomeDB	Q94BT6.
ProtClustDB	CLSN2689078.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q94BT6.
Genevestigator	Q94BT6.
GermOnline	AT5G57360. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.120.10.80. 2 hits.
InterPro	IPR001810. F-box_dom_cyclin-like. IPR015915. Kelch-typ_b-propeller. IPR011498. Kelch_2. IPR001610. PAC. IPR000014. PAS. [Graphical view]
Pfam	PF07646. Kelch_2. 1 hit. [Graphical view]
SMART	SM00256. FBOX. 1 hit. SM00086. PAC. 1 hit. SM00091. PAS. 1 hit. [Graphical view]
SUPFAM	SSF81383. F-box_dom_Skp2-like. 1 hit.
TIGRFAMs	TIGR00229. sensory_box. 1 hit.
PROSITE	PS50181. FBOX. 1 hit. PS50113. PAC. False negative. PS50112. PAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADO1_ARATH

Accession

Primary (citable) accession number: Q94BT6
Secondary accession number(s): Q9LDF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program