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UniProtKB/Swiss-Prot entry Q9C9W9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADO3_ARATH
Primary accession number Q9C9W9
Secondary accession number Q9M648
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name Adagio protein 3
Synonyms Flavin-binding kelch repeat F-box protein 1
F-box only protein 2a
FBX2a
Gene name
Name: ADO3
Synonyms: FKF1
OrderedLocusNames: At1g68050
ORFNames: T23K23.10
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Landsberg erecta;
DOI=10.1016/S0092-8674(00)80842-9; PubMed=10847687 [NCBI, ExPASy, EBI, Israel, Japan]
Nelson D.C., Lasswell J.E., Rogg L.E., Cohen M.A., Bartel B.;
"FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis.";
Cell 101:331-340(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/35068589; PubMed=11260718 [NCBI, ExPASy, EBI, Israel, Japan]
Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R., Cashmore A.R.;
"An Arabidopsis circadian clock component interacts with both CRY1 and phyB.";
Nature 410:487-490(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
DOI=10.1016/S1360-1385(00)01769-6; PubMed=11077244 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
[6]
FUNCTION, INDUCTION, FMN-BINDING AT CYS-91, AND MUTAGENESIS OF CYS-91.
DOI=10.1038/nature02090; PubMed=14628054 [NCBI, ExPASy, EBI, Israel, Japan]
Imaizumi T., Tran H.G., Swartz T.E., Briggs W.R., Kay S.A.;
"FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis.";
Nature 426:302-306(2003).
[7]
FUNCTION.
DOI=10.1073/pnas.1031791100; PubMed=12719523 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng P., He Q., Yang Y., Wang L., Liu Y.;
"Functional conservation of light, oxygen, or voltage domains in light sensing.";
Proc. Natl. Acad. Sci. U.S.A. 100:5938-5943(2003).
[8]
INTERACTION WITH SKP1A; SKP1B; SKP1K; SKP1N AND ADO2.
DOI=10.1093/jxb/erh226; PubMed=15310821 [NCBI, ExPASy, EBI, Israel, Japan]
Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N., Komatsu A., Seki M., Shinozaki K., Kiyosue T.;
"Identification of ASK and clock-associated proteins as molecular partners of LKP2 (LOV kelch protein 2) in Arabidopsis.";
J. Exp. Bot. 55:2015-2027(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF216523; AAF32298.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF252296; AAK27435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012563; AAG51994.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY064999; AAL57647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY113029; AAM47337.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F96703; F96703.
RefSeq NP_564919.1; -.
UniGene At.20568
3D structure databases
HSSP Q8LPE0; 1N9L. [HSSP ENTRY / PDB]
ModBase Q9C9W9.
Protein-protein interaction databases
IntAct Q9C9W9; -.
Organism-specific databases
GeneFarm 5108; 485.
TAIR At1g68050; -.
Gene expression databases
GermOnline AT1G68050; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
IPR015915; Kelch-typ_b-propeller.
IPR006652; Kelch_1.
IPR011498; Kelch_2.
IPR001610; PAC.
IPR000014; PAS.
IPR000700; PAS-assoc_C.
Graphical view of domain structure.
Gene3D G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
Pfam PF00646; F-box; 1.
PF01344; Kelch_1; 2.
PF07646; Kelch_2; 3.
Pfam graphical view of domain structure.
SMART SM00086; PAC; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00229; sensory_box; 1.
PROSITE PS50181; FBOX; FALSE_NEG.
PS50113; PAC; FALSE_NEG.
PS50112; PAS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9C9W9.
Genome annotation databases
GeneID 843133; -.
GenomeReviews CT485782_GR; AT1G68050.
KEGG ath:AT1G68050; -.
NMPDR fig|3702.1.peg.6256; -.
Other
ProtoNet Q9C9W9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Biological rhythms; Chromophore; Complete proteome; Flavoprotein; FMN; Kelch repeat; Nucleus; Photoreceptor protein; Receptor; Repeat; Sensory transduction; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   619  619     Adagio protein 3. PRO_0000119958
DOMAIN   44   123  80     PAS. 
DOMAIN   127   168  42     PAC. 
DOMAIN   211   257  47     F-box. 
REPEAT   304   354  51     Kelch 1. 
REPEAT   357   404  48     Kelch 2. 
REPEAT   409   457  49     Kelch 3. 
REPEAT   462   513  52     Kelch 4. 
REPEAT   523   571  49     Kelch 5. 
MOD_RES   91    91        S-4a-FMN cysteine. 
MUTAGEN   91    91        C->A: No FMN binding. 
CONFLICT   484   484        S -> I (in Ref. 1 and 2). 
CONFLICT   581   581        S -> N (in Ref. 1 and 2). 
Sequence information
Length: 619 AA [This is the length of the unprocessed precursor] Molecular weight: 69063 Da [This is the MW of the unprocessed precursor] CRC64: AC90C0641149A3D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAREHAIGEA TGKRKKRGRV EEAEEYCNDG IEEQVEDEKL PLEVGMFYYP MTPPSFIVSD 

        70         80         90        100        110        120 
ALEPDFPLIY VNRVFEVFTG YRADEVLGRN CRFLQYRDPR AQRRHPLVDP VVVSEIRRCL 

       130        140        150        160        170        180 
EEGIEFQGEL LNFRKDGTPL VNRLRLAPIR DDDGTITHVI GIQVFSETTI DLDRVSYPVF 

       190        200        210        220        230        240 
KHKQQLDQTS ECLFPSGSPR FKEHHEDFCG ILQLSDEVLA HNILSRLTPR DVASIGSACR 

       250        260        270        280        290        300 
RLRQLTKNES VRKMVCQNAW GKEITGTLEI MTKKLRWGRL ARELTTLEAV CWRKFTVGGI 

       310        320        330        340        350        360 
VQPSRCNFSA CAVGNRLVLF GGEGVNMQPL DDTFVLNLDA ECPEWQRVRV TSSPPGRWGH 

       370        380        390        400        410        420 
TLSCLNGSWL VVFGGCGRQG LLNDVFVLDL DAKHPTWKEV AGGTPPLPRS WHSSCTIEGS 

       430        440        450        460        470        480 
KLVVSGGCTD AGVLLSDTFL LDLTTDKPTW KEIPTSWAPP SRLGHSLSVF GRTKILMFGG 

       490        500        510        520        530        540 
LANSGHLKLR SGEAYTIDLE DEEPRWRELE CSAFPGVVVP PPRLDHVAVS MPCGRVIIFG 

       550        560        570        580        590        600 
GSIAGLHSPS QLFLIDPAEE KPSWRILNVP GKPPKLAWGH STCVVGGTRV LVLGGHTGEE 

       610 
WILNELHELC LASRQDSDL 

Q9C9W9 in FASTA format

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