ADO3_ARATH
ID ADO3_ARATH Reviewed; 619 AA.
AC Q9C9W9; Q9M648;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adagio protein 3;
DE AltName: Full=F-box only protein 2a;
DE Short=FBX2a;
DE AltName: Full=Flavin-binding kelch repeat F-box protein 1;
GN Name=ADO3; Synonyms=FKF1; OrderedLocusNames=At1g68050; ORFNames=T23K23.10;
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, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, INDUCTION, FMN-BINDING AT CYS-91, AND MUTAGENESIS OF CYS-91.
RX PubMed=14628054; DOI=10.1038/nature02090;
RA Imaizumi T., Tran H.G., Swartz T.E., Briggs W.R., Kay S.A.;
RT "FKF1 is essential for photoperiodic-specific light signalling in
RT Arabidopsis.";
RL Nature 426:302-306(2003).
RN [8]
RP FUNCTION.
RX PubMed=12719523; DOI=10.1073/pnas.1031791100;
RA Cheng P., He Q., Yang Y., Wang L., Liu Y.;
RT "Functional conservation of light, oxygen, or voltage domains in light
RT sensing.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5938-5943(2003).
RN [9]
RP INTERACTION WITH SKP1A; SKP1B; SKP1K; SKP1N AND ADO2.
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 [10]
RP INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK3; ASK11; ASK12 AND ASK13.
RX PubMed=14749489; DOI=10.1093/pcp/pch009;
RA Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M., Shinozaki K.,
RA Shimada H., Matsui M.;
RT "Expression and interaction analysis of Arabidopsis Skp1-related genes.";
RL Plant Cell Physiol. 45:83-91(2004).
RN [11]
RP FUNCTION, INTERACTION WITH CDF1; CDF2 AND CDF3, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=16002617; DOI=10.1126/science.1110586;
RA Imaizumi T., Schultz T.F., Harmon F.G., Ho L.A., Kay S.A.;
RT "FKF1 F-box protein mediates cyclic degradation of a repressor of CONSTANS
RT in Arabidopsis.";
RL Science 309:293-297(2005).
RN [12]
RP INTERACTION WITH GI.
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 [13]
RP FUNCTION, INTERACTION WITH GI, MUTAGENESIS OF CYS-91; ARG-92 AND GLN-163,
RP AND INDUCTION.
RX PubMed=17872410; DOI=10.1126/science.1146994;
RA Sawa M., Nusinow D.A., Kay S.A., Imaizumi T.;
RT "FKF1 and GIGANTEA complex formation is required for day-length measurement
RT in Arabidopsis.";
RL Science 318:261-265(2007).
RN [14]
RP FUNCTION.
RX PubMed=19619493; DOI=10.1016/j.devcel.2009.06.015;
RA Fornara F., Panigrahi K.C., Gissot L., Sauerbrunn N., Ruehl M.,
RA Jarillo J.A., Coupland G.;
RT "Arabidopsis DOF transcription factors act redundantly to reduce CONSTANS
RT expression and are essential for a photoperiodic flowering response.";
RL Dev. Cell 17:75-86(2009).
RN [15]
RP FUNCTION, INTERACTION WITH ADO1 AND ADO2, AND SUBCELLULAR LOCATION.
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 [16]
RP FUNCTION, INTERACTION WITH CO, AND SUBCELLULAR LOCATION.
RX PubMed=22628657; DOI=10.1126/science.1219644;
RA Song Y.H., Smith R.W., To B.J., Millar A.J., Imaizumi T.;
RT "FKF1 conveys timing information for CONSTANS stabilization in
RT photoperiodic flowering.";
RL Science 336:1045-1049(2012).
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(ADO3) E3 ubiquitin ligase
CC complex is involved in the regulation of circadian clock-dependent
CC processes including transition to flowering time, hypocotyl elongation,
CC cotyledons and leaf movement rhythms. Forms a complex with 'GIGANTEA'
CC (GI) to regulate 'CONSTANS' (CO) expression. Promotes CO expression
CC during the light period of long days by decreasing the stability of
CC CDF1 and CDF2 and by interacting directly with the CO protein and
CC stabilizing it. ADO3 function is mainly GI dependent. Does not act as a
CC regulator of CDF1 transcription. The interactions of ADO1/ZTL and ADO2
CC with ADO3 prevent its interaction with CDF1.
CC {ECO:0000269|PubMed:10847687, ECO:0000269|PubMed:12719523,
CC ECO:0000269|PubMed:14628054, ECO:0000269|PubMed:16002617,
CC ECO:0000269|PubMed:17872410, ECO:0000269|PubMed:19619493,
CC ECO:0000269|PubMed:21518052, ECO:0000269|PubMed:22628657}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ADO1 (via Kelch repeats), ADO2 (via Kelch
CC repeats), SKP1A/ASK1, SKP1B/ASK2, ASK3, SKP1K/ASK11, ASK12, ASK13 and
CC SKP1N/ASK14. Interacts (via Kelch repeats) with CDF1, CDF2 and CDF3.
CC Interacts (via N-terminus) with CO and GI (via N-terminus) in a blue-
CC light-dependent manner. {ECO:0000269|PubMed:14749489,
CC ECO:0000269|PubMed:15310821, ECO:0000269|PubMed:16002617,
CC ECO:0000269|PubMed:17704763, ECO:0000269|PubMed:17872410,
CC ECO:0000269|PubMed:21518052, ECO:0000269|PubMed:22628657}.
CC -!- INTERACTION:
CC Q9C9W9; Q8W1E3: CDF1; NbExp=2; IntAct=EBI-401228, EBI-1536051;
CC Q9C9W9; Q93ZL5: CDF2; NbExp=2; IntAct=EBI-401228, EBI-1536103;
CC Q9C9W9; Q8LFV3: CDF3; NbExp=2; IntAct=EBI-401228, EBI-1536119;
CC Q9C9W9; Q9SQI2: GI; NbExp=11; IntAct=EBI-401228, EBI-446380;
CC Q9C9W9; Q9FHW7: SKP1B; NbExp=5; IntAct=EBI-401228, EBI-604076;
CC Q9C9W9; P43292: SRK2G; NbExp=3; IntAct=EBI-401228, EBI-401174;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Moves from the nucleus
CC into cytosolic speckles upon interaction with ADO1 and ADO2.
CC -!- TISSUE SPECIFICITY: Highly expressed in stomata and leaves and to a
CC lower extent in seeds, roots, rosettes, stems and siliques. Also
CC present in sepals and anther filaments. {ECO:0000269|PubMed:10847687,
CC ECO:0000269|PubMed:16002617}.
CC -!- INDUCTION: Circadian-regulation. Expression is higher during the late
CC light phase than during the dark phase. {ECO:0000269|PubMed:10847687,
CC ECO:0000269|PubMed:14628054, ECO:0000269|PubMed:17872410}.
CC -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC is reversed in the dark.
CC -!- DISRUPTION PHENOTYPE: Late flowering. {ECO:0000269|PubMed:16002617}.
CC -!- MISCELLANEOUS: 'Adagio' means slowly in Italian.
CC -!- SIMILARITY: Belongs to the ADAGIO family. {ECO:0000305}.
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DR EMBL; AF216523; AAF32298.2; -; mRNA.
DR EMBL; AF252296; AAK27435.1; -; mRNA.
DR EMBL; AC012563; AAG51994.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34741.1; -; Genomic_DNA.
DR EMBL; AY064999; AAL57647.1; -; mRNA.
DR EMBL; AY113029; AAM47337.1; -; mRNA.
DR PIR; F96703; F96703.
DR RefSeq; NP_564919.1; NM_105475.4.
DR AlphaFoldDB; Q9C9W9; -.
DR SMR; Q9C9W9; -.
DR BioGRID; 28354; 24.
DR DIP; DIP-31333N; -.
DR IntAct; Q9C9W9; 16.
DR STRING; 3702.AT1G68050.1; -.
DR iPTMnet; Q9C9W9; -.
DR PaxDb; Q9C9W9; -.
DR PRIDE; Q9C9W9; -.
DR ProteomicsDB; 244875; -.
DR EnsemblPlants; AT1G68050.1; AT1G68050.1; AT1G68050.
DR GeneID; 843133; -.
DR Gramene; AT1G68050.1; AT1G68050.1; AT1G68050.
DR KEGG; ath:AT1G68050; -.
DR Araport; AT1G68050; -.
DR TAIR; locus:2200176; AT1G68050.
DR eggNOG; ENOG502QWBU; Eukaryota.
DR HOGENOM; CLU_033494_1_0_1; -.
DR InParanoid; Q9C9W9; -.
DR OMA; AVCWRKF; -.
DR OrthoDB; 466221at2759; -.
DR PhylomeDB; Q9C9W9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9C9W9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9W9; baseline and differential.
DR Genevisible; Q9C9W9; 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; IDA:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:2001007; P:negative regulation of cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009637; P:response to blue light; IDA:TAIR.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011498; Kelch_2.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Chromophore; Cytoplasm; Flavoprotein; Flowering; FMN;
KW Kelch repeat; Nucleus; Photoreceptor protein; Receptor; Reference proteome;
KW Repeat; Sensory transduction; Ubl conjugation pathway.
FT CHAIN 1..619
FT /note="Adagio protein 3"
FT /id="PRO_0000119958"
FT DOMAIN 44..123
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 127..168
FT /note="PAC"
FT DOMAIN 211..257
FT /note="F-box"
FT REPEAT 304..354
FT /note="Kelch 1"
FT REPEAT 357..404
FT /note="Kelch 2"
FT REPEAT 409..457
FT /note="Kelch 3"
FT REPEAT 462..513
FT /note="Kelch 4"
FT REPEAT 523..571
FT /note="Kelch 5"
FT MOD_RES 91
FT /note="S-4a-FMN cysteine"
FT MUTAGEN 91
FT /note="C->A: No FMN binding and decreased interaction with
FT GI."
FT /evidence="ECO:0000269|PubMed:14628054,
FT ECO:0000269|PubMed:17872410"
FT MUTAGEN 92
FT /note="R->D: Decreased interaction with GI."
FT /evidence="ECO:0000269|PubMed:17872410"
FT MUTAGEN 163
FT /note="Q->L: Decreased interaction with GI."
FT /evidence="ECO:0000269|PubMed:17872410"
FT CONFLICT 484
FT /note="S -> I (in Ref. 1; AAF32298 and 2; AAK27435)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="S -> N (in Ref. 1; AAF32298 and 2; AAK27435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 69063 MW; AC90C0641149A3D8 CRC64;
MAREHAIGEA TGKRKKRGRV EEAEEYCNDG IEEQVEDEKL PLEVGMFYYP MTPPSFIVSD
ALEPDFPLIY VNRVFEVFTG YRADEVLGRN CRFLQYRDPR AQRRHPLVDP VVVSEIRRCL
EEGIEFQGEL LNFRKDGTPL VNRLRLAPIR DDDGTITHVI GIQVFSETTI DLDRVSYPVF
KHKQQLDQTS ECLFPSGSPR FKEHHEDFCG ILQLSDEVLA HNILSRLTPR DVASIGSACR
RLRQLTKNES VRKMVCQNAW GKEITGTLEI MTKKLRWGRL ARELTTLEAV CWRKFTVGGI
VQPSRCNFSA CAVGNRLVLF GGEGVNMQPL DDTFVLNLDA ECPEWQRVRV TSSPPGRWGH
TLSCLNGSWL VVFGGCGRQG LLNDVFVLDL DAKHPTWKEV AGGTPPLPRS WHSSCTIEGS
KLVVSGGCTD AGVLLSDTFL LDLTTDKPTW KEIPTSWAPP SRLGHSLSVF GRTKILMFGG
LANSGHLKLR SGEAYTIDLE DEEPRWRELE CSAFPGVVVP PPRLDHVAVS MPCGRVIIFG
GSIAGLHSPS QLFLIDPAEE KPSWRILNVP GKPPKLAWGH STCVVGGTRV LVLGGHTGEE
WILNELHELC LASRQDSDL
