ADO2_ARATH
ID ADO2_ARATH Reviewed; 611 AA.
AC Q8W420; B5X4Z7; Q9C5S6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Adagio protein 2;
DE AltName: Full=F-box only protein 2c;
DE Short=FBX2c;
DE AltName: Full=Flavin-binding kelch repeat F-box protein 1-like protein 1;
DE Short=FKF1-like protein 1;
DE AltName: Full=LOV kelch protein 2;
GN Name=ADO2; Synonyms=FKL1, LKP2; OrderedLocusNames=At2g18915;
GN ORFNames=F19F24.11;
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] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=11752379; DOI=10.2307/3871526;
RA Schultz T.F., Kiyosue T., Yanovsky M., Wada M., Kay S.A.;
RT "A role for LKP2 in the circadian clock of Arabidopsis.";
RL Plant Cell 13:2659-2670(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH SKP1A; SKP1B; SKP1C; SKP1D; SKP1E; SKP1K; SKP1N; SKP1TA;
RP SKP1TB; ADO1; AD03; APRR1 AND APRR5, SELF-ASSOCIATION, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
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 [9]
RP INTERACTION WITH DI19 AND COL1, AND SUBCELLULAR LOCATION.
RX PubMed=15937324; DOI=10.1093/pcp/pci144;
RA Fukamatsu Y., Mitsui S., Yasuhara M., Tokioka Y., Ihara N., Fujita S.,
RA Kiyosue T.;
RT "Identification of LOV KELCH PROTEIN2 (LKP2)-interacting factors that can
RT recruit LKP2 to nuclear bodies.";
RL Plant Cell Physiol. 46:1340-1349(2005).
RN [10]
RP INTERACTION WITH CDF1; CDF2 AND CDF3, AND DISRUPTION PHENOTYPE.
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 [11]
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 [12]
RP FUNCTION, INTERACTION WITH ADO3, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP LYS-283; LYS-335; LYS-410; LYS-463; LYS-472 AND LYS-553, 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).
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(ADO2) 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 seem to be substrates of the SCF(ADO2) complex. ADO2 interacts with
CC ADO3 and export it to cytoplasmic speckles, preventing the interaction
CC of ADO3 with CDF1. Ubiquitination of ADO2 is not involved in this
CC recruitment. {ECO:0000269|PubMed:11752379,
CC ECO:0000269|PubMed:21518052}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Self-associates. Interacts (via Kelch repeats) with AD03,
CC CDF1, CDF2 and CDF3. Interacts with GI, ADO1, SKP1A/ASK1, SKP1B/ASK2,
CC SKP1C/ASK3, SKP1D/ASK4, SKP1E/ASK5, SKP1K/ASK11, SKP1N/ASK14,
CC SKP1TA/ASK20A, SKP1TB/ASK20B, APRR1, APRR5, DI19 and COL1.
CC {ECO:0000269|PubMed:15310821, ECO:0000269|PubMed:15937324,
CC ECO:0000269|PubMed:16002617, ECO:0000269|PubMed:17704763,
CC ECO:0000269|PubMed:21518052}.
CC -!- INTERACTION:
CC Q8W420; Q8W1E3: CDF1; NbExp=2; IntAct=EBI-1015688, EBI-1536051;
CC Q8W420; Q93ZL5: CDF2; NbExp=3; IntAct=EBI-1015688, EBI-1536103;
CC Q8W420; Q8LFV3: CDF3; NbExp=3; IntAct=EBI-1015688, EBI-1536119;
CC Q8W420; Q9SQI2: GI; NbExp=4; IntAct=EBI-1015688, EBI-446380;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W420-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W420-2; Sequence=VSP_016048;
CC -!- TISSUE SPECIFICITY: Weakly expressed in seedlings, root tips, stems,
CC leaves, flowers, young siliques, sepals and seeds.
CC {ECO:0000269|PubMed:11752379, ECO:0000269|PubMed:15310821}.
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 but no effect on flowering time. {ECO:0000269|PubMed:16002617,
CC ECO:0000269|PubMed:21518052}.
CC -!- MISCELLANEOUS: 'Adagio' means slowly in Italian.
CC -!- SIMILARITY: Belongs to the ADAGIO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK27434.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM14891.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF252295; AAK27434.1; ALT_INIT; mRNA.
DR EMBL; AB038797; BAB83169.1; -; mRNA.
DR EMBL; AC003673; AAM14891.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC06825.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06826.1; -; Genomic_DNA.
DR EMBL; AY099709; AAM20560.1; -; mRNA.
DR EMBL; BT046116; ACI46504.1; -; mRNA.
DR RefSeq; NP_565444.2; NM_127448.2. [Q8W420-2]
DR RefSeq; NP_849983.1; NM_179652.2. [Q8W420-1]
DR AlphaFoldDB; Q8W420; -.
DR SMR; Q8W420; -.
DR BioGRID; 1765; 30.
DR DIP; DIP-33897N; -.
DR IntAct; Q8W420; 16.
DR STRING; 3702.AT2G18915.2; -.
DR PaxDb; Q8W420; -.
DR PRIDE; Q8W420; -.
DR ProteomicsDB; 244874; -. [Q8W420-1]
DR EnsemblPlants; AT2G18915.1; AT2G18915.1; AT2G18915. [Q8W420-2]
DR EnsemblPlants; AT2G18915.2; AT2G18915.2; AT2G18915. [Q8W420-1]
DR GeneID; 816408; -.
DR Gramene; AT2G18915.1; AT2G18915.1; AT2G18915. [Q8W420-2]
DR Gramene; AT2G18915.2; AT2G18915.2; AT2G18915. [Q8W420-1]
DR KEGG; ath:AT2G18915; -.
DR Araport; AT2G18915; -.
DR TAIR; locus:505006254; AT2G18915.
DR eggNOG; ENOG502QQ74; Eukaryota.
DR HOGENOM; CLU_033494_1_0_1; -.
DR InParanoid; Q8W420; -.
DR OMA; GGCHISE; -.
DR OrthoDB; 273755at2759; -.
DR PhylomeDB; Q8W420; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8W420; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8W420; baseline and differential.
DR Genevisible; Q8W420; AT.
DR GO; GO:0015030; C:Cajal body; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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:0042752; P:regulation of circadian rhythm; IMP:TAIR.
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; 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 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 Alternative splicing; Biological rhythms; Chromophore; Cytoplasm;
KW Flavoprotein; Flowering; FMN; Kelch repeat; Nucleus; Photoreceptor protein;
KW Receptor; Reference proteome; Repeat; Sensory transduction;
KW Ubl conjugation pathway.
FT CHAIN 1..611
FT /note="Adagio protein 2"
FT /id="PRO_0000119957"
FT DOMAIN 35..114
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 118..158
FT /note="PAC"
FT DOMAIN 196..242
FT /note="F-box"
FT REPEAT 293..343
FT /note="Kelch 1"
FT REPEAT 358..396
FT /note="Kelch 2"
FT REPEAT 397..446
FT /note="Kelch 3"
FT REPEAT 463..515
FT /note="Kelch 4"
FT REPEAT 527..579
FT /note="Kelch 5"
FT REGION 1..20
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 VAR_SEQ 79..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11260718"
FT /id="VSP_016048"
FT MUTAGEN 283
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-335; R-410; R-463; R-472
FT and R-553."
FT /evidence="ECO:0000269|PubMed:21518052"
FT MUTAGEN 335
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-283; R-410; R-463; R-472
FT and R-553."
FT /evidence="ECO:0000269|PubMed:21518052"
FT MUTAGEN 410
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-283; R-335; R-463; R-472
FT and R-553."
FT /evidence="ECO:0000269|PubMed:21518052"
FT MUTAGEN 463
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-283; R-335; R-410; R-472
FT and R-553."
FT /evidence="ECO:0000269|PubMed:21518052"
FT MUTAGEN 472
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-283; R-335; R-410; R-463
FT and R-553."
FT /evidence="ECO:0000269|PubMed:21518052"
FT MUTAGEN 553
FT /note="K->R: No effect on the recruitment of ADO3 to the
FT cytoplasm; when associated with R-283; R-335; R-410; R-463
FT and R-472."
FT /evidence="ECO:0000269|PubMed:21518052"
SQ SEQUENCE 611 AA; 66351 MW; FDB9F994CBF0D017 CRC64;
MQNQMEWDSD SDLSGGDEVA EDGWFGGDNG AIPFPVGSLP GTAPCGFVVS DALEPDNPII
YVNTVFEIVT GYRAEEVIGR NCRFLQCRGP FTKRRHPMVD STIVAKMRQC LENGIEFQGE
LLNFRKDGSP LMNKLRLVPI REEDEITHFI GVLLFTDAKI DLGPSPDLSA KEIPRISRSF
TSALPIGERN VSRGLCGIFE LSDEVIAIKI LSQLTPGDIA SVGCVCRRLN ELTKNDDVWR
MVCQNTWGTE ATRVLESVPG AKRIGWVRLA REFTTHEATA WRKFSVGGTV EPSRCNFSAC
AVGNRIVIFG GEGVNMQPMN DTFVLDLGSS SPEWKSVLVS SPPPGRWGHT LSCVNGSRLV
VFGGYGSHGL LNDVFLLDLD ADPPSWREVS GLAPPIPRSW HSSCTLDGTK LIVSGGCADS
GALLSDTFLL DLSMDIPAWR EIPVPWTPPS RLGHTLTVYG DRKILMFGGL AKNGTLRFRS
NDVYTMDLSE DEPSWRPVIG YGSSLPGGMA APPPRLDHVA ISLPGGRILI FGGSVAGLDS
ASQLYLLDPN EEKPAWRILN VQGGPPRFAW GHTTCVVGGT RLVVLGGQTG EEWMLNEAHE
LLLATSTTAS T
