AFR_ARATH
ID AFR_ARATH Reviewed; 372 AA.
AC Q8LAW2; Q9SJB1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=F-box protein AFR;
DE AltName: Full=Protein ATTENUATED FAR-RED RESPONSE;
DE AltName: Full=SKP1-interacting partner 29;
GN Name=AFR; Synonyms=SKIP29; OrderedLocusNames=At2g24540; ORFNames=F25P17.16;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=11118138; DOI=10.1126/science.290.5499.2110;
RA Harmer S.L., Hogenesch J.B., Straume M., Chang H.-S., Han B., Zhu T.,
RA Wang X., Kreps J.A., Kay S.A.;
RT "Orchestrated transcription of key pathways in Arabidopsis by the circadian
RT clock.";
RL Science 290:2110-2113(2000).
RN [6]
RP FUNCTION, INDUCTION, AND INTERACTION WITH SKP1A/ASK1.
RX PubMed=14653999; DOI=10.1016/j.cub.2003.11.019;
RA Harmon F.G., Kay S.A.;
RT "The F box protein AFR is a positive regulator of phytochrome A-mediated
RT light signaling.";
RL Curr. Biol. 13:2091-2096(2003).
RN [7]
RP INTERACTION WITH SKP1A/ASK1.
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).
CC -!- FUNCTION: Component of SCF (ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity). Part of the
CC phyA-mediated signaling transduction pathway leading to the regulation
CC of gene expression and hypocotyls elongation in response to red and
CC far-red light exposure. {ECO:0000250, ECO:0000269|PubMed:14653999}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A. {ECO:0000250,
CC ECO:0000269|PubMed:12795696, ECO:0000269|PubMed:14653999}.
CC -!- INTERACTION:
CC Q8LAW2; Q39255: SKP1A; NbExp=4; IntAct=EBI-604438, EBI-532357;
CC -!- INDUCTION: Rhythmic expression with highest levels at the end of the
CC dark phase, just before the transition to light. Induction by far-red
CC light requires phyA. {ECO:0000269|PubMed:11118138,
CC ECO:0000269|PubMed:14653999}.
CC -!- DOMAIN: The kelch repeats form a beta-propeller structure involved in
CC protein-protein interaction.
CC -!- DOMAIN: The F-box is required for the interaction with SKP1A.
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; AC006954; AAD23891.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07590.1; -; Genomic_DNA.
DR EMBL; AY072009; AAL57704.1; -; mRNA.
DR EMBL; BT000847; AAN38684.1; -; mRNA.
DR EMBL; AY087570; AAM65112.1; -; mRNA.
DR PIR; H84637; H84637.
DR RefSeq; NP_565572.1; NM_128015.2.
DR AlphaFoldDB; Q8LAW2; -.
DR SMR; Q8LAW2; -.
DR BioGRID; 2342; 6.
DR IntAct; Q8LAW2; 6.
DR STRING; 3702.AT2G24540.1; -.
DR PaxDb; Q8LAW2; -.
DR PRIDE; Q8LAW2; -.
DR ProteomicsDB; 244685; -.
DR EnsemblPlants; AT2G24540.1; AT2G24540.1; AT2G24540.
DR GeneID; 816990; -.
DR Gramene; AT2G24540.1; AT2G24540.1; AT2G24540.
DR KEGG; ath:AT2G24540; -.
DR Araport; AT2G24540; -.
DR TAIR; locus:2046683; AT2G24540.
DR eggNOG; KOG1072; Eukaryota.
DR HOGENOM; CLU_044411_0_0_1; -.
DR InParanoid; Q8LAW2; -.
DR OMA; CLLHVPY; -.
DR OrthoDB; 939068at2759; -.
DR PhylomeDB; Q8LAW2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LAW2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LAW2; differential.
DR Genevisible; Q8LAW2; AT.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:UniProtKB.
DR GO; GO:0009585; P:red, far-red light phototransduction; IMP:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Kelch repeat; Phytochrome signaling pathway; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..372
FT /note="F-box protein AFR"
FT /id="PRO_0000119959"
FT DOMAIN 29..74
FT /note="F-box"
FT REPEAT 80..126
FT /note="Kelch 1"
FT REPEAT 135..178
FT /note="Kelch 2"
FT REPEAT 179..227
FT /note="Kelch 3"
FT REPEAT 229..276
FT /note="Kelch 4"
FT REPEAT 279..325
FT /note="Kelch 5"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 130
FT /note="M -> I (in Ref. 4; AAM65112)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="Q -> E (in Ref. 4; AAM65112)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="Q -> P (in Ref. 4; AAM65112)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="R -> K (in Ref. 4; AAM65112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41278 MW; 0F48D9747B900634 CRC64;
MAEQETTSNI NTINDQAEEE TRTKSQPLIS GLPNDIAELC LLRLPYPYHA LYRSVSSSWN
KTITNPRFLF SKQSLSISSP YLFVFAFNKS TARIQWQSLD LASGRWFVLP PMPNSFTKIS
SPHALSCASM PRQGKLFVLG GGDVNRSAVV YTALTNRWSC ISPMMSPRTY FVSGNVNGKI
MAVGGSVGGN GEATTEVESY DPDNDTWTVV KKLPMVLAKY DSAVIGKEMC VTEGWAWPFM
FPPMGQVYDS DEGTWREMSG GMKEGWTGVS VVIRDRLFVI SEHGDFPMKV YCSDDDTWRY
VSGEKLQGEK MRRPFAVTGA DDRVFVVASG INVAEGRVSE GQNGDFSVEW RMVSSPKSSI
QFSPASCHVL YV
