AFB2_ARATH
ID AFB2_ARATH Reviewed; 575 AA.
AC Q9LW29;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein AUXIN SIGNALING F-BOX 2;
GN Name=AFB2; Synonyms=LRF2; OrderedLocusNames=At3g26810; ORFNames=MDJ14.12;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 LEUCINE-RICH REPEATS.
RX PubMed=12008900; DOI=10.1023/a:1014440531842;
RA Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
RT "Cloning by pathway activation in yeast: identification of an Arabidopsis
RT thaliana F-box protein that can turn on glucose repression.";
RL Plant Mol. Biol. 49:69-79(2002).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP IAA7.
RX PubMed=15992545; DOI=10.1016/j.devcel.2005.05.014;
RA Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L.,
RA Ehrismann J.S., Juergens G., Estelle M.;
RT "Plant development is regulated by a family of auxin receptor F box
RT proteins.";
RL Dev. Cell 9:109-119(2005).
RN [6]
RP FUNCTION.
RX PubMed=15917797; DOI=10.1038/nature03543;
RA Dharmasiri N., Dharmasiri S., Estelle M.;
RT "The F-box protein TIR1 is an auxin receptor.";
RL Nature 435:441-445(2005).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=16627744; DOI=10.1126/science.1126088;
RA Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M.,
RA Voinnet O., Jones J.D.G.;
RT "A plant miRNA contributes to antibacterial resistance by repressing auxin
RT signaling.";
RL Science 312:436-439(2006).
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. Confers sensitivity to the
CC virulent bacterial pathogen P.syringae (By similarity). Auxin receptor
CC that mediates Aux/IAA proteins proteasomal degradation and auxin-
CC regulated transcription. Involved in embryogenesis regulation by auxin.
CC {ECO:0000250, ECO:0000269|PubMed:15917797, ECO:0000269|PubMed:15992545,
CC ECO:0000269|PubMed:16627744}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with Aux/IAA proteins (IAA7) in an auxin-
CC dependent manner. {ECO:0000250, ECO:0000269|PubMed:15992545}.
CC -!- INTERACTION:
CC Q9LW29; Q38825: IAA7; NbExp=2; IntAct=EBI-617556, EBI-602959;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in seedlings.
CC {ECO:0000269|PubMed:15992545}.
CC -!- INDUCTION: Repressed by miR393a (microRNA) in response to flg-22
CC (flagellin-derived peptide 22). {ECO:0000269|PubMed:16627744}.
CC -!- DOMAIN: The F-box is necessary for the interaction with SKP1.
CC {ECO:0000250}.
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DR EMBL; AB016889; BAB01228.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77218.1; -; Genomic_DNA.
DR EMBL; AY062568; AAL32646.1; -; mRNA.
DR EMBL; BT010396; AAQ56839.1; -; mRNA.
DR RefSeq; NP_566800.1; NM_113593.3.
DR AlphaFoldDB; Q9LW29; -.
DR SMR; Q9LW29; -.
DR BioGRID; 7626; 13.
DR DIP; DIP-34608N; -.
DR IntAct; Q9LW29; 5.
DR STRING; 3702.AT3G26810.1; -.
DR PaxDb; Q9LW29; -.
DR PRIDE; Q9LW29; -.
DR ProteomicsDB; 244687; -.
DR EnsemblPlants; AT3G26810.1; AT3G26810.1; AT3G26810.
DR GeneID; 822296; -.
DR Gramene; AT3G26810.1; AT3G26810.1; AT3G26810.
DR KEGG; ath:AT3G26810; -.
DR Araport; AT3G26810; -.
DR TAIR; locus:2088464; AT3G26810.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q9LW29; -.
DR OMA; ENGHEGR; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q9LW29; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LW29; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW29; baseline and differential.
DR Genevisible; Q9LW29; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0010011; F:auxin binding; IGI:TAIR.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010152; P:pollen maturation; IGI:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0048443; P:stamen development; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041101; Transp_inhibit.
DR Pfam; PF18511; F-box_5; 1.
DR Pfam; PF18791; Transp_inhibit; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 7.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Developmental protein; Nucleus; Plant defense;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..575
FT /note="Protein AUXIN SIGNALING F-BOX 2"
FT /id="PRO_0000272243"
FT DOMAIN 1..47
FT /note="F-box"
FT REGION 76..77
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 343..348
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 400..404
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 459..460
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 108..109
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 396..398
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 479..480
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT SITE 134
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 375
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 484
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 64605 MW; D383C4E0A76D50D6 CRC64;
MNYFPDEVIE HVFDFVTSHK DRNAISLVCK SWYKIERYSR QKVFIGNCYA INPERLLRRF
PCLKSLTLKG KPHFADFNLV PHEWGGFVLP WIEALARSRV GLEELRLKRM VVTDESLELL
SRSFVNFKSL VLVSCEGFTT DGLASIAANC RHLRDLDLQE NEIDDHRGQW LSCFPDTCTT
LVTLNFACLE GETNLVALER LVARSPNLKS LKLNRAVPLD ALARLMACAP QIVDLGVGSY
ENDPDSESYL KLMAVIKKCT SLRSLSGFLE AAPHCLSAFH PICHNLTSLN LSYAAEIHGS
HLIKLIQHCK KLQRLWILDS IGDKGLEVVA STCKELQELR VFPSDLLGGG NTAVTEEGLV
AISAGCPKLH SILYFCQQMT NAALVTVAKN CPNFIRFRLC ILEPNKPDHV TSQPLDEGFG
AIVKACKSLR RLSLSGLLTD QVFLYIGMYA NQLEMLSIAF AGDTDKGMLY VLNGCKKMKK
LEIRDSPFGD TALLADVSKY ETMRSLWMSS CEVTLSGCKR LAEKAPWLNV EIINENDNNR
MEENGHEGRQ KVDKLYLYRT VVGTRMDAPP FVWIL
