GRH1_ARATH
ID GRH1_ARATH Reviewed; 585 AA.
AC Q9ZR12; Q94AU0; Q9C5Y7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GRR1-like protein 1;
DE AltName: Full=Protein AUXIN SIGNALING F-BOX 1;
GN Name=GRH1; Synonyms=AFB1, FBL18, GER1, LRF1; OrderedLocusNames=At4g03190;
GN ORFNames=F4C21.11;
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], FUNCTION, INTERACTION WITH SKP1A/ASK1 AND
RP SKP1B/ASK2, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH SKP1A/ASK1 AND SKP1B/ASK2.
RX PubMed=10398681; DOI=10.1101/gad.13.13.1678;
RA Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
RA Crosby W.L., Yang M., Ma H., Estelle M.;
RT "Identification of an SCF ubiquitin-ligase complex required for auxin
RT response in Arabidopsis thaliana.";
RL Genes Dev. 13:1678-1691(1999).
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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CUL1; IAA7; IAA12 AND SKP1A/ASK1.
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 [8]
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 [9]
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. Auxin receptor that
CC mediates Aux/IAA proteins proteasomal degradation and auxin-regulated
CC transcription. Involved in embryogenesis regulation by auxin. Confers
CC sensitivity to the virulent bacterial pathogen P.syringae. Mediates
CC glucose repression in yeast. {ECO:0000269|PubMed:12008900,
CC 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.
CC Interacts with CUL1, SKP1A/ASK1 and SKP1B/ASK2. Interacts with Aux/IAA
CC proteins (IAA7 and IAA12) in an auxin-dependent manner.
CC {ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:12008900,
CC ECO:0000269|PubMed:15992545}.
CC -!- INTERACTION:
CC Q9ZR12; Q38825: IAA7; NbExp=2; IntAct=EBI-617479, EBI-602959;
CC Q9ZR12; Q39255: SKP1A; NbExp=3; IntAct=EBI-617479, EBI-532357;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15992545}.
CC -!- INDUCTION: Partially repressed by miR393a (microRNA) in response to
CC flg-22 (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; AF291816; AAK01147.1; -; mRNA.
DR EMBL; AC005275; AAD14447.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77804.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82287.1; -; Genomic_DNA.
DR EMBL; AY045799; AAK76473.1; -; mRNA.
DR EMBL; AY150427; AAN12969.1; -; mRNA.
DR PIR; E85040; E85040.
DR RefSeq; NP_567255.1; NM_116555.4.
DR AlphaFoldDB; Q9ZR12; -.
DR SMR; Q9ZR12; -.
DR BioGRID; 13336; 13.
DR DIP; DIP-34607N; -.
DR IntAct; Q9ZR12; 9.
DR STRING; 3702.AT4G03190.1; -.
DR iPTMnet; Q9ZR12; -.
DR PaxDb; Q9ZR12; -.
DR PRIDE; Q9ZR12; -.
DR ProteomicsDB; 247039; -.
DR EnsemblPlants; AT4G03190.1; AT4G03190.1; AT4G03190.
DR GeneID; 828045; -.
DR Gramene; AT4G03190.1; AT4G03190.1; AT4G03190.
DR KEGG; ath:AT4G03190; -.
DR Araport; AT4G03190; -.
DR TAIR; locus:2125527; AT4G03190.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q9ZR12; -.
DR OMA; EYLPALY; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q9ZR12; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZR12; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZR12; baseline and differential.
DR Genevisible; Q9ZR12; AT.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA: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:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045014; P:carbon catabolite repression of transcription by glucose; TAS:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010152; P:pollen maturation; IGI:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 6.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Developmental protein; Nucleus; Plant defense;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..585
FT /note="GRR1-like protein 1"
FT /id="PRO_0000272265"
FT DOMAIN 1..48
FT /note="F-box"
FT REGION 77..78
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 401..405
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 460..461
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 109..110
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 397..399
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 480..481
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 161
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 376
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 485
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="M -> I (in Ref. 4; AAK76473)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> S (in Ref. 1; AAK01147)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> T (in Ref. 1; AAK01147)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="C -> S (in Ref. 4; AAK76473)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="I -> M (in Ref. 4; AAK76473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 65648 MW; D39D627C82864D83 CRC64;
MGLRFPPKVL EHILSFIDSN EDRNSVSLVC KSWFETERKT RKRVFVGNCY AVSPAAVTRR
FPEMRSLTLK GKPHFADYNL VPDGWGGYAW PWIEAMAAKS SSLEEIRMKR MVVTDECLEK
IAASFKDFKV LVLTSCEGFS TDGIAAIAAT CRNLRVLELR ECIVEDLGGD WLSYFPESST
SLVSLDFSCL DSEVKISDLE RLVSRSPNLK SLKLNPAVTL DGLVSLLRCA PQLTELGTGS
FAAQLKPEAF SKLSEAFSNC KQLQSLSGLW DVLPEYLPAL YSVCPGLTSL NLSYATVRMP
DLVELLRRCS KLQKLWVMDL IEDKGLEAVA SYCKELRELR VFPSEPDLDA TNIPLTEQGL
VFVSKGCRKL ESVLYFCVQF TNAALFTIAR KRPNLKCFRL CVIEPFAPDY KTNEPLDKGF
KAIAEGCRDL RRLSVSGLLS DKAFKYIGKH AKKVRMLSIA FAGDSDLMLH HLLSGCESLK
KLEIRDCPFG DTALLEHAAK LETMRSLWMS SCFVSFGACK LLSQKMPRLN VEVIDEHPPE
SRPESSPVER IYIYRTVAGP RMDTPEFVWT IHKNPENGVS HLAIK
