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UniProtKB/Swiss-Prot entry Q570C0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TIR1_ARATH
Primary accession number Q570C0
Secondary accession number O24660
Integrated into Swiss-Prot on June 21, 2005
Sequence was last modified on June 21, 2005 (Sequence version 2)
Annotations were last modified on    April 29, 2008 (Entry version 37)
Name and origin of the protein
Protein name Protein TRANSPORT INHIBITOR RESPONSE 1
Synonym F-box/LRR-repeat protein 1
Gene name
Name: TIR1
Synonyms: FBL1, WEI1
OrderedLocusNames: At3g62980
ORFNames: T20O10.80
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-147 AND GLY-441.
PubMed=9436980 [NCBI, ExPASy, EBI, Israel, Japan]
Ruegger M., Dewey E., Gray W.M., Hobbie L., Turner J., Estelle M.;
"The TIR1 protein of Arabidopsis functions in auxin response and is related to human SKP2 and yeast grr1p.";
Genes Dev. 12:198-207(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-594.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH SKP1A; SKP1B AND CUL1, DOMAIN, AND MUTAGENESIS OF PRO-10.
DOI=10.1101/gad.13.13.1678; PubMed=10398681 [NCBI, ExPASy, EBI, Israel, Japan]
Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T., Crosby W.L., Yang M., Ma H., Estelle M.;
"Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana.";
Genes Dev. 13:1678-1691(1999).
[6]
GENE FAMILY, AND NOMENCLATURE.
DOI=10.1016/S1360-1385(00)01769-6; PubMed=11077244 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
[7]
INTERACTION WITH IAA7 AND IAA17.
DOI=10.1038/35104500; PubMed=11713520 [NCBI, ExPASy, EBI, Israel, Japan]
Gray W.M., Kepinski S., Rouse D., Leyser O., Estelle M.;
"Auxin regulates SCF(TIR1)-dependent degradation of AUX/IAA proteins.";
Nature 414:271-276(2001).
[8]
INTERACTION WITH THE CSN COMPLEX.
DOI=10.1126/science.1059776; PubMed=11337587 [NCBI, ExPASy, EBI, Israel, Japan]
Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S., Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
"Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCF(TIR1) in mediating auxin response.";
Science 292:1379-1382(2001).
[9]
INTERACTION WITH RBX1.
DOI=10.1105/tpc.003178; PubMed=12215511 [NCBI, ExPASy, EBI, Israel, Japan]
Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
"Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function.";
Plant Cell 14:2137-2144(2002).
[10]
INTERACTION WITH IAA3.
DOI=10.1046/j.1365-313X.2003.01909.x; PubMed=14617065 [NCBI, ExPASy, EBI, Israel, Japan]
Tian Q., Nagpal P., Reed J.W.;
"Regulation of Arabidopsis SHY2/IAA3 protein turnover.";
Plant J. 36:643-651(2003).
[11]
FUNCTION, AND MUTAGENESIS OF 574-TRP--LEU-594.
DOI=10.1073/pnas.0438070100; PubMed=12606727 [NCBI, ExPASy, EBI, Israel, Japan]
Alonso J.M., Stepanova A.N., Solano R., Wisman E., Ferrari S., Ausubel F.M., Ecker J.R.;
"Five components of the ethylene-response pathway identified in a screen for weak ethylene-insensitive mutants in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 100:2992-2997(2003).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IAA12; IAA7 AND SKP1A/ASK1.
DOI=10.1016/j.devcel.2005.05.014; PubMed=15992545 [NCBI, ExPASy, EBI, Israel, Japan]
Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L., Ehrismann J.S., Juergens G., Estelle M.;
"Plant development is regulated by a family of auxin receptor F box proteins.";
Dev. Cell 9:109-119(2005).
[13]
FUNCTION, AND INTERACTION WITH AUX/IAA PROTEINS AND AUXIN.
DOI=10.1038/nature03543; PubMed=15917797 [NCBI, ExPASy, EBI, Israel, Japan]
Dharmasiri N., Dharmasiri S., Estelle M.;
"The F-box protein TIR1 is an auxin receptor.";
Nature 435:441-445(2005).
[14]
FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN, AND MUTAGENESIS OF PRO-10; VAL-33 AND LYS-35.
DOI=10.1038/nature03542; PubMed=15917798 [NCBI, ExPASy, EBI, Israel, Japan]
Kepinski S., Leyser O.;
"The Arabidopsis F-box protein TIR1 is an auxin receptor.";
Nature 435:446-451(2005).
[15]
FUNCTION, AND INDUCTION.
DOI=10.1126/science.1126088; PubMed=16627744 [NCBI, ExPASy, EBI, Israel, Japan]
Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M., Voinnet O., Jones J.D.G.;
"A plant miRNA contributes to antibacterial resistance by repressing auxin signaling.";
Science 312:436-439(2006).
Comments
  • FUNCTION: Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. The SCF(TIR1) E3 ubiquitin ligase complex is involved in auxin-mediated signaling pathway that regulate root and hypocotyl growth, lateral root formation, cell elongation, and gravitropism. Appears to allow pericycle cells to overcome G2 arrest prior to lateral root development. Plays a role in ethylene signaling in roots. Confers sensitivity to the virulent bacterial pathogen P.syringae.
  • PATHWAY: Protein degradation; protein ubiquitination.
  • SUBUNIT: Interacts with auxin. Part of a SCF E3 ubiquitin ligase complex SCF(TIR1) composed of SKP1, CUL1, RBX1 and TIR1. SCF(TIR1) interacts with the COP9 signalosome (CSN) complex. Interacts with Aux/IAA proteins (IAA3, IAA7, IAA12 and IAA17) in an auxin-dependent manner. The interaction with IAA3, a negative regulator of auxin responses, is promoted by auxin, but repressed by juglon (5-hydroxy-1,4-naphthoquinone).
  • INTERACTION:
    P49677:IAA1; NbExp=1; IntAct=EBI-307183, EBI-630505;
    Q38830:IAA12; NbExp=1; IntAct=EBI-307183, EBI-617608;
    Q38822:IAA3; NbExp=1; IntAct=EBI-307183, EBI-307174;
    Q940X7:RBX1A; NbExp=1; IntAct=EBI-307183, EBI-532404;
    Q9SDY5:RCE1; NbExp=1; IntAct=EBI-307183, EBI-595116;
    Q39255:SKP1A; NbExp=4; IntAct=EBI-307183, EBI-532357;
    Q9FHW7:SKP1B; NbExp=4; IntAct=EBI-307183, EBI-604076;
  • SUBCELLULAR LOCATION: Nucleus.
  • TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers. In adult plants, mostly expressed in floral stigma, anther filaments, abscission zones and vascular tissues.
  • DEVELOPMENTAL STAGE: Abundant expression in developing embryos. In young seedlings, expressed in root apical meristem, and expanding cotyledons and hypocotyls. In older seedlings, still expressed in root apical meristems, but also in lateral root primordia, stipules, shoot apical meristem and vascular tissues.
  • INDUCTION: Repressed by miR393a (microRNA) in response to flg-22 (flagellin-derived peptide 22).
  • DOMAIN: The F-box is necessary for the interaction with SKP1.
  • MISCELLANEOUS: Plant lacking TIR1 are deficient in a variety of auxin-regulated growth processes including lateral root formation, and hypocotyl and cell elongation.
  • SIMILARITY: Contains 1 F-box domain.
  • SIMILARITY: Contains 16 LRR (leucine-rich) repeats.
  • WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants; URL="http://plantsubq.genomics.purdue.edu/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF005047; AAB69175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005048; AAB69176.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163816; CAB87743.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT001946; AAN71945.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK220790; BAD94031.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48087; T48087.
RefSeq NP_567135.1; -.
UniGene At.25594
3D structure databases
PDB
2P1M; X-ray; 1.80 A; B=1-594.[ExPASy / RCSB / EBI]
2P1N; X-ray; 2.50 A; B/E=1-594.[ExPASy / RCSB / EBI]
2P1O; X-ray; 1.90 A; B=1-594.[ExPASy / RCSB / EBI]
2P1P; X-ray; 2.21 A; B=1-594.[ExPASy / RCSB / EBI]
2P1Q; X-ray; 1.91 A; B=1-594.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2P1M; -.
2P1N; -.
2P1O; -.
2P1P; -.
2P1Q; -.
ModBase Q570C0.
Protein-protein interaction databases
IntAct Q570C0; -.
Organism-specific databases
GeneFarm 4958; -.
TAIR At3g62980; -.
Gene expression databases
GermOnline AT3G62980; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
IPR001611; LRR.
IPR013101; LRR_2.
Graphical view of domain structure.
Pfam PF00646; F-box; 1.
PF00560; LRR_1; 1.
PF07723; LRR_2; 1.
Pfam graphical view of domain structure.
SMART SM00256; FBOX; 1.
SMART graphical view of domain structure.
PROSITE PS50181; FBOX; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q570C0.
Genome annotation databases
GeneID 825473; -.
GenomeReviews BA000014_GR; AT3G62980.
KEGG ath:AT3G62980; -.
NMPDR fig|3702.1.peg.17686; -.
Other
ProtoNet Q570C0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Auxin signaling pathway; Cell cycle; Complete proteome; Developmental protein; Ethylene signaling pathway; Leucine-rich repeat; Nucleus; Plant defense; Repeat; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   594  594     Protein TRANSPORT INHIBITOR RESPONSE 1. PRO_0000119965
DOMAIN   3    50  48     F-box. 
REPEAT   96   113  18     LRR 1. 
REPEAT   114   146  33     LRR 2. 
REPEAT   147   174  28     LRR 3. 
REPEAT   175   201  27     LRR 4. 
REPEAT   202   228  27     LRR 5. 
REPEAT   229   255  27     LRR 6. 
REPEAT   256   279  24     LRR 7. 
REPEAT   280   304  25     LRR 8. 
REPEAT   305   328  24     LRR 9. 
REPEAT   329   362  34     LRR 10. 
REPEAT   363   387  25     LRR 11. 
REPEAT   388   422  35     LRR 12. 
REPEAT   423   449  27     LRR 13. 
REPEAT   450   471  22     LRR 14. 
REPEAT   472   493  22     LRR 15. 
REPEAT   494   517  24     LRR 16. 
MUTAGEN   10    10        P->A: Abolishes SCF(TIR1) complex formation, altered auxin-mediated response and reduced affinity for auxin. 
MUTAGEN   33    33        V->A: No affinity for auxin. 
MUTAGEN   35    35        K->A: No affinity for auxin. 
MUTAGEN   147   147        G->D: In tir1-1; insensitive to auxin ubiquitously and to ethylene in roots only. 
MUTAGEN   441   441        G->D: In tir1-2; insensitive to auxin. 
MUTAGEN   574   594        Missing: In tir1-101/wei1; insensitive to auxin ubiquitously and to ethylene in roots only. 
CONFLICT   490   490        D -> E (in Ref. 4; BAD94031). 
CONFLICT   568   568        D -> G (in Ref. 4; BAD94031). 
HELIX   11    19  9      
HELIX   24    31  8      
HELIX   35    44  10      
STRAND   47    52  6      
HELIX   58    64  7      
STRAND   70    74  5      
HELIX   78    82  5      
HELIX   94   103  10      
STRAND   109   114  6      
HELIX   119   128  10      
STRAND   134   139  6      
STRAND   141   144  4      
HELIX   145   154  10      
STRAND   160   162  3      
STRAND   167   169  3      
HELIX   173   178  6      
STRAND   188   190  3      
HELIX   200   209  10      
STRAND   215   217  3      
HELIX   224   233  10      
STRAND   238   241  4      
HELIX   251   262  12      
STRAND   269   271  3      
HELIX   278   284  7      
HELIX   285   288  4      
STRAND   293   295  3      
HELIX   303   310  8      
STRAND   318   322  5      
HELIX   323   325  3      
HELIX   326   336  11      
STRAND   342   346  5      
HELIX   361   370  10      
STRAND   376   382  7      
HELIX   386   395  10      
STRAND   401   408  8      
TURN   414   416  3      
HELIX   421   430  10      
STRAND   436   438  3      
HELIX   445   454  10      
STRAND   460   465  6      
HELIX   470   479  10      
STRAND   485   490  6      
HELIX   495   500  6      
HELIX   502   507  6      
STRAND   508   516  9      
HELIX   520   529  10      
STRAND   533   538  6      
STRAND   540   542  3      
HELIX   544   546  3      
STRAND   554   560  7      
STRAND   573   575  3      
Sequence information
Length: 594 AA [This is the length of the unprocessed precursor] Molecular weight: 66799 Da [This is the MW of the unprocessed precursor] CRC64: 9E19ED5DABF40D07 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI GNCYAVSPAT 

        70         80         90        100        110        120 
VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM SSSYTWLEEI RLKRMVVTDD 

       130        140        150        160        170        180 
CLELIAKSFK NFKVLVLSSC EGFSTDGLAA IAATCRNLKE LDLRESDVDD VSGHWLSHFP 

       190        200        210        220        230        240 
DTYTSLVSLN ISCLASEVSF SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL 

       250        260        270        280        290        300 
GTGGYTAEVR PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT 

       310        320        330        340        350        360 
VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP FVMEPNVALT 

       370        380        390        400        410        420 
EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT RFRLCIIEPK APDYLTLEPL 

       430        440        450        460        470        480 
DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC 

       490        500        510        520        530        540 
DSLRKLEIRD CPFGDKALLA NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE 

       550        560        570        580        590 
RGAPDSRPES CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL 

Q570C0 in FASTA format

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