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Protein TRANSPORT INHIBITOR RESPONSE 1 (Weak ethylene-insensitive protein 1)

 TIR1_ARATH              Reviewed;         594 AA.
Q570C0; A5YZP2; B2CVU0; O24660;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
22-NOV-2017, entry version 119.
RecName: Full=Protein TRANSPORT INHIBITOR RESPONSE 1;
AltName: Full=Weak ethylene-insensitive protein 1;
Name=TIR1; Synonyms=FBL1, WEI1; OrderedLocusNames=At3g62980;
ORFNames=T20O10.80;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION
PHENOTYPE, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-147 AND GLY-441.
PubMed=9436980; DOI=10.1101/gad.12.2.198;
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;
PubMed=11130713; DOI=10.1038/35048706;
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]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-380.
STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta,
cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0,
cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and
cv. Wassilewskija;
PubMed=17435248; DOI=10.1534/genetics.107.071928;
Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
"The genetic architecture of shoot branching in Arabidopsis thaliana:
a comparative assessment of candidate gene associations vs.
quantitative trait locus mapping.";
Genetics 176:1223-1236(2007).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 429-579.
STRAIN=cv. Ag-0, cv. An-1, cv. Bay-0, cv. Br-0, cv. C24, cv. Ct-1,
cv. Cvi-0, cv. Edi-0, cv. Ei-2, cv. Ga-0, cv. Gy-0, cv. Kas-2,
cv. Ll-0, cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3,
cv. Oy-0, cv. Sorbo, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, and
cv. Wt-5;
PubMed=18305205; DOI=10.1104/pp.108.116582;
Ehrenreich I.M., Purugganan M.D.;
"Sequence variation of microRNAs and their binding sites in
Arabidopsis.";
Plant Physiol. 146:1974-1982(2008).
[8]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH
SKP1A; SKP1B AND CUL1, DOMAIN, AND MUTAGENESIS OF PRO-10.
PubMed=10398681; DOI=10.1101/gad.13.13.1678;
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).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11077244; DOI=10.1016/S1360-1385(00)01769-6;
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
[10]
INTERACTION WITH IAA7 AND IAA17.
PubMed=11713520; DOI=10.1038/35104500;
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).
[11]
INTERACTION WITH THE CSN COMPLEX.
PubMed=11337587; DOI=10.1126/science.1059776;
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).
[12]
INTERACTION WITH RBX1.
PubMed=12215511; DOI=10.1105/tpc.003178;
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).
[13]
INTERACTION WITH IAA3.
PubMed=14617065; DOI=10.1046/j.1365-313X.2003.01909.x;
Tian Q., Nagpal P., Reed J.W.;
"Regulation of Arabidopsis SHY2/IAA3 protein turnover.";
Plant J. 36:643-651(2003).
[14]
FUNCTION, AND MUTAGENESIS OF 574-TRP--LEU-594.
PubMed=12606727; DOI=10.1073/pnas.0438070100;
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).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IAA12; IAA7 AND
SKP1A/ASK1.
PubMed=15992545; DOI=10.1016/j.devcel.2005.05.014;
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).
[16]
FUNCTION, AND INTERACTION WITH AUX/IAA PROTEINS AND AUXIN.
PubMed=15917797; DOI=10.1038/nature03543;
Dharmasiri N., Dharmasiri S., Estelle M.;
"The F-box protein TIR1 is an auxin receptor.";
Nature 435:441-445(2005).
[17]
FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN, AND MUTAGENESIS
OF PRO-10; VAL-33 AND LYS-35.
PubMed=15917798; DOI=10.1038/nature03542;
Kepinski S., Leyser O.;
"The Arabidopsis F-box protein TIR1 is an auxin receptor.";
Nature 435:446-451(2005).
[18]
FUNCTION, AND INDUCTION.
PubMed=16627744; DOI=10.1126/science.1126088;
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).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SKP1A; AUXIN;
AUX/IAA POLYPEPTIDE SUBSTRATE; AUXIN ANALOGS AND MYO-INOSITOL
HEXAKISPHOSPHATE.
PubMed=17410169; DOI=10.1038/nature05731;
Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C.,
Robinson C.V., Estelle M., Zheng N.;
"Mechanism of auxin perception by the TIR1 ubiquitin ligase.";
Nature 446:640-645(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA
POLYPEPTIDE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND MYO-INOSITOL
HEXAKISPHOSPHATE, AND FUNCTION.
PubMed=18391211; DOI=10.1073/pnas.0711146105;
Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S.,
Nozaki H.;
"Small-molecule agonists and antagonists of F-box protein-substrate
interactions in auxin perception and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008).
-!- 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. {ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:12606727, ECO:0000269|PubMed:15917797,
ECO:0000269|PubMed:15917798, ECO:0000269|PubMed:15992545,
ECO:0000269|PubMed:16627744, ECO:0000269|PubMed:18391211,
ECO:0000269|PubMed:9436980}.
-!- PATHWAY: Protein modification; 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). Interactions with auxin-responsive
proteins is inactivated by auxin antagonists.
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:11337587,
ECO:0000269|PubMed:11713520, ECO:0000269|PubMed:12215511,
ECO:0000269|PubMed:14617065, ECO:0000269|PubMed:15917797,
ECO:0000269|PubMed:15917798, ECO:0000269|PubMed:15992545,
ECO:0000269|PubMed:17410169, ECO:0000269|PubMed:18391211}.
-!- INTERACTION:
P93830:IAA17; NbExp=2; IntAct=EBI-307183, EBI-632243;
Q38822:IAA3; NbExp=2; IntAct=EBI-307183, EBI-307174;
Q38825:IAA7; NbExp=8; IntAct=EBI-307183, EBI-602959;
Q39255:SKP1A; NbExp=8; IntAct=EBI-307183, EBI-532357;
Q9FHW7:SKP1B; NbExp=4; IntAct=EBI-307183, EBI-604076;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
In adult plants, mostly expressed in floral stigma, anther
filaments, abscission zones and vascular tissues.
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:9436980}.
-!- 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.
{ECO:0000269|PubMed:10398681}.
-!- INDUCTION: Repressed by miR393a (microRNA) in response to flg-22
(flagellin-derived peptide 22). {ECO:0000269|PubMed:16627744}.
-!- DOMAIN: The F-box is necessary for the interaction with SKP1.
{ECO:0000269|PubMed:10398681}.
-!- DISRUPTION PHENOTYPE: Plant are deficient in a variety of auxin-
regulated growth processes including lateral root formation, and
hypocotyl and cell elongation. {ECO:0000269|PubMed:9436980}.
-!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a
structural cofactor.
-!- SEQUENCE CAUTION:
Sequence=BAD94031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF005047; AAB69175.1; -; Genomic_DNA.
EMBL; AF005048; AAB69176.1; -; mRNA.
EMBL; AL163816; CAB87743.1; -; Genomic_DNA.
EMBL; CP002686; AEE80419.1; -; Genomic_DNA.
EMBL; BT001946; AAN71945.1; -; mRNA.
EMBL; EF598824; ABR04117.1; -; Genomic_DNA.
EMBL; EF598825; ABR04118.1; -; Genomic_DNA.
EMBL; EF598826; ABR04119.1; -; Genomic_DNA.
EMBL; EF598827; ABR04120.1; -; Genomic_DNA.
EMBL; EF598828; ABR04121.1; -; Genomic_DNA.
EMBL; EF598829; ABR04122.1; -; Genomic_DNA.
EMBL; EF598830; ABR04123.1; -; Genomic_DNA.
EMBL; EF598831; ABR04124.1; -; Genomic_DNA.
EMBL; EF598832; ABR04125.1; -; Genomic_DNA.
EMBL; EF598833; ABR04126.1; -; Genomic_DNA.
EMBL; EF598834; ABR04127.1; -; Genomic_DNA.
EMBL; EF598835; ABR04128.1; -; Genomic_DNA.
EMBL; EF598836; ABR04129.1; -; Genomic_DNA.
EMBL; EF598837; ABR04130.1; -; Genomic_DNA.
EMBL; EF598838; ABR04131.1; -; Genomic_DNA.
EMBL; EF598839; ABR04132.1; -; Genomic_DNA.
EMBL; EF598840; ABR04133.1; -; Genomic_DNA.
EMBL; EF598841; ABR04134.1; -; Genomic_DNA.
EMBL; EF598842; ABR04135.1; -; Genomic_DNA.
EMBL; EF598843; ABR04136.1; -; Genomic_DNA.
EMBL; EF598844; ABR04137.1; -; Genomic_DNA.
EMBL; EF598845; ABR04138.1; -; Genomic_DNA.
EMBL; EF598846; ABR04139.1; -; Genomic_DNA.
EMBL; EF598847; ABR04140.1; -; Genomic_DNA.
EMBL; AK220790; BAD94031.1; ALT_INIT; mRNA.
EMBL; EU550991; ACB31753.1; -; Genomic_DNA.
EMBL; EU550992; ACB31754.1; -; Genomic_DNA.
EMBL; EU550993; ACB31755.1; -; Genomic_DNA.
EMBL; EU550994; ACB31756.1; -; Genomic_DNA.
EMBL; EU550995; ACB31757.1; -; Genomic_DNA.
EMBL; EU550996; ACB31758.1; -; Genomic_DNA.
EMBL; EU550997; ACB31759.1; -; Genomic_DNA.
EMBL; EU550998; ACB31760.1; -; Genomic_DNA.
EMBL; EU550999; ACB31761.1; -; Genomic_DNA.
EMBL; EU551000; ACB31762.1; -; Genomic_DNA.
EMBL; EU551001; ACB31763.1; -; Genomic_DNA.
EMBL; EU551002; ACB31764.1; -; Genomic_DNA.
EMBL; EU551003; ACB31765.1; -; Genomic_DNA.
EMBL; EU551004; ACB31766.1; -; Genomic_DNA.
EMBL; EU551005; ACB31767.1; -; Genomic_DNA.
EMBL; EU551006; ACB31768.1; -; Genomic_DNA.
EMBL; EU551007; ACB31769.1; -; Genomic_DNA.
EMBL; EU551008; ACB31770.1; -; Genomic_DNA.
EMBL; EU551009; ACB31771.1; -; Genomic_DNA.
EMBL; EU551010; ACB31772.1; -; Genomic_DNA.
EMBL; EU551011; ACB31773.1; -; Genomic_DNA.
EMBL; EU551012; ACB31774.1; -; Genomic_DNA.
EMBL; EU551013; ACB31775.1; -; Genomic_DNA.
EMBL; EU551014; ACB31776.1; -; Genomic_DNA.
PIR; T48087; T48087.
RefSeq; NP_567135.1; NM_116163.4.
UniGene; At.25594; -.
PDB; 2P1M; X-ray; 1.80 A; B=1-594.
PDB; 2P1N; X-ray; 2.50 A; B/E=1-594.
PDB; 2P1O; X-ray; 1.90 A; B=1-594.
PDB; 2P1P; X-ray; 2.21 A; B=1-594.
PDB; 2P1Q; X-ray; 1.91 A; B=1-594.
PDB; 3C6N; X-ray; 2.60 A; B=1-594.
PDB; 3C6O; X-ray; 2.70 A; B=1-594.
PDB; 3C6P; X-ray; 2.70 A; B=1-594.
PDBsum; 2P1M; -.
PDBsum; 2P1N; -.
PDBsum; 2P1O; -.
PDBsum; 2P1P; -.
PDBsum; 2P1Q; -.
PDBsum; 3C6N; -.
PDBsum; 3C6O; -.
PDBsum; 3C6P; -.
ProteinModelPortal; Q570C0; -.
SMR; Q570C0; -.
BioGrid; 10787; 21.
DIP; DIP-31740N; -.
ELM; Q570C0; -.
IntAct; Q570C0; 18.
STRING; 3702.AT3G62980.1; -.
iPTMnet; Q570C0; -.
PaxDb; Q570C0; -.
PRIDE; Q570C0; -.
EnsemblPlants; AT3G62980.1; AT3G62980.1; AT3G62980.
GeneID; 825473; -.
Gramene; AT3G62980.1; AT3G62980.1; AT3G62980.
KEGG; ath:AT3G62980; -.
Araport; AT3G62980; -.
TAIR; locus:2099237; AT3G62980.
eggNOG; KOG1947; Eukaryota.
eggNOG; ENOG410XQ54; LUCA.
HOGENOM; HOG000239805; -.
InParanoid; Q570C0; -.
KO; K14485; -.
OMA; WCRRRIF; -.
OrthoDB; EOG093606S7; -.
PhylomeDB; Q570C0; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q570C0; -.
PRO; PR:Q570C0; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q570C0; baseline and differential.
Genevisible; Q570C0; AT.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:TAIR.
GO; GO:0010011; F:auxin binding; IDA:UniProtKB.
GO; GO:0038198; F:auxin receptor activity; IDA:UniProtKB.
GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IC:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0010311; P:lateral root formation; IMP:TAIR.
GO; GO:0010152; P:pollen maturation; IGI:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0048443; P:stamen development; IGI:TAIR.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF12937; F-box-like; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00367; LRR_CC; 6.
SUPFAM; SSF81383; SSF81383; 1.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Cell cycle; Complete proteome;
Developmental protein; Ethylene signaling pathway; Nucleus;
Plant defense; Reference proteome; Ubl conjugation pathway.
CHAIN 1 594 Protein TRANSPORT INHIBITOR RESPONSE 1.
/FTId=PRO_0000119965.
DOMAIN 3 50 F-box.
REGION 81 82 Interaction with auxin-responsive
proteins.
REGION 113 114 Myo-inositol hexakisphosphate binding.
REGION 347 352 Interaction with auxin-responsive
proteins.
REGION 401 403 Myo-inositol hexakisphosphate binding.
REGION 403 404 Auxin binding.
REGION 405 409 Interaction with auxin-responsive
proteins.
REGION 438 439 Auxin binding.
REGION 464 465 Interaction with auxin-responsive
proteins.
REGION 484 485 Myo-inositol hexakisphosphate binding.
BINDING 74 74 Myo-inositol hexakisphosphate.
{ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211}.
BINDING 344 344 Myo-inositol hexakisphosphate.
{ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211}.
BINDING 436 436 Myo-inositol hexakisphosphate.
{ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211}.
BINDING 509 509 Myo-inositol hexakisphosphate.
{ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211}.
SITE 139 139 Interaction with auxin-responsive
proteins.
SITE 165 165 Interaction with auxin-responsive
proteins.
SITE 380 380 Interaction with auxin-responsive
proteins.
SITE 489 489 Interaction with auxin-responsive
proteins.
MUTAGEN 10 10 P->A: Abolishes SCF(TIR1) complex
formation, altered auxin-mediated
response and reduced affinity for auxin.
{ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:15917798}.
MUTAGEN 33 33 V->A: No affinity for auxin.
{ECO:0000269|PubMed:15917798}.
MUTAGEN 35 35 K->A: No affinity for auxin.
{ECO:0000269|PubMed:15917798}.
MUTAGEN 147 147 G->D: In tir1-1; insensitive to auxin
ubiquitously and to ethylene in roots
only. {ECO:0000269|PubMed:9436980}.
MUTAGEN 441 441 G->D: In tir1-2; insensitive to auxin.
{ECO:0000269|PubMed:9436980}.
MUTAGEN 574 594 Missing: In tir1-101/wei1; insensitive to
auxin ubiquitously and to ethylene in
roots only.
{ECO:0000269|PubMed:12606727}.
CONFLICT 490 490 D -> E (in Ref. 6; BAD94031).
{ECO:0000305}.
CONFLICT 568 568 D -> G (in Ref. 6; BAD94031).
{ECO:0000305}.
HELIX 11 19 {ECO:0000244|PDB:2P1M}.
HELIX 24 31 {ECO:0000244|PDB:2P1M}.
HELIX 35 44 {ECO:0000244|PDB:2P1M}.
STRAND 47 52 {ECO:0000244|PDB:2P1M}.
HELIX 53 55 {ECO:0000244|PDB:2P1N}.
HELIX 58 64 {ECO:0000244|PDB:2P1M}.
STRAND 70 74 {ECO:0000244|PDB:2P1M}.
HELIX 78 82 {ECO:0000244|PDB:2P1M}.
HELIX 94 103 {ECO:0000244|PDB:2P1M}.
STRAND 109 114 {ECO:0000244|PDB:2P1M}.
HELIX 119 128 {ECO:0000244|PDB:2P1M}.
STRAND 134 139 {ECO:0000244|PDB:2P1M}.
STRAND 141 144 {ECO:0000244|PDB:2P1M}.
HELIX 145 154 {ECO:0000244|PDB:2P1M}.
STRAND 160 162 {ECO:0000244|PDB:2P1M}.
STRAND 167 169 {ECO:0000244|PDB:2P1M}.
HELIX 173 178 {ECO:0000244|PDB:2P1M}.
STRAND 188 190 {ECO:0000244|PDB:2P1M}.
HELIX 200 209 {ECO:0000244|PDB:2P1M}.
STRAND 215 217 {ECO:0000244|PDB:2P1M}.
HELIX 224 233 {ECO:0000244|PDB:2P1M}.
STRAND 238 241 {ECO:0000244|PDB:2P1M}.
HELIX 251 262 {ECO:0000244|PDB:2P1M}.
STRAND 269 271 {ECO:0000244|PDB:2P1M}.
HELIX 278 284 {ECO:0000244|PDB:2P1M}.
HELIX 285 288 {ECO:0000244|PDB:2P1M}.
STRAND 293 295 {ECO:0000244|PDB:2P1M}.
HELIX 303 310 {ECO:0000244|PDB:2P1M}.
STRAND 318 322 {ECO:0000244|PDB:2P1M}.
HELIX 323 325 {ECO:0000244|PDB:2P1M}.
HELIX 326 336 {ECO:0000244|PDB:2P1M}.
STRAND 342 346 {ECO:0000244|PDB:2P1M}.
STRAND 350 352 {ECO:0000244|PDB:3C6N}.
HELIX 361 370 {ECO:0000244|PDB:2P1M}.
STRAND 376 382 {ECO:0000244|PDB:2P1M}.
HELIX 386 395 {ECO:0000244|PDB:2P1M}.
STRAND 401 408 {ECO:0000244|PDB:2P1M}.
TURN 414 416 {ECO:0000244|PDB:2P1M}.
HELIX 421 430 {ECO:0000244|PDB:2P1M}.
STRAND 436 438 {ECO:0000244|PDB:2P1M}.
HELIX 445 454 {ECO:0000244|PDB:2P1M}.
STRAND 460 465 {ECO:0000244|PDB:2P1M}.
HELIX 470 479 {ECO:0000244|PDB:2P1M}.
STRAND 485 490 {ECO:0000244|PDB:2P1M}.
HELIX 495 500 {ECO:0000244|PDB:2P1M}.
HELIX 502 507 {ECO:0000244|PDB:2P1M}.
STRAND 508 516 {ECO:0000244|PDB:2P1M}.
HELIX 520 529 {ECO:0000244|PDB:2P1M}.
STRAND 533 538 {ECO:0000244|PDB:2P1M}.
STRAND 540 542 {ECO:0000244|PDB:2P1M}.
HELIX 544 546 {ECO:0000244|PDB:2P1M}.
STRAND 554 560 {ECO:0000244|PDB:2P1M}.
STRAND 573 575 {ECO:0000244|PDB:2P1M}.
SEQUENCE 594 AA; 66799 MW; 9E19ED5DABF40D07 CRC64;
MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI GNCYAVSPAT
VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM SSSYTWLEEI RLKRMVVTDD
CLELIAKSFK NFKVLVLSSC EGFSTDGLAA IAATCRNLKE LDLRESDVDD VSGHWLSHFP
DTYTSLVSLN ISCLASEVSF SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL
GTGGYTAEVR PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT
VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP FVMEPNVALT
EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT RFRLCIIEPK APDYLTLEPL
DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC
DSLRKLEIRD CPFGDKALLA NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE
RGAPDSRPES CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL


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