TIR1L_ARATH
ID TIR1L_ARATH Reviewed; 619 AA.
AC Q9LTX2; Q56YW2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transport inhibitor response 1-like protein;
DE Short=TIR1-like protein;
GN OrderedLocusNames=At5g49980; ORFNames=K9P8.12;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 552-619.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. May
CC interact with auxin and auxin-responsive proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The F-box is necessary for the interaction with SKP1.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a structural
CC cofactor. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93754.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB024032; BAA97019.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95880.1; -; Genomic_DNA.
DR EMBL; AY056431; AAL08287.1; -; mRNA.
DR EMBL; AY139774; AAM98092.1; -; mRNA.
DR EMBL; BT004536; AAO42782.1; -; mRNA.
DR EMBL; AK221208; BAD93754.1; ALT_INIT; mRNA.
DR RefSeq; NP_568718.1; NM_124377.3.
DR AlphaFoldDB; Q9LTX2; -.
DR SMR; Q9LTX2; -.
DR BioGRID; 20308; 5.
DR IntAct; Q9LTX2; 1.
DR STRING; 3702.AT5G49980.1; -.
DR iPTMnet; Q9LTX2; -.
DR PaxDb; Q9LTX2; -.
DR PRIDE; Q9LTX2; -.
DR ProteomicsDB; 234304; -.
DR EnsemblPlants; AT5G49980.1; AT5G49980.1; AT5G49980.
DR GeneID; 835062; -.
DR Gramene; AT5G49980.1; AT5G49980.1; AT5G49980.
DR KEGG; ath:AT5G49980; -.
DR Araport; AT5G49980; -.
DR TAIR; locus:2158824; AT5G49980.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q9LTX2; -.
DR OMA; MSKNCSD; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q9LTX2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LTX2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTX2; baseline and differential.
DR Genevisible; Q9LTX2; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0010011; F:auxin binding; ISS:UniProtKB.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; ISS:UniProtKB.
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 Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
DR InterPro; IPR036047; F-box-like_dom_sf.
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; SM00367; LRR_CC; 5.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..619
FT /note="Transport inhibitor response 1-like protein"
FT /id="PRO_0000285579"
FT DOMAIN 54..97
FT /note="F-box"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..127
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 394..399
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 451..455
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 510..511
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 447..449
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 530..531
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 426
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 535
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 619 AA; 69317 MW; D0614AF071EE4FD2 CRC64;
MTQDRSEMSE DDDDQQSPPL DLPSTAIADP CSSSSSPNKS RNCISNSQTF PDHVLENVLE
NVLQFLDSRC DRNAASLVCK SWWRVEALTR SEVFIGNCYA LSPARLTQRF KRVRSLVLKG
KPRFADFNLM PPDWGANFAP WVSTMAQAYP CLEKVDLKRM FVTDDDLALL ADSFPGFKEL
ILVCCEGFGT SGISIVANKC RKLKVLDLIE SEVTDDEVDW ISCFPEDVTC LESLAFDCVE
APINFKALEG LVARSPFLKK LRLNRFVSLV ELHRLLLGAP QLTSLGTGSF SHDEEPQSEQ
EPDYAAAFRA CKSVVCLSGF RELMPEYLPA IFPVCANLTS LNFSYANISP DMFKPIILNC
HKLQVFWALD SICDEGLQAV AATCKELREL RIFPFDPRED SEGPVSELGL QAISEGCRKL
ESILYFCQRM TNAAVIAMSE NCPELTVFRL CIMGRHRPDH VTGKPMDEGF GAIVKNCKKL
TRLAVSGLLT DQAFRYMGEY GKLVRTLSVA FAGDSDMALR HVLEGCPRLQ KLEIRDSPFG
DVALRSGMHR YYNMRFVWMS ACSLSKGCCK DIARAMPNLV VEVIGSDDDD DNRDYVETLY
MYRSLDGPRN DAPKFVTIL
