TRN1_ARATH
ID TRN1_ARATH Reviewed; 1380 AA.
AC Q9FJ57;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein TORNADO 1;
DE AltName: Full=Protein LOPPED 1;
GN Name=TRN1; Synonyms=LOP1; OrderedLocusNames=At5g55540; ORFNames=MTE17.26;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8674420; DOI=10.1242/dev.122.6.1811;
RA Carland F.M., McHale N.A.;
RT "LOP1: a gene involved in auxin transport and vascular patterning in
RT Arabidopsis.";
RL Development 122:1811-1819(1996).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=9003284; DOI=10.1007/s004380050293;
RA Cnops G., den Boer B., Gerats A., Van Montagu M., Van Lijsebettens M.;
RT "Chromosome landing at the Arabidopsis TORNADO1 locus using an AFLP-based
RT strategy.";
RL Mol. Gen. Genet. 253:32-41(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=10887093; DOI=10.1242/dev.127.15.3385;
RA Cnops G., Wang X., Linstead P., Van Montagu M., Van Lijsebettens M.,
RA Dolan L.;
RT "Tornado1 and tornado2 are required for the specification of radial and
RT circumferential pattern in the Arabidopsis root.";
RL Development 127:3385-3394(2000).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16531491; DOI=10.1105/tpc.105.040568;
RA Cnops G., Neyt P., Raes J., Petrarulo M., Nelissen H., Malenica N.,
RA Luschnig C., Tietz O., Ditengou F., Palme K., Azmi A., Prinsen E.,
RA Van Lijsebettens M.;
RT "The TORNADO1 and TORNADO2 genes function in several patterning processes
RT during early leaf development in Arabidopsis thaliana.";
RL Plant Cell 18:852-866(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21658947; DOI=10.1016/j.cub.2011.05.015;
RA Lieber D., Lora J., Schrempp S., Lenhard M., Laux T.;
RT "Arabidopsis WIH1 and WIH2 genes act in the transition from somatic to
RT reproductive cell fate.";
RL Curr. Biol. 21:1009-1017(2011).
CC -!- FUNCTION: Involved in the basipetal transport of auxin (IAA) that
CC modulates growth and organs organization. Required for initial
CC divisions in the epidermal/lateral root cap leading to the formation of
CC epidermal cells and a clone of lateral root cap cells, as well as for
CC the maintenance of the radial pattern of cell specification in the
CC root, thus regulating the distinction between the lateral root cap and
CC epidermis. {ECO:0000269|PubMed:10887093, ECO:0000269|PubMed:16531491,
CC ECO:0000269|PubMed:8674420, ECO:0000269|PubMed:9003284}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems and
CC flowers. Present in ovules, prominently in nucellus and integuments.
CC {ECO:0000269|PubMed:16531491, ECO:0000269|PubMed:21658947}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the shoot apical meristem
CC (SAM) and the young leaf primordia. Also detected in the lamina of the
CC cotyledons, especially in the mesophyll and vascular bundles.
CC {ECO:0000269|PubMed:16531491}.
CC -!- DISRUPTION PHENOTYPE: Severe dwarfism combined with twisted and
CC malformed organs, and sterility. Loss of initial meristematic divisions
CC in the epidermal/lateral root cap. Defection in basipetal transport of
CC auxin (IAA) leading to several development aberrations.
CC {ECO:0000269|PubMed:10887093, ECO:0000269|PubMed:16531491,
CC ECO:0000269|PubMed:8674420, ECO:0000269|PubMed:9003284}.
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DR EMBL; AB015479; BAB08571.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96644.1; -; Genomic_DNA.
DR RefSeq; NP_200365.1; NM_124936.3.
DR AlphaFoldDB; Q9FJ57; -.
DR SMR; Q9FJ57; -.
DR STRING; 3702.AT5G55540.1; -.
DR PaxDb; Q9FJ57; -.
DR PRIDE; Q9FJ57; -.
DR ProteomicsDB; 232374; -.
DR EnsemblPlants; AT5G55540.1; AT5G55540.1; AT5G55540.
DR GeneID; 835648; -.
DR Gramene; AT5G55540.1; AT5G55540.1; AT5G55540.
DR KEGG; ath:AT5G55540; -.
DR Araport; AT5G55540; -.
DR TAIR; locus:2173952; AT5G55540.
DR eggNOG; KOG4308; Eukaryota.
DR HOGENOM; CLU_255815_0_0_1; -.
DR InParanoid; Q9FJ57; -.
DR OMA; IIFFEEL; -.
DR OrthoDB; 63138at2759; -.
DR PhylomeDB; Q9FJ57; -.
DR PRO; PR:Q9FJ57; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ57; baseline and differential.
DR Genevisible; Q9FJ57; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009926; P:auxin polar transport; IDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010540; P:basipetal auxin transport; IMP:UniProtKB.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009956; P:radial pattern formation; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR032171; COR.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16095; COR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Developmental protein; GTP-binding; Hydrolase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1380
FT /note="Protein TORNADO 1"
FT /id="PRO_0000421040"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 26..46
FT /note="LRR 1"
FT REPEAT 47..70
FT /note="LRR 2"
FT REPEAT 105..132
FT /note="LRR 3"
FT REPEAT 161..184
FT /note="LRR 4"
FT REPEAT 266..289
FT /note="LRR 5"
FT REPEAT 299..322
FT /note="LRR 6"
FT REPEAT 323..346
FT /note="LRR 7"
FT REPEAT 348..371
FT /note="LRR 8"
FT REPEAT 446..472
FT /note="LRR 9"
FT REPEAT 476..502
FT /note="LRR 10"
FT DOMAIN 493..702
FT /note="Roc"
FT REPEAT 640..665
FT /note="LRR 11"
FT REPEAT 688..712
FT /note="LRR 12"
FT REPEAT 799..826
FT /note="LRR 13"
FT REPEAT 1023..1046
FT /note="LRR 14"
FT REPEAT 1131..1154
FT /note="LRR 15"
FT REPEAT 1229..1254
FT /note="LRR 16"
FT BINDING 506..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 567..571
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 641..644
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
SQ SEQUENCE 1380 AA; 156947 MW; C853381BB96E6CE3 CRC64;
MESEPDQSFK DLSWFLQAIK DPQQTFFNLQ TLSFSSSGNT THCQLITESS MNINVTRDNL
TSLSQIFIEL ATSLETQTSL RNLEFEGIFW EIELLQSLGL LLDNTSKIKQ LAFRKNRFSE
QCLNELSEIL KRNRFLKEVM FLESSIGYRG ATLLGSALQV NDSLEELQIW EDSIGSKGAE
ELSRMIEMNS SLKLFSIFDS SPFTATPLIS AVLGMNREME VHMWSGDHKR DRSLKLVEFL
PESKTLRIYQ IDISGSCRVA AALGMNTTVR SLDMTGAKLN SRWAKEFRWV LEQNKTLREV
KLSKTGLKDK AVVYIAAGLF KNKSLQSLYV DGNRFGSVGV EDLLCPLSRF SALQLQANIT
LRSIVFGGSN TKIGRDGLTA VLKMVTTNET VVHLGIHDDA SLGPDDFIHI FKSLQKNASL
RRFSLQGCKG VRGDRVLEAI TETLQINPLI EEIDLARTPL QDSGKADEIY QKLGHNGRKI
DEAETDDSLK DMPLTEPKSV RAFLCGQNYA GKTTLCNSIL QSSSASGFPY VENVRNLMNP
VEQVVKTVGG MKIKTFKDEE TKISMWNLAG QHEFFALHDL MFPSPCFFLI VLSLFRKPSN
KEPKTPAEVE EELEYWLRFI VSNSRKAIQQ CMKPNVTIVL THSEKINLQS ESFQATVGCI
QRLRDKFQAL VEFYPTVFTV DARSSPSVSK LTHHIRMTSK AILQRVPRVY QLCNDIVQLL
SDWRSENSNK PIMRWKAFAD LCQFKVPSLR IKSRNENIQI VETRRHAIAT CLHQMGEVIY
FDDLGFLILD YEWFCGEVLT QLIKLDVRKQ STGERNGFVS RKELEKTLRS SLQSPIPGMT
SKVLEHFDAC DLVKMMKKVE LCYEQDPSSP DSSLLVPSIL EEGRGKTQKW QINTHDCVYS
GRHLQCDDSS HMFLTAGFFP RLQVHLHNRI MELKNQHGAT YSLEKYLIAI TIHGINIRVE
LGGQLGNYID VLACSSKSLT ETLRLIHQLI IPAIQSSCRG VILLEHIIRP QCVQDLTPPR
FRQSQFVSLH RLKEALSSVP AETMYDYQHT WDSVLDSGKT VLRAGFDLAR NLLSDDDFRE
VLQRRYHDLH NLAQELQVPT DENPEADNHV PVTNELEKVD PSFGGIAKGV EAVLQRLKII
EQEIRDLKQE IQGLRYYEHR LLIQLHHKVN YLVNYNVQMD ERKVPNMFYF IRAENYGRRL
ITSMVPGMVA LRIHMLCEFR REMHVVEDQL GCDVMQIDNQ AVKCLAPYMT NFMKLVTFAL
RIGANWAAGM GHMIPDLSHT IAHLANPAVM TGAAGAAGAI GVAAALGRNR GRDRDIQEQE
QRAAQQWLID YLREQTCSTG RDIAEKFGLW RVRYRDDGSI AWICKRHMIT RAHEVIQVPL
