TOR1_ARATH
ID TOR1_ARATH Reviewed; 864 AA.
AC Q9T041; Q68VK4; Q84MA0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Microtubule-associated protein TORTIFOLIA1 {ECO:0000303|PubMed:15324671};
DE AltName: Full=Microtubule-associated protein SPIRAL2 {ECO:0000303|PubMed:15557095};
DE AltName: Full=Protein CONVOLUTA;
GN Name=TOR1 {ECO:0000303|PubMed:15324671};
GN Synonyms=CN, SPR2 {ECO:0000303|PubMed:15557095};
GN OrderedLocusNames=At4g27060 {ECO:0000312|Araport:AT4G27060};
GN ORFNames=T24A18.10;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GENE FAMILY.
RX PubMed=15324671; DOI=10.1016/j.cub.2004.08.033;
RA Buschmann H., Fabri C.O., Hauptmann M., Hutzler P., Laux T., Lloyd C.W.,
RA Schaeffner A.R.;
RT "Helical growth of the Arabidopsis mutant tortifolia1 reveals a plant-
RT specific microtubule-associated protein.";
RL Curr. Biol. 14:1515-1521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GENE FAMILY.
RX PubMed=15557095; DOI=10.1104/pp.104.051748;
RA Shoji T., Narita N.N., Hayashi K., Asada J., Hamada T., Sonobe S.,
RA Nakajima K., Hashimoto T.;
RT "Plant-specific microtubule-associated protein SPIRAL2 is required for
RT anisotropic growth in Arabidopsis.";
RL Plant Physiol. 136:3933-3944(2004).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-864.
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18577573; DOI=10.1242/jcs.030221;
RA Yao M., Wakamatsu Y., Itoh T.J., Shoji T., Hashimoto T.;
RT "Arabidopsis SPIRAL2 promotes uninterrupted microtubule growth by
RT suppressing the pause state of microtubule dynamics.";
RL J. Cell Sci. 121:2372-2381(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP INTERACTION WITH WAV3.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22122664; DOI=10.1111/j.1365-313x.2011.04870.x;
RA Sakai T., Mochizuki S., Haga K., Uehara Y., Suzuki A., Harada A., Wada T.,
RA Ishiguro S., Okada K.;
RT "The wavy growth 3 E3 ligase family controls the gravitropic response in
RT Arabidopsis roots.";
RL Plant J. 70:303-314(2012).
RN [10]
RP FUNCTION.
RX PubMed=24055158; DOI=10.1016/j.cub.2013.07.061;
RA Wightman R., Chomicki G., Kumar M., Carr P., Turner S.R.;
RT "SPIRAL2 determines plant microtubule organization by modulating
RT microtubule severing.";
RL Curr. Biol. 23:1902-1907(2013).
CC -!- FUNCTION: Plant-specific microtubule-associated protein (MAP) that
CC regulates the orientation of cortical microtubules and the direction of
CC organ growth (PubMed:18577573). Determines microtubule organization by
CC modulating microtubule severing (PubMed:24055158).
CC {ECO:0000269|PubMed:18577573, ECO:0000269|PubMed:24055158}.
CC -!- SUBUNIT: Interacts with WAV3. {ECO:0000269|PubMed:22122664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15324671, ECO:0000269|PubMed:15557095,
CC ECO:0000269|PubMed:18577573}. Note=Bound to microtubules.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, stems, flowers,
CC siliques, inflorescences, petioles, cotyledons, and leaves.
CC Particularly present in root tips and shoot meristems.
CC {ECO:0000269|PubMed:15324671, ECO:0000269|PubMed:15557095,
CC ECO:0000269|PubMed:18577573}.
CC -!- DISRUPTION PHENOTYPE: Right-handed twisting of petioles. Enhanced
CC twisting when associated with SP2L disruption.
CC {ECO:0000269|PubMed:18577573}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79561.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB176521; BAD54701.1; -; mRNA.
DR EMBL; AJ249836; CAC80696.2; -; mRNA.
DR EMBL; AL035680; CAB38836.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79561.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85295.1; -; Genomic_DNA.
DR EMBL; BT006451; AAP21259.1; -; mRNA.
DR PIR; T06036; T06036.
DR RefSeq; NP_194436.2; NM_118840.5.
DR AlphaFoldDB; Q9T041; -.
DR SMR; Q9T041; -.
DR BioGRID; 14101; 5.
DR IntAct; Q9T041; 4.
DR STRING; 3702.AT4G27060.1; -.
DR iPTMnet; Q9T041; -.
DR PaxDb; Q9T041; -.
DR PRIDE; Q9T041; -.
DR ProteomicsDB; 228290; -.
DR EnsemblPlants; AT4G27060.1; AT4G27060.1; AT4G27060.
DR GeneID; 828814; -.
DR Gramene; AT4G27060.1; AT4G27060.1; AT4G27060.
DR KEGG; ath:AT4G27060; -.
DR Araport; AT4G27060; -.
DR TAIR; locus:2136467; AT4G27060.
DR eggNOG; ENOG502QUFS; Eukaryota.
DR HOGENOM; CLU_019435_0_0_1; -.
DR InParanoid; Q9T041; -.
DR OMA; GKYNGRA; -.
DR OrthoDB; 142050at2759; -.
DR PhylomeDB; Q9T041; -.
DR PRO; PR:Q9T041; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T041; baseline and differential.
DR Genevisible; Q9T041; AT.
DR GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0010031; P:circumnutation; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033337; TORTIFOLIA1/SPIRAL2-like.
DR PANTHER; PTHR31355; PTHR31355; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..864
FT /note="Microtubule-associated protein TORTIFOLIA1"
FT /id="PRO_0000076255"
FT REPEAT 76..113
FT /note="HEAT 1"
FT REPEAT 117..154
FT /note="HEAT 2"
FT REPEAT 167..204
FT /note="HEAT 3"
FT REPEAT 208..245
FT /note="HEAT 4"
FT REPEAT 248..285
FT /note="HEAT 5"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 508..561
FT /evidence="ECO:0000255"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 864 AA; 94004 MW; 4A6191A5D90E71A4 CRC64;
MSTPTTSGSA AKPTRPARSS SLATRSCSNS GSLTSFQAMV ELKQKILTSI SKLADRDTYQ
IAVEDLEKTI QSLTPETLPM FLNCLYDSCS DPKPAVKKEC LHLLSYVCSL HCDSTAAHLT
KIIAQIVKRL KDSDSGVRDA CRDTIGALSG IYLKGKEEGT NTGSASLAVG LFVKPLFEAM
GEQNKVVQSG ASMCMARMVE SAASPPVTSF QKLCPRICKL LSNSSFLAKA SLLPVVSSLS
QVGAIAPQSL ESLLESIHDC LGSTDWVTRK AAAETLTALA SHSSGLIKEK TDSTITVLET
CRFDKIKPVR ESVTEALQLW KKISGKYVDG ASDDSKLSAS EQLGSEKNGE KRSNLADLMK
KEASDGSTLS PDSASKGKGC FPEKAVGLLK KKAPVLSDKD FNPEFFQRLE RRQSVEVVVP
RRCKNNDEEE SGLDDLNAMG SSNRLKNTQA DDKQVKGRFD GNGSQARTSG DDKAGVVNGK
ETPGHHAPVS NTDNQSEGSF TSNRGNWSAI QRQLLQLERQ QTNLMNMLQE FIGGSHDSMV
TLEGRVRGLE RIVEDMARDL SISSGRRANL TAGFGKYNSF ANYPTGKYNG RAPGERGSQT
DGAMRGRMWN SDMADDWFIP PHAASRNGQA GPRRSPRSEQ YENEHMGNGR RGWDNKASGT
IRFGEGPSAR SVWQASKDEA TLEAIRVAGE DGAVPRPTRV AVAPEAEAMG DDDNEGQERD
PIWVSWSNAM HSLRVGDIDA AYAEVLCAGD QHLVIKLMDK TGPSLDQMSN EIANEALNFI
SQFLLDHSLY DICLSWSQQL LELVLQDGAD TFGVPMELKT EILYNLQDAC STMDPPEDWE
GPAPEQLVVQ LASVWEIDLQ QFDK
