TORL1_ARATH
ID TORL1_ARATH Reviewed; 821 AA.
AC F4I6M4; Q9C6J1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=TORTIFOLIA1-like protein 1 {ECO:0000303|PubMed:15324671};
DE AltName: Full=Microtubule-associated protein SPIRAL2-like {ECO:0000303|PubMed:18577573};
GN Name=TOR1L1 {ECO:0000303|PubMed:15324671};
GN Synonyms=SP2L {ECO:0000303|PubMed:18577573};
GN OrderedLocusNames=At1g50890 {ECO:0000312|Araport:AT1G50890};
GN ORFNames=F8A12.11 {ECO:0000312|EMBL:AAG50927.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
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).
CC -!- FUNCTION: Plant-specific microtubule-associated protein (MAP) that
CC regulates the orientation of cortical microtubules and the direction of
CC organ growth. {ECO:0000269|PubMed:18577573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18577573}. Note=Bound to microtubules.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, hypocotyls,
CC stems, flowers, siliques, cotyledons, and leaves. Particularly present
CC in hydathodes of cotyledons and root hairs.
CC {ECO:0000269|PubMed:18577573}.
CC -!- DISRUPTION PHENOTYPE: Right-handed twisting of petioles when associated
CC with SPR2 disruption. {ECO:0000269|PubMed:18577573}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC079284; AAG50927.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32598.1; -; Genomic_DNA.
DR PIR; H96545; H96545.
DR RefSeq; NP_175502.2; NM_103969.3.
DR AlphaFoldDB; F4I6M4; -.
DR SMR; F4I6M4; -.
DR iPTMnet; F4I6M4; -.
DR PaxDb; F4I6M4; -.
DR PRIDE; F4I6M4; -.
DR ProteomicsDB; 232554; -.
DR EnsemblPlants; AT1G50890.1; AT1G50890.1; AT1G50890.
DR GeneID; 841511; -.
DR Gramene; AT1G50890.1; AT1G50890.1; AT1G50890.
DR KEGG; ath:AT1G50890; -.
DR Araport; AT1G50890; -.
DR TAIR; locus:2036411; AT1G50890.
DR eggNOG; ENOG502QUFS; Eukaryota.
DR HOGENOM; CLU_019435_0_0_1; -.
DR InParanoid; F4I6M4; -.
DR OMA; SEQCMLE; -.
DR OrthoDB; 142050at2759; -.
DR PRO; PR:F4I6M4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I6M4; baseline and differential.
DR Genevisible; F4I6M4; AT.
DR GO; GO:0010005; C:cortical microtubule, transverse to long axis; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0010031; P:circumnutation; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..821
FT /note="TORTIFOLIA1-like protein 1"
FT /id="PRO_0000412561"
FT REPEAT 69..110
FT /note="HEAT 1"
FT REPEAT 114..151
FT /note="HEAT 2"
FT REPEAT 163..201
FT /note="HEAT 3"
FT REPEAT 205..242
FT /note="HEAT 4"
FT REPEAT 245..282
FT /note="HEAT 5"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..554
FT /evidence="ECO:0000255"
FT COMPBIAS 576..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9T041"
SQ SEQUENCE 821 AA; 89945 MW; 519E33C37BD0D865 CRC64;
MRSQTASKTS MKPSSNSSAF SVRSSVAVSS HSAMVELKQR ILTSLSRLGD RDTYQIAVDD
LEKIVVSVPD SPEILPVLLH CLFDSSSDLK APVKRESIRL LSFLCLSYTD LSFSQLAKII
SHIVKRLKDA DNGVRDACRD AIGSLSAQFL KEKEVENGNY VGSSLVGLFA KPLFEAMAEQ
NKSLQSGAAI CMGKMIDSAT EPPVAAFQKL CPRISKLLNS PNYITKASLL PVVGSLSQVG
AIAPQSLESL LHSIHECLGC TNWVTRKAAA DVLISLAVHS SSLVADKTDS TLTALEACRF
DKIKPVRESL SEALNVWKNI AGKGESGTMD DQKDVSSEQC ILERNGETDS VSCEEAGLVM
QGSCDGLSSS SDSISKAVLI LRKKAPRLTG KDLNPEFFQK LEKRGSGDMP VEVILPSRQK
NSSNSNTEDE SDANTSVLRS RSNGLCRTAG VHTKQRHFGD FAREKWVDER MNGGESRLRA
FDGDHTEVIQ ADTSENRGNW PPLQRQLLHL ERQQTHIMNM LQDFMGGSHD GMISLENRVR
GLERIVEEMS REMSIQSGAR GKATASWRSD VDGWDSPNYG PSSRNTQTST RKIRGTGPSE
QSGNSRRAWD KSSVAIRLGE GPSARSVWQA SKDEATLEAI RVAGEDCGTS RNRRVSIPEA
EAMMDEDDDN RGGQQGDPIW TCWSNSVHAL RVGDTDSAFA EVLSTGDDHL LVKLMDKTGP
VLDQLSSDMG NEAIHSIAQF LLDHTLYDIC LSWIQQLLEV SVENGADFMG IPLELKKELL
LNLHEALSTT DPPEDWEGLA PDHLLVELAS NWNIEIQHFD T
