WDL1_ARATH
ID WDL1_ARATH Reviewed; 286 AA.
AC Q8GYX9; B9DGL4; Q2HIS4; Q8LAB8; Q9SR11;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein WVD2-like 1;
DE Short=AtWDL1;
GN Name=WDL1; OrderedLocusNames=At3g04630; ORFNames=F7O18.11;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=12586874; DOI=10.1104/pp.015966;
RA Yuen C.Y., Pearlman R.S., Silo-Suh L., Hilson P., Carroll K.L.,
RA Masson P.H.;
RT "WVD2 and WDL1 modulate helical organ growth and anisotropic cell expansion
RT in Arabidopsis.";
RL Plant Physiol. 131:493-506(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17319849; DOI=10.1111/j.1365-313x.2006.03015.x;
RA Perrin R.M., Wang Y., Yuen C.Y., Will J., Masson P.H.;
RT "WVD2 is a novel microtubule-associated protein in Arabidopsis thaliana.";
RL Plant J. 49:961-971(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Microtubule-associated protein (MAP) that regulates the
CC orientation of interphase cortical microtubules. Modulates both
CC rotational polarity and anisotropic cell expansion during organ growth.
CC Promotes clockwise root and etiolated hypocotyls coiling, clockwise
CC leaf curling, but left-handed petiole twisting.
CC {ECO:0000269|PubMed:12586874, ECO:0000269|PubMed:17319849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17319849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GYX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GYX9-2; Sequence=VSP_044608;
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF04893.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011437; AAF04893.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74108.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74109.1; -; Genomic_DNA.
DR EMBL; AK117325; BAC41996.1; -; mRNA.
DR EMBL; BT024507; ABD19688.1; -; mRNA.
DR EMBL; AK317197; BAH19881.1; -; mRNA.
DR EMBL; AY087930; AAM67336.1; -; mRNA.
DR RefSeq; NP_001319470.1; NM_001337538.1.
DR RefSeq; NP_566233.1; NM_111335.2. [Q8GYX9-2]
DR RefSeq; NP_850514.1; NM_180183.3. [Q8GYX9-1]
DR AlphaFoldDB; Q8GYX9; -.
DR SMR; Q8GYX9; -.
DR STRING; 3702.AT3G04630.1; -.
DR iPTMnet; Q8GYX9; -.
DR PaxDb; Q8GYX9; -.
DR PRIDE; Q8GYX9; -.
DR ProteomicsDB; 242673; -. [Q8GYX9-1]
DR DNASU; 819621; -.
DR EnsemblPlants; AT3G04630.1; AT3G04630.1; AT3G04630. [Q8GYX9-2]
DR EnsemblPlants; AT3G04630.2; AT3G04630.2; AT3G04630. [Q8GYX9-1]
DR GeneID; 819621; -.
DR Gramene; AT3G04630.1; AT3G04630.1; AT3G04630. [Q8GYX9-2]
DR Gramene; AT3G04630.2; AT3G04630.2; AT3G04630. [Q8GYX9-1]
DR KEGG; ath:AT3G04630; -.
DR Araport; AT3G04630; -.
DR TAIR; locus:2084878; AT3G04630.
DR eggNOG; ENOG502RERJ; Eukaryota.
DR HOGENOM; CLU_1157835_0_0_1; -.
DR InParanoid; Q8GYX9; -.
DR OrthoDB; 1128803at2759; -.
DR PhylomeDB; Q8GYX9; -.
DR PRO; PR:Q8GYX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYX9; baseline and differential.
DR Genevisible; Q8GYX9; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0010031; P:circumnutation; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR InterPro; IPR027329; TPX2_C.
DR InterPro; IPR044806; WVD2/WDL1-3.
DR PANTHER; PTHR46372; PTHR46372; 1.
DR Pfam; PF06886; TPX2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..286
FT /note="Protein WVD2-like 1"
FT /id="PRO_0000420702"
FT REGION 31..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..182
FT /evidence="ECO:0000255"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 78
FT /note="Q -> QQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.6"
FT /id="VSP_044608"
FT CONFLICT 235
FT /note="V -> A (in Ref. 5; BAH19881)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> K (in Ref. 6; AAM67336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31950 MW; 4DDE02C3573CC7E0 CRC64;
MGREVVEVLM DRNADVSSAR VHVAPKIAAE ETDEEFEVKE CTEEKSLSEN APNVGSAERV
GAQKSPKTRN GNAKVSKQDA PLLAVRKPLQ PENKKHIDDE DNCSIASSVA TSMRMGKSGL
TYGSAPTFRS AQRAEKRKEY YQKLEEKNQA LEAERNELEQ RQKDEQEAAL KQLRKNLKFK
AKPVPNFYYE APPAKPELKK LPLTRPKSPK LILSRRKSFS DAVSSSSREE ILKTVSNRNR
HSTGTVQNKD DDHRNKNTNA AHDSPRVRSG KGKSGLKPVN ESSEEA
