ID   WDL6_ARATH              Reviewed;         403 AA.
AC   Q0WSZ8; Q9SKK1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein WVD2-like 6 {ECO:0000305};
GN   Name=WDL6 {ECO:0000303|PubMed:23653471};
GN   OrderedLocusNames=At2g25480 {ECO:0000312|Araport:AT2G25480};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=23653471; DOI=10.1105/tpc.113.112789;
RA   Liu X., Qin T., Ma Q., Sun J., Liu Z., Yuan M., Mao T.;
RT   "Light-regulated hypocotyl elongation involves proteasome-dependent
RT   degradation of the microtubule regulatory protein WDL3 in Arabidopsis.";
RL   Plant Cell 25:1740-1755(2013).
CC   -!- FUNCTION: Microtubule-associated protein (MAP) that regulates the
CC       orientation of interphase cortical microtubules.
CC       {ECO:0000250|UniProtKB:Q8GYX9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8GYX9}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC       {ECO:0000269|PubMed:23653471}.
CC   -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC006300; AAD20707.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07706.1; -; Genomic_DNA.
DR   EMBL; AK227768; BAE99750.1; -; mRNA.
DR   RefSeq; NP_001324900.1; NM_001336000.1.
DR   RefSeq; NP_180118.2; NM_128105.4.
DR   AlphaFoldDB; Q0WSZ8; -.
DR   SMR; Q0WSZ8; -.
DR   STRING; 3702.AT2G25480.1; -.
DR   iPTMnet; Q0WSZ8; -.
DR   PaxDb; Q0WSZ8; -.
DR   PRIDE; Q0WSZ8; -.
DR   ProteomicsDB; 242782; -.
DR   DNASU; 817086; -.
DR   EnsemblPlants; AT2G25480.1; AT2G25480.1; AT2G25480.
DR   GeneID; 817086; -.
DR   Gramene; AT2G25480.1; AT2G25480.1; AT2G25480.
DR   KEGG; ath:AT2G25480; -.
DR   Araport; AT2G25480; -.
DR   TAIR; locus:2040090; AT2G25480.
DR   eggNOG; ENOG502REWY; Eukaryota.
DR   HOGENOM; CLU_047642_0_0_1; -.
DR   InParanoid; Q0WSZ8; -.
DR   OMA; SFNERQA; -.
DR   OrthoDB; 874965at2759; -.
DR   PhylomeDB; Q0WSZ8; -.
DR   PRO; PR:Q0WSZ8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q0WSZ8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   InterPro; IPR027329; TPX2_C.
DR   InterPro; IPR044833; WDL4/5/6.
DR   PANTHER; PTHR31358; PTHR31358; 1.
DR   Pfam; PF06886; TPX2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN           1..403
FT                   /note="Protein WVD2-like 6"
FT                   /id="PRO_0000435678"
FT   REGION          1..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   403 AA;  44343 MW;  78B7F9E766C36797 CRC64;
     MDSESVVAAD GADCAIANGE VTMEGDSSNG NGGTSENLEC CSTQHPMEAS EGTQNEQVDD
     SKQMRGQKVQ GRVKHEKTSG GKNIPSVLVK KKKDGKVVAS NGSVAPNVKP VKSPKSKSLN
     GREAHVTKHG NHDSLPAEGT RDKPKLRETR KQVNDTSEDD TQYPKEDDGK PRRASALPNY
     GFSFRCDQRA EKRREFYSKL EEKIHAKEEE KNTVQAKSKE TQEAELKMLR KSLNFKATPM
     PTFYQEPQLP KTELKKIAIT RPKSPKLGRK KTNSRADSEE AITIQTPRFG RLSLDEKTPK
     DNPVVEGSVP GETKKPPVRK SLPRLPSEKT NLSNGKVAPA KAVTASTKAK SERKKPDKDV
     DDLSQSSPVD DNADPEDSQE QAPRVNEDRN ESHMVVEVVA VEP