WDL3_ARATH
ID WDL3_ARATH Reviewed; 338 AA.
AC Q84WL6; Q9LS82;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein WVD2-like 3 {ECO:0000305};
DE AltName: Full=Protein WAVE-DAMPENED 2-LIKE3 {ECO:0000303|PubMed:23653471};
GN Name=WDL3 {ECO:0000303|PubMed:23653471};
GN OrderedLocusNames=At3g23090 {ECO:0000312|Araport:AT3G23090};
GN ORFNames=MXC7.13 {ECO:0000312|EMBL:BAB02101.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 [4]
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 oaf RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, AND
RP INDUCTION.
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. Binds to, bundles and
CC stabilizes microtubules. Required for the organization and stability of
CC cortical microtubules in hypocotyls. Required for normal hypocotyl cell
CC elongation. Acts as negative regulator of hypocotyl cell elongation in
CC the light. {ECO:0000269|PubMed:23653471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23653471}. Note=Associates with cortical
CC microtubules. {ECO:0000269|PubMed:23653471}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q84WL6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, root hairs, cotyledons,
CC hypocotyls, trichomes, flowers and siliques.
CC {ECO:0000269|PubMed:23653471}.
CC -!- INDUCTION: By light (at protein level). Down-regulated by dark (at
CC protein level). {ECO:0000269|PubMed:23653471}.
CC -!- PTM: Ubiquitinated (Probable). Proteasomal-dependent degradation in the
CC dark (PubMed:23653471). {ECO:0000269|PubMed:23653471,
CC ECO:0000305|PubMed:23653471}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02101.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026655; BAB02101.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76715.1; -; Genomic_DNA.
DR EMBL; BT003083; AAO23648.1; -; mRNA.
DR EMBL; AK227638; BAE99628.1; -; mRNA.
DR RefSeq; NP_001326991.1; NM_001338615.1.
DR RefSeq; NP_188950.1; NM_113210.4. [Q84WL6-1]
DR AlphaFoldDB; Q84WL6; -.
DR SMR; Q84WL6; -.
DR STRING; 3702.AT3G23090.2; -.
DR iPTMnet; Q84WL6; -.
DR PaxDb; Q84WL6; -.
DR ProteomicsDB; 242635; -. [Q84WL6-1]
DR DNASU; 821884; -.
DR EnsemblPlants; AT3G23090.1; AT3G23090.1; AT3G23090. [Q84WL6-1]
DR GeneID; 821884; -.
DR Gramene; AT3G23090.1; AT3G23090.1; AT3G23090. [Q84WL6-1]
DR KEGG; ath:AT3G23090; -.
DR Araport; AT3G23090; -.
DR TAIR; locus:2094583; AT3G23090.
DR eggNOG; ENOG502RERJ; Eukaryota.
DR PRO; PR:Q84WL6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84WL6; baseline and differential.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0051511; P:negative regulation of unidimensional cell growth; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB.
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 Reference proteome; Ubl conjugation.
FT CHAIN 1..338
FT /note="Protein WVD2-like 3"
FT /id="PRO_0000435675"
FT REGION 68..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..240
FT /evidence="ECO:0000255"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 37782 MW; D04F37188FD67E59 CRC64;
MDICMDKEPD GVVVYANGDS CNPNQENVSE PLLDSVSRDD ANVHTELRYG EENIEVNEYD
VKECTSEIPV GKPIGDDFES KDVTKSSLHA KHASKSGRGN NKTRNTVPQP FSLATEKRAS
STRSFTSESL ESAGLKKFPD GHSKVQSQAT KVPRKPLQPK NKKLSDEEDS CSVASYATSG
AKSAKSRTVV TAAPSFRSTE RAEKRKEFYT KLEEKHQAME AEKTQSEARN KEATEAALRQ
LRKSLRFKAN PMPKFYHEGP PPKVELKKPL PTRAKSPKLG RRNPKEGNRA KGASRRHETR
KTLVISKEDH DDETTRNADQ INHKEMNRNL EPETAFAC
