WDL4_ARATH
ID WDL4_ARATH Reviewed; 432 AA.
AC Q9SJ62; Q93ZD3;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Protein WVD2-like 4 {ECO:0000305};
GN Name=WDL4 {ECO:0000303|PubMed:23653471};
GN OrderedLocusNames=At2g35880 {ECO:0000312|Araport:AT2G35880};
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;
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 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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}.
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DR EMBL; AC007017; AAD21469.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09173.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63304.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63305.1; -; Genomic_DNA.
DR EMBL; AY057620; AAL14415.1; -; mRNA.
DR EMBL; AY140090; AAM98231.1; -; mRNA.
DR PIR; B84774; B84774.
DR RefSeq; NP_001325399.1; NM_001336577.1.
DR RefSeq; NP_001325400.1; NM_001336576.1.
DR RefSeq; NP_565829.1; NM_129147.4.
DR AlphaFoldDB; Q9SJ62; -.
DR SMR; Q9SJ62; -.
DR IntAct; Q9SJ62; 4.
DR STRING; 3702.AT2G35880.1; -.
DR iPTMnet; Q9SJ62; -.
DR PaxDb; Q9SJ62; -.
DR PRIDE; Q9SJ62; -.
DR ProteomicsDB; 242545; -.
DR EnsemblPlants; AT2G35880.1; AT2G35880.1; AT2G35880.
DR EnsemblPlants; AT2G35880.2; AT2G35880.2; AT2G35880.
DR EnsemblPlants; AT2G35880.3; AT2G35880.3; AT2G35880.
DR GeneID; 818161; -.
DR Gramene; AT2G35880.1; AT2G35880.1; AT2G35880.
DR Gramene; AT2G35880.2; AT2G35880.2; AT2G35880.
DR Gramene; AT2G35880.3; AT2G35880.3; AT2G35880.
DR KEGG; ath:AT2G35880; -.
DR Araport; AT2G35880; -.
DR TAIR; locus:2039235; AT2G35880.
DR eggNOG; ENOG502QTFB; Eukaryota.
DR HOGENOM; CLU_040103_0_0_1; -.
DR InParanoid; Q9SJ62; -.
DR OMA; RFMSQSS; -.
DR OrthoDB; 1307210at2759; -.
DR PhylomeDB; Q9SJ62; -.
DR PRO; PR:Q9SJ62; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ62; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0072657; P:protein localization to membrane; IMP:TAIR.
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 Acetylation; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..432
FT /note="Protein WVD2-like 4"
FT /id="PRO_0000435676"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 432 AA; 46697 MW; 250717B88DDC6028 CRC64;
MASEDLNIVA ESKKGEENVI VDNSKDMNRP ENLDLSTEKT DTANENGPKD EASKLVKEAD
LPESGTSVKS KTAKDNKPVK RKSGTFSRSP RFMSQSSSFP TKGAYTDITR KSIDATTSKT
SLKPVVAGGS KPKATPSSSS GVSAKRTSLV SAPLKKQTMP VKTISKDAAS GPTSKLGDEG
SKSIKEETAG KDVEEAGSTT AVVADKVSNP LKAEMASKDD EDTRSTTTST STPRGRRSSV
GSASGFSFRL EERAEKRKEF YMKLEEKIHA KEVEKTNLQA KSKESQEEEI KRLRKSLTFK
AGPMPSFYKE PPPKVELKKI PTTRPKSPKL GRRKSSSDAT GGEAAPRVTK PKDSSSSTVK
KPITKSQPKL ETQEKSVKAK EKKKKVKKEE AEKRGEEEKA TAVAAKPEEQ KPNSNNIQVK
AEIMASEVVV GG
