WDL5_ARATH
ID WDL5_ARATH Reviewed; 437 AA.
AC Q94C48; F4JU98; O49359; Q9SUV5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein WVD2-like 5 {ECO:0000305};
GN Name=WDL5 {ECO:0000303|PubMed:23653471};
GN OrderedLocusNames=At4g32330 {ECO:0000312|Araport:AT4G32330};
GN ORFNames=F10M6.40 {ECO:0000312|EMBL:CAA16958.1},
GN F8B4.30 {ECO:0000312|EMBL:CAA22560.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-415, AND
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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94C48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94C48-2; Sequence=VSP_058146;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:23653471}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA22560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021811; CAA16958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL034567; CAA22560.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79950.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86040.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86041.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86042.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66294.1; -; Genomic_DNA.
DR EMBL; AY035182; AAK59686.1; -; mRNA.
DR EMBL; AY113894; AAM44942.1; -; mRNA.
DR EMBL; BX828309; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T05343; T05343.
DR PIR; T05396; T05396.
DR RefSeq; NP_001119094.1; NM_001125622.2. [Q94C48-1]
DR RefSeq; NP_001328200.1; NM_001342134.1. [Q94C48-1]
DR RefSeq; NP_567893.1; NM_119385.3. [Q94C48-1]
DR RefSeq; NP_974659.1; NM_202930.1. [Q94C48-2]
DR AlphaFoldDB; Q94C48; -.
DR SMR; Q94C48; -.
DR STRING; 3702.AT4G32330.1; -.
DR iPTMnet; Q94C48; -.
DR MetOSite; Q94C48; -.
DR PaxDb; Q94C48; -.
DR PRIDE; Q94C48; -.
DR ProteomicsDB; 242546; -. [Q94C48-1]
DR DNASU; 829367; -.
DR EnsemblPlants; AT4G32330.1; AT4G32330.1; AT4G32330. [Q94C48-1]
DR EnsemblPlants; AT4G32330.2; AT4G32330.2; AT4G32330. [Q94C48-2]
DR EnsemblPlants; AT4G32330.3; AT4G32330.3; AT4G32330. [Q94C48-1]
DR EnsemblPlants; AT4G32330.4; AT4G32330.4; AT4G32330. [Q94C48-1]
DR GeneID; 829367; -.
DR Gramene; AT4G32330.1; AT4G32330.1; AT4G32330. [Q94C48-1]
DR Gramene; AT4G32330.2; AT4G32330.2; AT4G32330. [Q94C48-2]
DR Gramene; AT4G32330.3; AT4G32330.3; AT4G32330. [Q94C48-1]
DR Gramene; AT4G32330.4; AT4G32330.4; AT4G32330. [Q94C48-1]
DR KEGG; ath:AT4G32330; -.
DR Araport; AT4G32330; -.
DR TAIR; locus:2127771; AT4G32330.
DR eggNOG; ENOG502REWY; Eukaryota.
DR HOGENOM; CLU_047642_0_0_1; -.
DR InParanoid; Q94C48; -.
DR OMA; LQNGMND; -.
DR PhylomeDB; Q94C48; -.
DR PRO; PR:Q94C48; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94C48; 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; IDA:TAIR.
DR GO; GO:0071369; P:cellular response to ethylene stimulus; IMP:TAIR.
DR GO; GO:0001578; P:microtubule bundle formation; 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 Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..437
FT /note="Protein WVD2-like 5"
FT /id="PRO_0000435677"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 188
FT /note="Missing (in isoform 2)"
FT /id="VSP_058146"
SQ SEQUENCE 437 AA; 47543 MW; 47D036F095D94686 CRC64;
MDPESIMAAD GTDSAPANGG LAMENVCVKE NGAVSVETVD TTSESQNENS ANSSTLDTIE
HVKEAAEGTQ VEHVDDSKCM KGEKAQRKPR HEKLSGGKNN SSVHIKKSKE GKSADAKVAA
SNGSVAPNVQ TTNPLKSKSF NGREAQVTKQ GKHDSAPAES ADGEKVKPKS QKKQAHETSE
DDTQSSNSPK ADDGKPRKVG ALPNYGFSFK CDQRAEKRKE FYVKLEEKTH AKEEEINSMQ
AKSKETQEAE LRMLRKSLNF KATPMPSFYQ EPQPPKTELK KIPPTRPKSP KLGRKKTASG
ADSEETQTPR LGRLSLDERA SKDNPTAKGI MPTVDLKKQP VRKSLPRLPS QKTVLPDGKP
APAKAAIIPA KVRPEKKKLE KDAETVNQTS HPTEEEAQVT VSSNADVEDS HETVSPRMNE
DRADKSIEVS EAVAVEH