WDL2_ARATH
ID WDL2_ARATH Reviewed; 338 AA.
AC Q9ASW8; Q8LES4; Q9SLI7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein WVD2-like 2 {ECO:0000305};
GN Name=WDL2 {ECO:0000303|PubMed:23653471};
GN OrderedLocusNames=At1g54460 {ECO:0000312|Araport:AT1G54460};
GN ORFNames=F20D21.28 {ECO:0000312|EMBL:AAD25625.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [5]
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=AAD25625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005287; AAD25625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33106.1; -; Genomic_DNA.
DR EMBL; AF361626; AAK32794.1; -; mRNA.
DR EMBL; AY055093; AAL05893.1; -; mRNA.
DR EMBL; AY085262; AAM62494.1; -; mRNA.
DR PIR; E96586; E96586.
DR RefSeq; NP_564659.1; NM_104324.4.
DR AlphaFoldDB; Q9ASW8; -.
DR STRING; 3702.AT1G54460.1; -.
DR iPTMnet; Q9ASW8; -.
DR PaxDb; Q9ASW8; -.
DR PRIDE; Q9ASW8; -.
DR ProteomicsDB; 242745; -.
DR DNASU; 841888; -.
DR EnsemblPlants; AT1G54460.1; AT1G54460.1; AT1G54460.
DR GeneID; 841888; -.
DR Gramene; AT1G54460.1; AT1G54460.1; AT1G54460.
DR KEGG; ath:AT1G54460; -.
DR Araport; AT1G54460; -.
DR TAIR; locus:2020048; AT1G54460.
DR eggNOG; ENOG502RERJ; Eukaryota.
DR HOGENOM; CLU_042861_2_0_1; -.
DR InParanoid; Q9ASW8; -.
DR OMA; KYIMFSS; -.
DR OrthoDB; 1303777at2759; -.
DR PhylomeDB; Q9ASW8; -.
DR PRO; PR:Q9ASW8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ASW8; 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 GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR InterPro; IPR027329; TPX2_C.
DR InterPro; IPR044806; WVD2/WDL1-3.
DR PANTHER; PTHR46372; PTHR46372; 1.
DR Pfam; PF06886; TPX2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..338
FT /note="Protein WVD2-like 2"
FT /id="PRO_0000435674"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..214
FT /evidence="ECO:0000255"
FT COMPBIAS 15..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 76
FT /note="V -> A (in Ref. 4; AAM62494)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="G -> D (in Ref. 4; AAM62494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37399 MW; ED238D305ACCA492 CRC64;
MGRELVDKHM DKKANSLTAS STGSSDDNKV PSPSTNEAAE VKECTEQNLV ADDARLRQQG
ITETPGSHKS SVKPRVTAKT TVPKPFSLSA EKPRRAAVDN NSLGNGASHN SSSASRVSQL
NSPLPTRRIP DHKMHHDEED SFSVASSSAT SIRSFKPKIT IGVAPTFSST SRLERRREFY
QKLEEKQKAL EAEKRENEKR LKEEQEAVTK QLRKNMAYKA NPVPSFYQEG PPPKQPLKKF
PLTRPKSPNL NRRKSCSDTV NASYQEVKGK HCARHRHSVG GCKDEVKTNS VPRTPNSSSK
DQMRKSKKGT PKSEEVHEMF NSGHDGETGE NGVGVVEE
