WVD2_ARATH
ID WVD2_ARATH Reviewed; 202 AA.
AC Q84ZT9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein WAVE-DAMPENED 2;
DE Short=AtWVD2;
GN Name=WVD2; OrderedLocusNames=At5g28646; ORFNames=F4I4;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12586874; DOI=10.1104/pp.015966;
RA Yuen C.Y., Pearlman R.S., Silo-Suh L., Hilson P., Carroll K.L.,
RA Masson P.H.;
RT "WVD2 and WDL1 modulate helical organ growth and anisotropic cell expansion
RT in Arabidopsis.";
RL Plant Physiol. 131:493-506(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17319849; DOI=10.1111/j.1365-313x.2006.03015.x;
RA Perrin R.M., Wang Y., Yuen C.Y., Will J., Masson P.H.;
RT "WVD2 is a novel microtubule-associated protein in Arabidopsis thaliana.";
RL Plant J. 49:961-971(2007).
CC -!- FUNCTION: Microtubule-associated protein (MAP) that regulates the
CC orientation of interphase cortical microtubules. Able to bundle
CC microtubules in vitro. Modulates both rotational polarity and
CC anisotropic cell expansion during organ growth. Promotes clockwise root
CC and etiolated hypocotyls coiling, clockwise leaf curling, but left-
CC handed petiole twisting. {ECO:0000269|PubMed:12586874,
CC ECO:0000269|PubMed:17319849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17319849}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, cotyledons, hypocotyls,
CC roots, leaves, flowers, inflorescence stems and siliques.
CC {ECO:0000269|PubMed:12586874}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR EMBL; AF548461; AAO43563.1; -; Genomic_DNA.
DR EMBL; AF272705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93822.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93823.1; -; Genomic_DNA.
DR RefSeq; NP_001154744.1; NM_001161272.2.
DR RefSeq; NP_680247.4; NM_147942.4.
DR AlphaFoldDB; Q84ZT9; -.
DR SMR; Q84ZT9; -.
DR STRING; 3702.AT5G28646.1; -.
DR PaxDb; Q84ZT9; -.
DR PRIDE; Q84ZT9; -.
DR ProteomicsDB; 242662; -.
DR DNASU; 832970; -.
DR EnsemblPlants; AT5G28646.1; AT5G28646.1; AT5G28646.
DR EnsemblPlants; AT5G28646.2; AT5G28646.2; AT5G28646.
DR GeneID; 832970; -.
DR Gramene; AT5G28646.1; AT5G28646.1; AT5G28646.
DR Gramene; AT5G28646.2; AT5G28646.2; AT5G28646.
DR KEGG; ath:AT5G28646; -.
DR Araport; AT5G28646; -.
DR TAIR; locus:504955059; AT5G28646.
DR eggNOG; ENOG502RERJ; Eukaryota.
DR HOGENOM; CLU_1157835_0_0_1; -.
DR InParanoid; Q84ZT9; -.
DR OMA; PERAFHP; -.
DR OrthoDB; 1128803at2759; -.
DR PhylomeDB; Q84ZT9; -.
DR PRO; PR:Q84ZT9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84ZT9; baseline and differential.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:TAIR.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
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..202
FT /note="Protein WAVE-DAMPENED 2"
FT /id="PRO_0000420701"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..143
FT /evidence="ECO:0000255"
FT COMPBIAS 21..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 23341 MW; CF8E9D0877ED0A55 CRC64;
MRREVFESVS TNASNERVHV APKIAAEEQD YEEKECTEEN SLSQNHKSSN VITENDSKKK
NLDEEDDCSV ASSMKNAKSK VTHGTAPRFR SAQRAEKRKE YYQKLEEKHQ ALEAERIELE
QRQKEEQEAA IKQLRKNLKF KANPVPDFYY QRPPVKPELK KFPLTRPKSP KLNLSRRKSC
SDAITSSGEE NSNSQNRQSV VE
