VILI3_ARATH
ID VILI3_ARATH Reviewed; 965 AA.
AC O81645; A0A1I9LLW4; C0Z212; Q9LEA4; Q9SCN1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Villin-3 {ECO:0000303|PubMed:10631247};
GN Name=VLN3 {ECO:0000303|PubMed:10631247};
GN OrderedLocusNames=At3g57410 {ECO:0000312|Araport:AT3G57410};
GN ORFNames=F28O9.260 {ECO:0000312|EMBL:CAB68147.1},
GN T8H10.10 {ECO:0000312|EMBL:CAB66098.1};
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 [MRNA], TISSUE SPECIFICITY, FUNCTION, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10631247; DOI=10.1104/pp.122.1.35;
RA Klahre U., Friederich E., Kost B., Louvard D., Chua N.-H.;
RT "Villin-like actin-binding proteins are expressed ubiquitously in
RT Arabidopsis.";
RL Plant Physiol. 122:35-47(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880, AND IDENTIFICATION BY
RP 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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20807878; DOI=10.1105/tpc.110.076240;
RA Khurana P., Henty J.L., Huang S., Staiger A.M., Blanchoin L., Staiger C.J.;
RT "Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities
RT in actin bundle formation and turnover.";
RL Plant Cell 22:2727-2748(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22563899; DOI=10.1111/j.1365-313x.2012.05044.x;
RA Bao C., Wang J., Zhang R., Zhang B., Zhang H., Zhou Y., Huang S.;
RT "Arabidopsis VILLIN2 and VILLIN3 act redundantly in sclerenchyma
RT development via bundling of actin filaments.";
RL Plant J. 71:962-975(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22209875; DOI=10.1104/pp.111.192385;
RA van der Honing H.S., Kieft H., Emons A.M., Ketelaar T.;
RT "Arabidopsis VILLIN2 and VILLIN3 are required for the generation of thick
RT actin filament bundles and for directional organ growth.";
RL Plant Physiol. 158:1426-1438(2012).
CC -!- FUNCTION: Binds actin and actin filament bundles in a Ca(2+)-
CC insensitive manner, but severs actin filaments in a calcium-dependent
CC manner, regardless of the presence or not of VLN1 (AC O81643). Acts
CC redundantly with VLN2 (AC O81644) to generate thick actin filament
CC bundles, to regulate directional organ growth (PubMed:22209875) and in
CC sclerenchyma development (PubMed:22563899).
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:20807878,
CC ECO:0000269|PubMed:22209875, ECO:0000269|PubMed:22563899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:22209875}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including root
CC hairs. {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:20807878,
CC ECO:0000269|PubMed:22209875, ECO:0000269|PubMed:22563899}.
CC -!- DOMAIN: The HP domain is important for the localization to actin
CC filament bundles. {ECO:0000269|PubMed:22209875}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Vln2 and vln3 double
CC mutants show absence of thick actin filament bundles in the cells,
CC anomaly in the growth direction of organs (PubMed:22209875) and defects
CC in sclerenchyma development, but no alterations in the secondary cell-
CC wall machinery (PubMed:22563899). {ECO:0000269|PubMed:22209875,
CC ECO:0000269|PubMed:22563899}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB68147.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF081203; AAC31607.1; -; mRNA.
DR EMBL; AL133248; CAB66098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137080; CAB68147.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79652.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63565.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63566.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63567.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63568.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63569.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63570.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63572.1; -; Genomic_DNA.
DR EMBL; AK318626; BAH56741.1; -; mRNA.
DR PIR; T50668; T50668.
DR RefSeq; NP_001319779.1; NM_001339858.1.
DR RefSeq; NP_001325645.1; NM_001339860.1.
DR RefSeq; NP_001325646.1; NM_001339866.1.
DR RefSeq; NP_001325647.1; NM_001339863.1.
DR RefSeq; NP_001325648.1; NM_001339862.1.
DR RefSeq; NP_001325649.1; NM_001339865.1.
DR RefSeq; NP_001325651.1; NM_001339861.1.
DR RefSeq; NP_567048.1; NM_115601.3.
DR AlphaFoldDB; O81645; -.
DR SMR; O81645; -.
DR BioGRID; 10224; 3.
DR STRING; 3702.AT3G57410.1; -.
DR iPTMnet; O81645; -.
DR PaxDb; O81645; -.
DR PRIDE; O81645; -.
DR ProteomicsDB; 242331; -.
DR EnsemblPlants; AT3G57410.1; AT3G57410.1; AT3G57410.
DR EnsemblPlants; AT3G57410.2; AT3G57410.2; AT3G57410.
DR EnsemblPlants; AT3G57410.3; AT3G57410.3; AT3G57410.
DR EnsemblPlants; AT3G57410.4; AT3G57410.4; AT3G57410.
DR EnsemblPlants; AT3G57410.5; AT3G57410.5; AT3G57410.
DR EnsemblPlants; AT3G57410.7; AT3G57410.7; AT3G57410.
DR EnsemblPlants; AT3G57410.8; AT3G57410.8; AT3G57410.
DR EnsemblPlants; AT3G57410.9; AT3G57410.9; AT3G57410.
DR GeneID; 824908; -.
DR Gramene; AT3G57410.1; AT3G57410.1; AT3G57410.
DR Gramene; AT3G57410.2; AT3G57410.2; AT3G57410.
DR Gramene; AT3G57410.3; AT3G57410.3; AT3G57410.
DR Gramene; AT3G57410.4; AT3G57410.4; AT3G57410.
DR Gramene; AT3G57410.5; AT3G57410.5; AT3G57410.
DR Gramene; AT3G57410.7; AT3G57410.7; AT3G57410.
DR Gramene; AT3G57410.8; AT3G57410.8; AT3G57410.
DR Gramene; AT3G57410.9; AT3G57410.9; AT3G57410.
DR KEGG; ath:AT3G57410; -.
DR Araport; AT3G57410; -.
DR TAIR; locus:2082523; AT3G57410.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_0_1; -.
DR InParanoid; O81645; -.
DR OrthoDB; 1376537at2759; -.
DR PRO; PR:O81645; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O81645; baseline and differential.
DR Genevisible; O81645; AT.
DR GO; GO:0005884; C:actin filament; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0051014; P:actin filament severing; IDA:TAIR.
DR Gene3D; 1.10.950.10; -; 1.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR044155; Villin-3.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF101; PTHR11977:SF101; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..965
FT /note="Villin-3"
FT /id="PRO_0000218734"
FT REPEAT 27..79
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..190
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 262..304
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 401..452
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 533..573
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 635..676
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 900..965
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 769..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 859..860
FT /note="KA -> ETS (in Ref. 1; AAC31607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 965 AA; 106349 MW; 1571DB7D6EF1B6A8 CRC64;
MSGSTKVLDP AFQGVGQKPG TEIWRIENFE PVPVPKSEHG KFYMGDTYIV LQTTQNKGGA
YLFDIHFWIG KDTSQDEAGT AAVKTVELDA ALGGRAVQYR EIQGHESDKF LSYFKPCIIP
LEGGVASGFK KPEEEEFETR LYTCKGKRAV HLKQVPFARS SLNHDDVFIL DTKEKIYQFN
GANSNIQERA KALVVIQYLK DKFHEGTSDV AIVDDGKLDT ESDSGEFWVL FGGFAPIARK
VASEDEIIPE TTPPKLYSIA DGQVESIDGD LSKSMLENNK CYLLDCGSEI FIWVGRVTQV
EERKTAIQAA EDFVASENRP KATRITRVIQ GYEPHSFKSN FDSWPSGSAT PANEEGRGKV
AALLKQQGVG LKGLSKSTPV NEDIPPLLEG GGKLEVWYID ANSKTVLSKD HVGKLYSGDC
YLVLYTYHSG ERKEDYFLCC WFGKNSNQED QETAVRLAST MTNSLKGRPV QARIFEGKEP
PQFVALFQHM VVLKGGLSSG YKNSMTEKGS SGETYTPESI ALIQVSGTGV HNNKALQVEA
VATSLNSYDC FLLQSGTSMF LWVGNHSTHE QQELAAKVAE FLKPGTTIKH AKEGTESSSF
WFALGGKQNF TSKKVSSETV RDPHLFSFSF NRGKFQVEEI HNFDQDDLLT EEMHLLDTHA
EVFVWVGQCV DPKEKQTAFE IGQRYINLAG SLEGLSPKVP LYKITEGNEP CFFTTYFSWD
STKATVQGNS YQKKAALLLG THHVVEDQSS SGNQGPRQRA AALAALTSAF NSSSGRTSSP
SRDRSNGSQG GPRQRAEALA ALTSAFNSSP SSKSPPRRSG LTSQASQRAA AVAALSQVLT
AEKKKSPDTS PSAEAKDEKA FSEVEATEEA TEAKEEEEVS PAAEASAEEA KPKQDDSEVE
TTGVTFTYER LQAKSEKPVT GIDFKRREAY LSEVEFKTVF GMEKESFYKL PGWKQDLLKK
KFNLF
