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Protein

Villin-3

Gene

VLN3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds actin and actin filament bundles in a Ca2+-insensitive manner, but severs actin filaments in a calcium-dependent manner, regardless of the presence or not of VLN1 (AC O81643). Acts redundantly with VLN2 (AC O81644) to generate thick actin filament bundles, to regulate directional organ growth (PubMed:22209875) and in sclerenchyma development (PubMed:22563899).4 Publications

GO - Molecular functioni

  • actin filament binding Source: TAIR

GO - Biological processi

  • actin filament bundle assembly Source: UniProtKB
  • actin filament capping Source: UniProtKB-KW
  • actin filament severing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-31 Publication
Gene namesi
Name:VLN31 Publication
Ordered Locus Names:At3g57410Imported
ORF Names:F28O9.260Imported, T8H10.10Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G57410.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: TAIR
  • cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Vln2 and vln3 double mutants show absence of thick actin filament bundles in the cells, anomaly in the growth direction of organs (PubMed:22209875) and defects in sclerenchyma development, but no alterations in the secondary cell-wall machinery (PubMed:22563899).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 965965Villin-3PRO_0000218734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei880 – 8801PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO81645.
PRIDEiO81645.

PTM databases

iPTMnetiO81645.

Expressioni

Tissue specificityi

Expressed in all tissues examined, including root hairs.4 Publications

Gene expression databases

GenevisibleiO81645. AT.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: TAIR

Protein-protein interaction databases

BioGridi10224. 2 interactions.
MINTiMINT-8060963.
STRINGi3702.AT3G57410.1.

Structurei

3D structure databases

ProteinModelPortaliO81645.
SMRiO81645. Positions 10-726, 921-965.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 7953Gelsolin-like 1Sequence analysisAdd
BLAST
Repeati150 – 19041Gelsolin-like 2Sequence analysisAdd
BLAST
Repeati262 – 30443Gelsolin-like 3Sequence analysisAdd
BLAST
Repeati401 – 45252Gelsolin-like 4Sequence analysisAdd
BLAST
Repeati533 – 57341Gelsolin-like 5Sequence analysisAdd
BLAST
Repeati635 – 67642Gelsolin-like 6Sequence analysisAdd
BLAST
Domaini900 – 96566HPPROSITE-ProRule annotationAdd
BLAST

Domaini

The HP domain is important for the localization to actin filament bundles.1 Publication

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
HOGENOMiHOG000233631.
InParanoidiO81645.
OMAiALYMISD.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR030009. Villin-2/3/4/5_plant.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF46. PTHR11977:SF46. 2 hits.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O81645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSTKVLDP AFQGVGQKPG TEIWRIENFE PVPVPKSEHG KFYMGDTYIV
60 70 80 90 100
LQTTQNKGGA YLFDIHFWIG KDTSQDEAGT AAVKTVELDA ALGGRAVQYR
110 120 130 140 150
EIQGHESDKF LSYFKPCIIP LEGGVASGFK KPEEEEFETR LYTCKGKRAV
160 170 180 190 200
HLKQVPFARS SLNHDDVFIL DTKEKIYQFN GANSNIQERA KALVVIQYLK
210 220 230 240 250
DKFHEGTSDV AIVDDGKLDT ESDSGEFWVL FGGFAPIARK VASEDEIIPE
260 270 280 290 300
TTPPKLYSIA DGQVESIDGD LSKSMLENNK CYLLDCGSEI FIWVGRVTQV
310 320 330 340 350
EERKTAIQAA EDFVASENRP KATRITRVIQ GYEPHSFKSN FDSWPSGSAT
360 370 380 390 400
PANEEGRGKV AALLKQQGVG LKGLSKSTPV NEDIPPLLEG GGKLEVWYID
410 420 430 440 450
ANSKTVLSKD HVGKLYSGDC YLVLYTYHSG ERKEDYFLCC WFGKNSNQED
460 470 480 490 500
QETAVRLAST MTNSLKGRPV QARIFEGKEP PQFVALFQHM VVLKGGLSSG
510 520 530 540 550
YKNSMTEKGS SGETYTPESI ALIQVSGTGV HNNKALQVEA VATSLNSYDC
560 570 580 590 600
FLLQSGTSMF LWVGNHSTHE QQELAAKVAE FLKPGTTIKH AKEGTESSSF
610 620 630 640 650
WFALGGKQNF TSKKVSSETV RDPHLFSFSF NRGKFQVEEI HNFDQDDLLT
660 670 680 690 700
EEMHLLDTHA EVFVWVGQCV DPKEKQTAFE IGQRYINLAG SLEGLSPKVP
710 720 730 740 750
LYKITEGNEP CFFTTYFSWD STKATVQGNS YQKKAALLLG THHVVEDQSS
760 770 780 790 800
SGNQGPRQRA AALAALTSAF NSSSGRTSSP SRDRSNGSQG GPRQRAEALA
810 820 830 840 850
ALTSAFNSSP SSKSPPRRSG LTSQASQRAA AVAALSQVLT AEKKKSPDTS
860 870 880 890 900
PSAEAKDEKA FSEVEATEEA TEAKEEEEVS PAAEASAEEA KPKQDDSEVE
910 920 930 940 950
TTGVTFTYER LQAKSEKPVT GIDFKRREAY LSEVEFKTVF GMEKESFYKL
960
PGWKQDLLKK KFNLF
Length:965
Mass (Da):106,349
Last modified:January 25, 2012 - v2
Checksum:i1571DB7D6EF1B6A8
GO

Sequence cautioni

The sequence CAB66098.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB68147.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti859 – 8602KA → ETS in AAC31607 (PubMed:10631247).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081203 mRNA. Translation: AAC31607.1.
AL133248 Genomic DNA. Translation: CAB66098.1. Sequence problems.
AL137080 Genomic DNA. Translation: CAB68147.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79652.1.
AK318626 mRNA. Translation: BAH56741.1.
PIRiT50668.
RefSeqiNP_567048.1. NM_115601.2.
UniGeneiAt.22370.

Genome annotation databases

EnsemblPlantsiAT3G57410.1; AT3G57410.1; AT3G57410.
GeneIDi824908.
GrameneiAT3G57410.1; AT3G57410.1; AT3G57410.
KEGGiath:AT3G57410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081203 mRNA. Translation: AAC31607.1.
AL133248 Genomic DNA. Translation: CAB66098.1. Sequence problems.
AL137080 Genomic DNA. Translation: CAB68147.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79652.1.
AK318626 mRNA. Translation: BAH56741.1.
PIRiT50668.
RefSeqiNP_567048.1. NM_115601.2.
UniGeneiAt.22370.

3D structure databases

ProteinModelPortaliO81645.
SMRiO81645. Positions 10-726, 921-965.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10224. 2 interactions.
MINTiMINT-8060963.
STRINGi3702.AT3G57410.1.

PTM databases

iPTMnetiO81645.

Proteomic databases

PaxDbiO81645.
PRIDEiO81645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G57410.1; AT3G57410.1; AT3G57410.
GeneIDi824908.
GrameneiAT3G57410.1; AT3G57410.1; AT3G57410.
KEGGiath:AT3G57410.

Organism-specific databases

TAIRiAT3G57410.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
HOGENOMiHOG000233631.
InParanoidiO81645.
OMAiALYMISD.

Miscellaneous databases

PROiO81645.

Gene expression databases

GenevisibleiO81645. AT.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR030009. Villin-2/3/4/5_plant.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF46. PTHR11977:SF46. 2 hits.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis."
    Klahre U., Friederich E., Kost B., Louvard D., Chua N.-H.
    Plant Physiol. 122:35-47(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities in actin bundle formation and turnover."
    Khurana P., Henty J.L., Huang S., Staiger A.M., Blanchoin L., Staiger C.J.
    Plant Cell 22:2727-2748(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "Arabidopsis VILLIN2 and VILLIN3 act redundantly in sclerenchyma development via bundling of actin filaments."
    Bao C., Wang J., Zhang R., Zhang B., Zhang H., Zhou Y., Huang S.
    Plant J. 71:962-975(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  8. "Arabidopsis VILLIN2 and VILLIN3 are required for the generation of thick actin filament bundles and for directional organ growth."
    van der Honing H.S., Kieft H., Emons A.M., Ketelaar T.
    Plant Physiol. 158:1426-1438(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiVILI3_ARATH
AccessioniPrimary (citable) accession number: O81645
Secondary accession number(s): C0Z212, Q9LEA4, Q9SCN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: January 25, 2012
Last modified: February 17, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.