VILI4_ARATH
ID VILI4_ARATH Reviewed; 974 AA.
AC O65570; F4JPJ2; Q541Y5; Q9SZW9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Villin-4 {ECO:0000303|PubMed:10631247};
GN Name=VLN4 {ECO:0000303|PubMed:10631247};
GN OrderedLocusNames=At4g30160 {ECO:0000312|Araport:AT4G30160};
GN ORFNames=F6G3.190 {ECO:0000312|EMBL:CAB43851.1},
GN F9N11.10 {ECO:0000312|EMBL:CAB52460.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RA Klein M.V.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-787, 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21275995; DOI=10.1111/j.1469-8137.2010.03632.x;
RA Zhang Y., Xiao Y., Du F., Cao L., Dong H., Ren H.;
RT "Arabidopsis VILLIN4 is involved in root hair growth through regulating
RT actin organization in a Ca2+-dependent manner.";
RL New Phytol. 190:667-682(2011).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22019634; DOI=10.4161/psb.6.9.16501;
RA Du F., Zhang Y., Ren H.;
RT "The universal bundling activity of AtVLN4 in diffusely growing cells.";
RL Plant Signal. Behav. 6:1290-1293(2011).
CC -!- FUNCTION: Binds actin and actin filament bundles in a Ca(2+)-
CC insensitive manner, but caps the barbed end of actin filaments and is
CC able to sever them in a calcium-dependent manner. Involved in root hair
CC growth through regulating actin organization in a Ca(2+)-dependent
CC manner. {ECO:0000269|PubMed:21275995, ECO:0000269|PubMed:22019634}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21275995}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O65570-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O65570-2; Sequence=VSP_056809;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in vegetative tissues.
CC Detected in the whole seedling, hypocotyl, cotyledon, primary root,
CC roots hair cells and trichomes. Expressed in flowers but not in the
CC silique. {ECO:0000269|PubMed:21275995, ECO:0000269|PubMed:22019634}.
CC -!- DISRUPTION PHENOTYPE: No changes in the primary root length, but
CC shorter root hairs. Increased sensitivity to latrunculin B (LatB) and
CC instability of actin filaments. {ECO:0000269|PubMed:21275995,
CC ECO:0000269|PubMed:22019634}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; Y12782; CAA73320.1; -; mRNA.
DR EMBL; AL078464; CAB43851.1; -; Genomic_DNA.
DR EMBL; AL109796; CAB52460.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB81009.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85727.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85728.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68140.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68141.1; -; Genomic_DNA.
DR EMBL; AK117296; BAC41968.1; -; mRNA.
DR EMBL; BT005980; AAO64915.1; -; mRNA.
DR PIR; T14076; T14076.
DR RefSeq; NP_001190869.1; NM_001203940.1. [O65570-2]
DR RefSeq; NP_001329917.1; NM_001342000.1. [O65570-1]
DR RefSeq; NP_001329918.1; NM_001341999.1. [O65570-1]
DR RefSeq; NP_194745.1; NM_119162.5. [O65570-1]
DR PDB; 5VNT; NMR; -; A=912-974.
DR PDBsum; 5VNT; -.
DR AlphaFoldDB; O65570; -.
DR SMR; O65570; -.
DR BioGRID; 14426; 1.
DR STRING; 3702.AT4G30160.2; -.
DR iPTMnet; O65570; -.
DR PaxDb; O65570; -.
DR PRIDE; O65570; -.
DR ProteomicsDB; 242699; -. [O65570-1]
DR EnsemblPlants; AT4G30160.1; AT4G30160.1; AT4G30160. [O65570-1]
DR EnsemblPlants; AT4G30160.2; AT4G30160.2; AT4G30160. [O65570-2]
DR EnsemblPlants; AT4G30160.3; AT4G30160.3; AT4G30160. [O65570-1]
DR EnsemblPlants; AT4G30160.4; AT4G30160.4; AT4G30160. [O65570-1]
DR GeneID; 829139; -.
DR Gramene; AT4G30160.1; AT4G30160.1; AT4G30160. [O65570-1]
DR Gramene; AT4G30160.2; AT4G30160.2; AT4G30160. [O65570-2]
DR Gramene; AT4G30160.3; AT4G30160.3; AT4G30160. [O65570-1]
DR Gramene; AT4G30160.4; AT4G30160.4; AT4G30160. [O65570-1]
DR KEGG; ath:AT4G30160; -.
DR Araport; AT4G30160; -.
DR TAIR; locus:2128911; AT4G30160.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_1_1; -.
DR InParanoid; O65570; -.
DR OMA; DNRTKTH; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; O65570; -.
DR PRO; PR:O65570; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65570; baseline and differential.
DR Genevisible; O65570; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051764; P:actin crosslink formation; IDA:TAIR.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:TAIR.
DR GO; GO:0007015; P:actin filament organization; IMP:TAIR.
DR GO; GO:0051014; P:actin filament severing; IDA:TAIR.
DR GO; GO:0099636; P:cytoplasmic streaming; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP: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; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR Pfam; PF00626; Gelsolin; 4.
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 3D-structure; Actin capping; Actin-binding; Alternative splicing; Calcium;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..974
FT /note="Villin-4"
FT /id="PRO_0000218735"
FT REPEAT 29..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..305
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 394..451
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 532..572
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 634..675
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 909..974
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 738..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81645"
FT VAR_SEQ 635
FT /note="K -> KVRILLKSFF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056809"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:5VNT"
FT HELIX 933..939
FT /evidence="ECO:0007829|PDB:5VNT"
FT HELIX 942..949
FT /evidence="ECO:0007829|PDB:5VNT"
FT HELIX 953..958
FT /evidence="ECO:0007829|PDB:5VNT"
FT HELIX 961..970
FT /evidence="ECO:0007829|PDB:5VNT"
SQ SEQUENCE 974 AA; 109327 MW; E81BCBA2191ECB7D CRC64;
MSVSMRDLDP AFQGAGQKAG IEIWRIENFI PTPIPKSSIG KFFTGDSYIV LKTTALKTGA
LRHDIHYWLG KDTSQDEAGT AAVKTVELDA ALGGRAVQYR EVQGHETEKF LSYFKPCIIP
QEGGVASGFK HVVAEEHITR LFVCRGKHVV HVKEVPFARS SLNHDDIYIL DTKSKIFQFN
GSNSSIQERA KALEVVQYIK DTYHDGTCEV ATVEDGKLMA DADSGEFWGF FGGFAPLPRK
TANDEDKTYN SDITRLFCVE KGQANPVEGD TLKREMLDTN KCYILDCGIE VFVWMGRTTS
LDDRKIASKA AEEMIRSSER PKSQMIRIIE GFETVPFRSK FESWTQETNT TVSEDGRGRV
AALLQRQGVN VRGLMKAAPP KEEPQVFIDC TGNLQVWRVN GQAKTLLQAA DHSKFYSGDC
YVFQYSYPGE EKEEVLIGTW FGKQSVEEER GSAVSMASKM VESMKFVPAQ ARIYEGKEPI
QFFVIMQSFI VFKGGISSGY KKYIAEKEVD DDTYNENGVA LFRIQGSGPE NMQAIQVDPV
AASLNSSYYY ILHNDSSVFT WAGNLSTATD QELAERQLDL IKPNQQSRAQ KEGSESEQFW
ELLGGKAEYS SQKLTKEPER DPHLFSCTFT KEVLKVTEIY NFTQDDLMTE DIFIIDCHSE
IFVWVGQEVV PKNKLLALTI GEKFIEKDSL LEKLSPEAPI YVIMEGGEPS FFTRFFTSWD
SSKSAMHGNS FQRKLKIVKN GGTPVADKPK RRTPASYGGR ASVPDKSQQR SRSMSFSPDR
VRVRGRSPAF NALAATFESQ NARNLSTPPP VVRKLYPRSV TPDSSKFAPA PKSSAIASRS
ALFEKIPPQE PSIPKPVKAS PKTPESPAPE SNSKEQEEKK ENDKEEGSMS SRIESLTIQE
DAKEGVEDEE DLPAHPYDRL KTTSTDPVSD IDVTRREAYL SSEEFKEKFG MTKEAFYKLP
KWKQNKFKMA VQLF
