ID VILI1_ARATH Reviewed; 909 AA.
AC O81643; O82367; Q9SIK8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Villin-1 {ECO:0000303|PubMed:10631247};
GN Name=VLN1 {ECO:0000303|PubMed:10631247};
GN OrderedLocusNames=At2g29890 {ECO:0000312|Araport:AT2G29890};
GN ORFNames=F6K5.2 {ECO:0000312|EMBL:AAD23629.2}, T27A16.1;
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, SUBCELLULAR
RP LOCATION, ALTERNATIVE SPLICING, GENE FAMILY, AND 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 FUNCTION.
RX PubMed=15659626; DOI=10.1105/tpc.104.028555;
RA Huang S., Robinson R.C., Gao L.Y., Matsumoto T., Brunet A., Blanchoin L.,
RA Staiger C.J.;
RT "Arabidopsis VILLIN1 generates actin filament cables that are resistant to
RT depolymerization.";
RL Plant Cell 17:486-501(2005).
RN [5]
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).
CC -!- FUNCTION: Binds actin and actin filament bundles in a
CC Ca(2+)/calmodulin-insensitive manner, but is unable to sever, cap, and
CC nucleate actin filament formation in vitro. Does not protect individual
CC filaments from severing by VLN3 (AC O81645).
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:15659626,
CC ECO:0000269|PubMed:20807878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10631247}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81643-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Mainly detected
CC in the vascular tissue and the pericycle of roots and in the
CC vasculature of leaves. Not expressed in the root cap.
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:20807878}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF081201; AAC31605.1; -; mRNA.
DR EMBL; AC007113; AAD23629.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08315.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61989.1; -; Genomic_DNA.
DR PIR; H84701; H84701.
DR PIR; T50671; T50671.
DR RefSeq; NP_001324173.1; NM_001336228.1. [O81643-1]
DR RefSeq; NP_029567.1; NM_128543.4. [O81643-1]
DR AlphaFoldDB; O81643; -.
DR SMR; O81643; -.
DR BioGRID; 2889; 1.
DR STRING; 3702.O81643; -.
DR iPTMnet; O81643; -.
DR PaxDb; 3702-AT2G29890-3; -.
DR ProteomicsDB; 242664; -. [O81643-1]
DR EnsemblPlants; AT2G29890.1; AT2G29890.1; AT2G29890. [O81643-1]
DR EnsemblPlants; AT2G29890.5; AT2G29890.5; AT2G29890. [O81643-1]
DR GeneID; 817539; -.
DR Gramene; AT2G29890.1; AT2G29890.1; AT2G29890. [O81643-1]
DR Gramene; AT2G29890.5; AT2G29890.5; AT2G29890. [O81643-1]
DR KEGG; ath:AT2G29890; -.
DR Araport; AT2G29890; -.
DR TAIR; AT2G29890; VLN1.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; O81643; -.
DR OMA; EMFFLVF; -.
DR PhylomeDB; O81643; -.
DR PRO; PR:O81643; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81643; baseline and differential.
DR Genevisible; O81643; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IEA:UniProt.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.40.20.10; Severin; 6.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
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; VILLIN; 1.
DR PANTHER; PTHR11977:SF25; VILLIN-1; 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; SSF55753; Actin depolymerizing proteins; 6.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Alternative splicing; Calcium; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..909
FT /note="Villin-1"
FT /id="PRO_0000218732"
FT REPEAT 29..79
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 149..189
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 262..305
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 391..448
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 529..569
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 631..672
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 844..909
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 733..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O65570"
FT CONFLICT 8
FT /note="I -> F (in Ref. 1; AAC31605)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..353
FT /note="QTVESSL -> SDRWSLAF (in Ref. 1; AAC31605)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="I -> T (in Ref. 1; AAC31605)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="L -> V (in Ref. 1; AAC31605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 102950 MW; 4F04501BC4523FCC CRC64;
MSRLSKDIDS AFQGVGTKSG LEIWCVYNKQ LISIPKSSFG KFHSGNAYLV LRTFLRKIES
PQYDIHYWLG IDANEVDSIL ASDKALDLDA ALGCCTVQYR EVQGQETEKF LSYFKPCIIP
VEGKYSPKTG IAGETYQVTL LRCKGDHVVR VKEVPFLRSS LNHDDVFILD TASKVFLFAG
CNSSTQEKAK AMEVVEYIKD NKHDGRCEVA TIEDGKFSGD SDAGEFWSFF GGYAPIPKLS
SSTTQEQTQT PCAELFWIDT KGNLHPTGTS SLDKDMLEKN KCYMLDCHSE VFVWMGRNTS
LTERKTSISS SEEFLRKEGR STTTSLVLLT EGLENARFRS FFNKWPQTVE SSLYNEGREK
VAALFKQKGY DVEELPDEED DPLYTNCRDN LKVWRVDGDD VSLLSIPDQT KLFTGDCYLV
QYKYTYKERT EHLLYVWIGC ESIQQDRADA ITNASAIVGT TKGESVLCHI YQGNEPSRFF
PMFQSLVVFK GGLSRRYKVL LAEKEKIGEE YNENKASLFR VVGTSPRNMQ AIQVNLVATS
LNSSYSYILQ YGASAFTWIG KLSSDSDHEV LDRMLYFLDT SCQPIYIREG NETDTFWNLL
GGKSEYPKEK EMRKQIEEPH LFTCSCSSDV LKVKEIYNFV QDDLTTEDVF LLDCQSEVYV
WIGSNSNIKS KEEALTLGLK FLEMDILEEG LTMRTPVYVV TEGHEPPFFT RFFEWVPEKA
NMHGNSFERK LASLKGKKTS TKRSSGSQYR SQSKDNASRD LQSRSVSSNG SERGVSPCSS
EKLLSLSSAE DMTNSSNSTP VVKKLFSESL LVDPNDGVAR QESSSKSDIS KQKPRVGINS
DLSSLESLAY SYEQLRVDSQ KPVTDIDATR REAYLTEKEF EERFGMAKSE FYALPKWKQN
KLKISLHLF
//
