VILI5_ARATH
ID VILI5_ARATH Reviewed; 962 AA.
AC Q9LVC6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Villin-5 {ECO:0000303|PubMed:20807879};
GN Name=VLN5 {ECO:0000303|PubMed:20807879};
GN OrderedLocusNames=At5g57320 {ECO:0000312|Araport:AT5G57320};
GN ORFNames=MJB24.13 {ECO:0000312|EMBL:BAA96955.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20807879; DOI=10.1105/tpc.110.076257;
RA Zhang H., Qu X., Bao C., Khurana P., Wang Q., Xie Y., Zheng Y., Chen N.,
RA Blanchoin L., Staiger C.J., Huang S.;
RT "Arabidopsis VILLIN5, an actin filament bundling and severing protein, is
RT necessary for normal pollen tube growth.";
RL Plant Cell 22:2749-2767(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23715472; DOI=10.1105/tpc.113.110940;
RA Qu X., Zhang H., Xie Y., Wang J., Chen N., Huang S.;
RT "Arabidopsis villins promote actin turnover at pollen tube tips and
RT facilitate the construction of actin collars.";
RL Plant Cell 25:1803-1817(2013).
CC -!- FUNCTION: Major actin filament stabilizing factor and regulator of
CC actin dynamics. 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. Required for the
CC construction of actin collars in pollen tubes. Acts synergistically
CC with VLN2 (AC O81644) to regulate polarized pollen tube growth.
CC {ECO:0000269|PubMed:20807879, ECO:0000269|PubMed:23715472}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23715472}. Note=Present in the apical and subapical
CC regions of pollen tubes. {ECO:0000269|PubMed:23715472}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, but expressed preferentially in pollen
CC and stamens. {ECO:0000269|PubMed:20807879}.
CC -!- DISRUPTION PHENOTYPE: Retarded pollen tube growth, but no effect on
CC pollen germination, root hair growth, organization or amount of
CC filamentous actin in pollen grains or tubes. Increased sensitivity to
CC latrunculin B (LatB) and instability of actin filaments in pollen
CC tubes. Decreased severing frequency of actin filaments. Vln2 and vln5
CC double mutants have pollen tubes curled and wider at some regions along
CC the tube. They accumulate actin filaments at the tips of pollen tubes
CC (PubMed:23715472). {ECO:0000269|PubMed:20807879,
CC ECO:0000269|PubMed:23715472}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB019233; BAA96955.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96884.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70704.1; -; Genomic_DNA.
DR RefSeq; NP_001318818.1; NM_001345256.1.
DR RefSeq; NP_001332290.1; NM_001345257.1.
DR AlphaFoldDB; Q9LVC6; -.
DR SMR; Q9LVC6; -.
DR STRING; 3702.AT5G57320.1; -.
DR iPTMnet; Q9LVC6; -.
DR PaxDb; Q9LVC6; -.
DR PRIDE; Q9LVC6; -.
DR ProteomicsDB; 242542; -.
DR EnsemblPlants; AT5G57320.1; AT5G57320.1; AT5G57320.
DR EnsemblPlants; AT5G57320.2; AT5G57320.2; AT5G57320.
DR GeneID; 835837; -.
DR Gramene; AT5G57320.1; AT5G57320.1; AT5G57320.
DR Gramene; AT5G57320.2; AT5G57320.2; AT5G57320.
DR KEGG; ath:AT5G57320; -.
DR Araport; AT5G57320; -.
DR TAIR; locus:2165570; AT5G57320.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_1_1; -.
DR InParanoid; Q9LVC6; -.
DR OMA; WRINCEE; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q9LVC6; -.
DR PRO; PR:Q9LVC6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVC6; baseline and differential.
DR Genevisible; Q9LVC6; 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 GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..962
FT /note="Villin-5"
FT /id="PRO_0000430591"
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 396..453
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 534..574
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 636..677
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 897..962
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 749..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O65570"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O65570"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81645"
SQ SEQUENCE 962 AA; 107826 MW; 6BB6E0C1DD6D49C2 CRC64;
MTFSMRDLDQ ALQGAGQKSG IEIWRIENFK PVTVPQESHG KFFTGDSYIV LKTTASRSGS
LHHDIHYWLG KDSSQDEAGA VAVMTVELDS ALGGRAVQYR EVQGHETEKF LSYFKPCIIP
QEGGVASGFN HVKPEEHQTR LYICKGKHVV RVKEVPFVRS TLNHEDVFIL DTESKIFQFS
GSKSSIQERA KALEVVQYIK DTYHDGKCDI AAVEDGRMMA DAEAGEFWGL FGGFAPLPKK
PAVNDDETAA SDGIKLFSVE KGQTDAVEAE CLTKELLDTN KCYILDCGLE LFVWKGRSTS
IDQRKSATEA AEEFFRSSEP PKSNLVSVME GYETVMFRSK FDSWPASSTI AEPQQGRGKV
AALLQRQGVN VQGLVKTSSS SSKDEPKPYI DGTGNLQVWR INCEEKILLE AAEQSKFYSG
DCYILQYSYP GEDREEHLVG TWFGKQSVEE DRASAISLAN KMVESMKFVP AQARINEGKE
PIQFFVIMQS FITFKGGVSD AFKKYIAEND IPDTTYEAEG VALFRVQGSG PENMQAIQIE
AASAGLNSSH CYILHGDSTV FTWCGNLTSS EDQELMERML DLIKPNEPTK AQKEGSESEQ
FWELLGGKSE YPSQKIKRDG ESDPHLFSCT YTNESLKATE IFNFTQDDLM TEDIFILDCH
TEVFVWVGQQ VDPKKKPQAL DIGENFLKHD FLLENLASET PIYIVTEGNE PPFFTRFFTW
DSSKSGMHGD SFQRKLAILT NKGKPLLDKP KRRVPAYSSR STVPDKSQPR SRSMTFSPDR
ARVRGRSPAF NALAANFEKL NIRNQSTPPP MVSPMVRKLY PKSHAPDLSK IAPKSAIAAR
TALFEKPTPT SQEPPTSPSS SEATNQAEAP KSTSETNEEE AMSSINEDSK EEEAEEESSL
PTFPYERLKT DSEDPVSDVD LTRREAYLTS VEFKEKFEMT KNEFYKLPKW KQNKLKMSVN
LF
