VILI2_ARATH
ID VILI2_ARATH Reviewed; 976 AA.
AC O81644; O22946; Q0WV87; Q8RXZ3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Villin-2 {ECO:0000303|PubMed:10631247};
GN Name=VLN2 {ECO:0000303|PubMed:10631247};
GN OrderedLocusNames=At2g41740 {ECO:0000312|Araport:AT2G41740};
GN ORFNames=T11A7.16 {ECO:0000312|EMBL:AAC02774.2};
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [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, AND TISSUE SPECIFICITY.
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).
RN [9]
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: Ca(2+)-regulated actin-binding protein. Involved in actin
CC filaments bundling. Caps the barbed end of actin filaments and is able
CC to sever them in a calcium-dependent manner. Required for the
CC construction of actin collars in pollen tubes. Acts redundantly with
CC VLN5 (AC Q9LVC6) to generate thick actin filament bundles and to
CC regulate polarized pollen tube growth (PubMed:23715472). Acts
CC redundantly with VLN3 (AC O81645) to regulate directional organ growth
CC and in sclerenchyma development (PubMed:22209875, PubMed:22563899,
CC respectively). {ECO:0000269|PubMed:10631247,
CC ECO:0000269|PubMed:22209875, ECO:0000269|PubMed:22563899,
CC ECO:0000269|PubMed:23715472}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:23715472}.
CC Note=Present in the apical and subapical regions of pollen tubes.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Mainly detected
CC in the root epidermis and vasculature. Expressed in the root cap.
CC {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:22209875,
CC ECO:0000269|PubMed:22563899}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no visible effect on
CC pollen tube growth. Decreased severing frequency of actin filaments.
CC Vln2 and vln5 double mutants have pollen tubes curled and wider at some
CC regions along the tube. They accumulate actin filaments at the tips of
CC pollen tubes (PubMed:23715472). Vln2 and vln3 double mutants show
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, ECO:0000269|PubMed:23715472}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF081202; AAC31606.1; -; mRNA.
DR EMBL; AC002339; AAC02774.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10027.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61457.1; -; Genomic_DNA.
DR EMBL; AY080601; AAL85012.1; -; mRNA.
DR EMBL; AY133782; AAM91716.1; -; mRNA.
DR EMBL; AK226882; BAE98961.1; -; mRNA.
DR PIR; E84845; E84845.
DR PIR; T50669; T50669.
DR RefSeq; NP_001323674.1; NM_001336936.1.
DR RefSeq; NP_565958.1; NM_129738.5.
DR AlphaFoldDB; O81644; -.
DR SMR; O81644; -.
DR BioGRID; 4110; 2.
DR IntAct; O81644; 1.
DR STRING; 3702.AT2G41740.1; -.
DR iPTMnet; O81644; -.
DR PaxDb; O81644; -.
DR PRIDE; O81644; -.
DR ProteomicsDB; 242777; -.
DR EnsemblPlants; AT2G41740.1; AT2G41740.1; AT2G41740.
DR EnsemblPlants; AT2G41740.2; AT2G41740.2; AT2G41740.
DR GeneID; 818773; -.
DR Gramene; AT2G41740.1; AT2G41740.1; AT2G41740.
DR Gramene; AT2G41740.2; AT2G41740.2; AT2G41740.
DR KEGG; ath:AT2G41740; -.
DR Araport; AT2G41740; -.
DR TAIR; locus:2054401; AT2G41740.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_0_1; -.
DR InParanoid; O81644; -.
DR OMA; DPNIWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; O81644; -.
DR PRO; PR:O81644; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81644; baseline and differential.
DR Genevisible; O81644; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051017; P:actin filament bundle assembly; IGI:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
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; IPR030009; Villin-2_plant.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 2.
DR PANTHER; PTHR11977:SF114; PTHR11977:SF114; 2.
DR Pfam; PF00626; Gelsolin; 5.
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..976
FT /note="Villin-2"
FT /id="PRO_0000218733"
FT REPEAT 27..77
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 148..188
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 260..302
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 399..450
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 531..571
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 633..674
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 911..976
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 769..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81645"
FT CONFLICT 99
FT /note="E -> V (in Ref. 1; AAC31606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 107842 MW; F10BAB629A0A957E CRC64;
MSTKVLDPAF QGAGQKPGTE IWRIENFEAV PVPKSEHGKF YMGDTYIVLQ TTQNKGGAYL
FDIHFWIGKD TSQDEAGTAA VKTVELDAVL GGRAVQHREI QGHESDKFLS YFKPCIIPLE
GGVASGFKTV EEEVFETRLY TCKGKRAIRL KQVPFARSSL NHDDVFILDT EEKIYQFNGA
NSNIQERAKA LEVVQYLKDK YHEGTCDVAI VDDGKLDTES DSGAFWVLFG GFAPIGRKVA
NDDDIVPEST PPKLYCITDG KMEPIDGDLS KSMLENTKCY LLDCGAEIYI WVGRVTQVDE
RKAASQSAEE FLASENRPKA THVTRVIQGY ESHSFKSNFD SWPSGSATPG NEEGRGKVAA
LLKQQGVGLK GIAKSAPVNE DIPPLLESGG KLEVWYVNGK VKTPLPKEDI GKLYSGDCYL
VLYTYHSGER KDEYFLSCWF GKKSIPEDQD TAIRLANTMS NSLKGRPVQG RIYEGKEPPQ
FVALFQPMVV LKGGLSSGYK SSMGESESTD ETYTPESIAL VQVSGTGVHN NKAVQVETVA
TSLNSYECFL LQSGTSMFLW HGNQSTHEQL ELATKVAEFL KPGITLKHAK EGTESSTFWF
ALGGKQNFTS KKASSETIRD PHLFSFAFNR GKFQVEEIYN FAQDDLLTED IYFLDTHAEV
FVWVGQCVEP KEKQTVFEIG QKYIDLAGSL EGLHPKVPIY KINEGNEPCF FTTYFSWDAT
KAIVQGNSFQ KKASLLFGTH HVVEDKSNGG NQGLRQRAEA LAALNSAFNS SSNRPAYSSQ
DRLNESHDGP RQRAEALAAL SSAFNSSSSS TKSPPPPRPV GTSQASQRAA AVAALSQVLV
AENKKSPDTS PTRRSTSSNP ADDIPLTEAK DEEEASEVAG LEAKEEEEVS PAADETEAKQ
ETEEQGDSEI QPSGATFTYE QLRAKSENPV TGIDFKRREA YLSEEEFQSV FGIEKEAFNN
LPRWKQDLLK KKFDLF
