VLN1_ORYSJ
ID VLN1_ORYSJ Reviewed; 849 AA.
AC Q0DKN3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Villin-1 {ECO:0000303|PubMed:20807878};
GN Name=VLN1 {ECO:0000303|PubMed:20807878};
GN OrderedLocusNames=LOC_Os05g06110 {ECO:0000305},
GN Os05g0153000 {ECO:0000312|EMBL:BAF16590.1};
GN ORFNames=OsJ_17157 {ECO:0000312|EMBL:EEE62368.1},
GN OSNPB_050153000 {ECO:0000312|EMBL:BAS92329.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
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: Ca(2+)-independent actin-binding protein. Binds actin
CC microfilaments (MFs). Involved in actin filament bundling, severing and
CC capping. Caps the barbed end of actin filaments and protects them from
CC disassembly. Promotes VLN3-mediated MF severing.
CC {ECO:0000269|PubMed:20807878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O81644}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, young leaves, and
CC inflorescences, mostly in the vasculature of roots, leaves, and
CC filaments of the anthers. Also detected in guard cells.
CC {ECO:0000269|PubMed:20807878}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AP008211; BAF16590.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92329.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62368.1; -; Genomic_DNA.
DR RefSeq; XP_015637915.1; XM_015782429.1.
DR AlphaFoldDB; Q0DKN3; -.
DR SMR; Q0DKN3; -.
DR STRING; 4530.OS05T0153000-01; -.
DR PaxDb; Q0DKN3; -.
DR PRIDE; Q0DKN3; -.
DR EnsemblPlants; Os05t0153000-01; Os05t0153000-01; Os05g0153000.
DR EnsemblPlants; Os05t0153000-02; Os05t0153000-02; Os05g0153000.
DR GeneID; 4337837; -.
DR Gramene; Os05t0153000-01; Os05t0153000-01; Os05g0153000.
DR Gramene; Os05t0153000-02; Os05t0153000-02; Os05g0153000.
DR KEGG; osa:4337837; -.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_1_1; -.
DR InParanoid; Q0DKN3; -.
DR OMA; FNWDYSK; -.
DR OrthoDB; 1376537at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0032432; C:actin filament bundle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR030010; Villin-1-like_plant.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF25; PTHR11977:SF25; 1.
DR Pfam; PF00626; Gelsolin; 5.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..849
FT /note="Villin-1"
FT /id="PRO_0000438159"
FT REPEAT 30..107
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 147..213
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 262..335
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 405..475
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 527..566
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REGION 739..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 95314 MW; E82F97DA66CDC644 CRC64;
MKGVDDAFLG VGDKPGLDIW CIMGSNLIAI EKSLHGKFYT GNTYIILSTV ELKSGVRQHN
VHYWVGEEAK EEDCLTASDK AIELDVALGS NTVQYRETQG EESDKFLSYF KPCIIPIQGS
LSSHMRIYGD KSKDTTMFRC EGEHVARVTE VPFSRSSLDH KAVFVVDTES KIFLFSGCNS
SMQTRAKALD VVKHLKENRH CGRCEIATIE DGKLVGDSDA GDFWNLFGGY APIPRDVQDT
VMTELMTTSS KKLFWINKRN LVPVETNLLE REMLNSDRNY ILDCGTEVFL WMGMTTLVSE
RRTSVTALED YVRCEGRQSN ARSVILTEGH ETVEFKMHFQ HWPKNAVPKL YEAGREKVAA
IFKHQGYDVT EIPEDKPRHF ISCNGSLKVW LVDNGSVTLL CTEEQEQLYN GDCYIIRYSY
IEDGKDYHLF FAWSGLNSIN EDRVAAASLM SGMIDSVKGH AVVAQVFEGR EPEMFFLVFK
SLIIFKGGRS MAYKNFVSQR SDANGWYQKN GVALFRVQGL KHDCIRAIQV DLAASSLNSS
HCYILQAGGS FFTWLGSLSS PSDHNLLDRM MDKLCPLKQS LLVREGSEPD RFWEALGGRS
EYLREKQVKD WPADPHLYTC HFEQGLFKAK EVFSFSQDDL VTEEILILDC VEELHIWVGH
QSGVLSKEQA LDIGKMFLQA GIHQDGRRPI DTTMYIVTEG DEPRFFTSFF NWDYSKQTML
GNSFERKLAI LKGISQKLET PERSLRKSSS SSLPRRSPGT SSSEPTTPEQ RAAARTFASA
STGKLLRERS PAALSPSLST PSPSPRSRSS ASSSPASWNS TPSTVARRLF PPSLHASAEA
VATGTPRRR
