VLN1_ORYSI
ID VLN1_ORYSI Reviewed; 849 AA.
AC B8AY58;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Villin-1 {ECO:0000250|UniProtKB:Q0DKN3};
GN Name=VLN1 {ECO:0000250|UniProtKB:Q0DKN3};
GN ORFNames=OsI_18497 {ECO:0000312|EMBL:EEC78540.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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:0000250|UniProtKB:Q0DKN3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O81644}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; CM000130; EEC78540.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AY58; -.
DR SMR; B8AY58; -.
DR STRING; 39946.B8AY58; -.
DR EnsemblPlants; BGIOSGA019199-TA; BGIOSGA019199-PA; BGIOSGA019199.
DR Gramene; BGIOSGA019199-TA; BGIOSGA019199-PA; BGIOSGA019199.
DR HOGENOM; CLU_002568_2_1_1; -.
DR OMA; FNWDYSK; -.
DR Proteomes; UP000007015; 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; ISS:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; 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 3: Inferred from homology;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..849
FT /note="Villin-1"
FT /id="PRO_0000438164"
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; 95220 MW; 98A409EC66CF7F66 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
EYSKEKQVKD WPADPHLYTC HFEQGLFKAK EVFSFSQDDL VTEEILILDC VEELHIWVGH
QSGVLSMEQA LDIGKMFLQA GIHQDGRRPI DTTMYIVTEG DEPRFFTSFF NWDYSKQTML
GNSFERKLAI LKGISQKLET PERSLRKSSS SSLPRRSPGT SSSEPTTPEQ RAAARTFASA
STGKLLRERS PAALSPSLST PSPSPRSRSS ASSSPASWNS TPSTVARRLF PPSLHASAEA
VATGTPRRL
