VLN3_ORYSJ
ID VLN3_ORYSJ Reviewed; 970 AA.
AC Q67U26; B9FQC0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Villin-3 {ECO:0000303|PubMed:20807878};
GN Name=VLN3 {ECO:0000303|PubMed:20807878};
GN OrderedLocusNames=LOC_Os06g44890 {ECO:0000305},
GN Os06g0659300 {ECO:0000312|EMBL:BAF20177.1};
GN ORFNames=B1047G05.32 {ECO:0000312|EMBL:BAD38345.1},
GN OsJ_22231 {ECO:0000312|EMBL:EEE66162.1},
GN OSJNBa0051O02.4 {ECO:0000312|EMBL:BAD46401.1},
GN OSNPB_060659300 {ECO:0000312|EMBL:BAS98964.1};
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+)-regulated 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 is able to sever
CC them in a calcium-dependent manner. MF severing is promoted by VLN1.
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 and in epidermal cells of the elongation zone
CC and root hairs. Also detected in guard cells.
CC {ECO:0000269|PubMed:20807878}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD38345.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD46401.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF20177.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS98964.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE66162.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005760; BAD38345.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP005769; BAD46401.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008212; BAF20177.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014962; BAS98964.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000143; EEE66162.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015643765.1; XM_015788279.1.
DR RefSeq; XP_015643767.1; XM_015788281.1.
DR AlphaFoldDB; Q67U26; -.
DR SMR; Q67U26; -.
DR STRING; 4530.OS06T0659300-01; -.
DR iPTMnet; Q67U26; -.
DR PaxDb; Q67U26; -.
DR PRIDE; Q67U26; -.
DR GeneID; 4341731; -.
DR KEGG; osa:4341731; -.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_1_1; -.
DR InParanoid; Q67U26; -.
DR OrthoDB; 1376537at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0032432; C:actin filament bundle; IDA: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; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
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; IPR036180; Gelsolin-like_dom_sf.
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; 6.
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 SUPFAM; SSF82754; SSF82754; 1.
DR PROSITE; PS51089; HP; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..970
FT /note="Villin-3"
FT /id="PRO_0000438165"
FT REPEAT 31..111
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 151..219
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 273..339
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 416..484
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 536..576
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 643..714
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 905..970
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 741..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 108722 MW; 66F8759168D11DCE CRC64;
MAVSMREVDA VFQGAGQKDG LEIWRIEKLQ AVPVPKESHG RFFTGDSYVI LKTTALKNGS
FRHDIHYWLG KDTSQDEAGT AAIKTVELDA ALGGRAVQYR EVQGNETERF LSYFKPCIIP
EEGGIASGFR HTEINEREHV TRLFVCRGKH TVHVKEVPFA RSSLNHDDIF ILDTKSKIFQ
FNGSNSSIQE RAKALEVVQY LKDSNHEGKC DVGSVEDGKL MADADAGEFW GLFGGFAPLP
RKTFSDLNGK DSAFSSKLIC LNKGQTVPVD FDVLTRELLD STKCYLLDCG SEIYVWMGRE
TPLEERKRAG SAAEELLREV NRPKSHIVRL MEGFETVIFR SKFSKWPKKA DAVVSDESRG
KVAALLKRQG FNVKGLAKAA PVKEEPQPQI DCTGNLQVWR VNGTEKTFLS FSEQCKFYSG
DCYIFQYSYP GEEGEECLIG TWFGKKSVQD EKTTAISVAS KMVESLKFQA VMVRLYEGKE
PAEFFSIFQN LVIFKGGVST GYKKFVSENG IEDDTYSENG VALFRVQGSG PENMQAIQVD
TAATSLNSSY CYVLHDGDTL FTWIGNLSSS MDQELAERQL DVIKPNLQSR MLKEGSEYDQ
FWKLLGVKSE YPSQKIAKDQ ESDPHLFSCT FSKGVLKVRE IFNFTQDDLM TEDVFILDCH
SCVFVWVGQR VDTKMRAQAL SVGEKFLELD ILMENSSQET PVYVITEGSE PQFFTRFFTW
DSAKSAMHGN SFERRLSIVK DGVKPKLDKP KRRPTTSSSH TGRSSVPEKS QRSRSMSFSP
DRVRVRGRSP AFNALAANFE NPNARNLSTP PPAIRKPSPK SPSSDPTKPP QRAASIAAIS
ASFERPRPTL IPKSIKASPD VNKPQVEASK PKPEANGKDS TPSKDSPTVT PTIQEDLKEG
QPENEEGLPV YPYERLRTSS INPVTDIDVT KRETYLSAAE FRERFGMTKE AFAKLPKWKQ
NRLKIALQLF
