ID VLN2_ORYSJ Reviewed; 966 AA.
AC Q10L71;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE RecName: Full=Villin-2 {ECO:0000303|PubMed:20807878};
GN Name=VLN2 {ECO:0000303|PubMed:20807878};
GN OrderedLocusNames=LOC_Os03g24220 {ECO:0000312|EMBL:ABF96038.1},
GN Os03g0356700 {ECO:0000312|EMBL:BAF12054.1};
GN ORFNames=OSNPB_030356700 {ECO:0000312|EMBL:BAS84252.1};
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP 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).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Kitaake;
RX PubMed=26486445; DOI=10.1105/tpc.15.00581;
RA Wu S., Xie Y., Zhang J., Ren Y., Zhang X., Wang J., Guo X., Wu F.,
RA Sheng P., Wang J., Wu C., Wang H., Huang S., Wan J.;
RT "VLN2 regulates plant architecture by affecting microfilament dynamics and
RT polar auxin transport in rice.";
RL Plant Cell 27:2829-2845(2015).
CC -!- FUNCTION: Ca(2+)-regulated actin-binding protein (By similarity). Binds
CC actin microfilaments (MFs). Involved in actin filament bundling,
CC severing and capping. Caps the barbed end of actin filaments and is
CC able to sever them in a calcium-dependent manner. May regulate cell
CC expansion in developing organs. Required for the regulation of plant
CC architecture via the modulation of polar auxin transport and root
CC gravitropism (PubMed:26486445). {ECO:0000250|UniProtKB:O81644,
CC ECO:0000269|PubMed:26486445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O81644}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in growing tissues.
CC {ECO:0000269|PubMed:26486445}.
CC -!- DISRUPTION PHENOTYPE: Malformed organs, including twisted roots and
CC shoots at the seedling stage, mainly caused by asymmetrical expansion
CC of cells on the opposite sides of an organ. Increased dynamic actin
CC cytoskeleton network. Hypersensitive gravitropic response, faster
CC recycling of PIN2, and altered auxin distribution.
CC {ECO:0000269|PubMed:26486445}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; DP000009; ABF96038.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12054.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS84252.1; -; Genomic_DNA.
DR RefSeq; XP_015631607.1; XM_015776121.1.
DR AlphaFoldDB; Q10L71; -.
DR SMR; Q10L71; -.
DR STRING; 39947.Q10L71; -.
DR PaxDb; 39947-Q10L71; -.
DR EnsemblPlants; Os03t0356700-01; Os03t0356700-01; Os03g0356700.
DR GeneID; 4332869; -.
DR Gramene; Os03t0356700-01; Os03t0356700-01; Os03g0356700.
DR KEGG; osa:4332869; -.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_2_0_1; -.
DR InParanoid; Q10L71; -.
DR OMA; DPNIWSA; -.
DR OrthoDB; 25995at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q10L71; baseline and differential.
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:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.40.20.10; Severin; 6.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
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; VILLIN; 1.
DR PANTHER; PTHR11977:SF98; VILLIN-2; 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; SSF55753; Actin depolymerizing proteins; 6.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Auxin signaling pathway; Calcium; Cytoplasm;
KW Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..966
FT /note="Villin-2"
FT /id="PRO_0000438160"
FT REPEAT 29..112
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..221
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 273..338
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 414..487
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 535..604
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 645..716
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 901..966
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 771..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106120 MW; 8EC0D8CA76E0C6B6 CRC64;
MSSAKPVLDP AFQGVGQKPG TEIWRIQDFK PVPLPKADYG KFYNGDSYIV LQTTCSKGGG
AYLFDIHFWI GKDSSQDEAG TAAIKTVELD TMLGGRAVQH RELQGYESDK FLSYFKPCII
PLEGGFASGF KTPEEDKFET RLYICKGKRA IRVKEVPFAR SSLNHDDVFI LDTEKKIYQF
NGANSNIQER AKALEAIQHL KETYHNGVCD VAIVDDGKLQ AESDSGEFWV LFGGFAPIGK
KAICDDDVVL ETTAPKLYSI NNGQLKLEDT VLTKSILENN KCFLVDCGSD LFIWVGRLTQ
VEERKAASAA VEEFIATQNR PKTTRVTRVI QGYENHTFKS KFESWPVNSA GSAGAEEGRG
KVAALLKQQG VDIKGASKSS APVDEEVPPL LEGDGKLEVY CVNGSAKTAL PKEELGKFYS
GDCYIVLYTY HSGDKREEFY LTYWIGKDSI PEDQEMAFQT ANSIWNSLKG RPILGRIYQG
KEPPQFIALF QPMVILKGGI SSGYQKFVEE KGLKDETYSG DGIALFRISG TSIHNNKVLQ
VDAVSSNLSP TDCFVLQSGN SMFTWIGNAS SYEQQQWAAK VAEFLKPGVA VKHCKEGTES
SAFWFALGGK QNYTSRNATH DVVREPHLYT FSLRNGKLEV TEIFNFSQDD LLTEDMMVLD
THGEVFVWMG QCVDAKEKQK AFEIGQKYAE HAAAFESLSP DVPLYKVVEG NEPCFFRTYF
SWDNTRSVIH GNSFQKKLSL LFGMRSESGS KSSGDGGPTQ RASALAALSS AFNPSSQKNK
GNDRPKSSDG GPTQRASAMA ALTSAFNPSA KPKSPPQRAG QGSQRAAAVA ALSNVLTAEG
SSQSPRIGDA DTAELTPSAA SPLSEGASEF SADKDAPGDG ALSEGGRTEP DVSVEQTANE
NGGETTFSYD RLISKSTNPV RGIDYKRRET YLSDSEFQTV FGITKEEFYQ QPGWKQELQK
RKHDLF
//
