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VILI1_ARATH
ID   VILI1_ARATH             Reviewed;         909 AA.
AC   O81643; O82367; Q9SIK8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Villin-1 {ECO:0000303|PubMed:10631247};
GN   Name=VLN1 {ECO:0000303|PubMed:10631247};
GN   OrderedLocusNames=At2g29890 {ECO:0000312|Araport:AT2G29890};
GN   ORFNames=F6K5.2 {ECO:0000312|EMBL:AAD23629.2}, T27A16.1;
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], TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR
RP   LOCATION, ALTERNATIVE SPLICING, 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   FUNCTION.
RX   PubMed=15659626; DOI=10.1105/tpc.104.028555;
RA   Huang S., Robinson R.C., Gao L.Y., Matsumoto T., Brunet A., Blanchoin L.,
RA   Staiger C.J.;
RT   "Arabidopsis VILLIN1 generates actin filament cables that are resistant to
RT   depolymerization.";
RL   Plant Cell 17:486-501(2005).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
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: Binds actin and actin filament bundles in a
CC       Ca(2+)/calmodulin-insensitive manner, but is unable to sever, cap, and
CC       nucleate actin filament formation in vitro. Does not protect individual
CC       filaments from severing by VLN3 (AC O81645).
CC       {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:15659626,
CC       ECO:0000269|PubMed:20807878}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10631247}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O81643-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Mainly detected
CC       in the vascular tissue and the pericycle of roots and in the
CC       vasculature of leaves. Not expressed in the root cap.
CC       {ECO:0000269|PubMed:10631247, ECO:0000269|PubMed:20807878}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR   EMBL; AF081201; AAC31605.1; -; mRNA.
DR   EMBL; AC007113; AAD23629.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08315.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61989.1; -; Genomic_DNA.
DR   PIR; H84701; H84701.
DR   PIR; T50671; T50671.
DR   RefSeq; NP_001324173.1; NM_001336228.1. [O81643-1]
DR   RefSeq; NP_029567.1; NM_128543.4. [O81643-1]
DR   AlphaFoldDB; O81643; -.
DR   SMR; O81643; -.
DR   BioGRID; 2889; 1.
DR   STRING; 3702.AT2G29890.3; -.
DR   iPTMnet; O81643; -.
DR   PaxDb; O81643; -.
DR   ProteomicsDB; 242664; -. [O81643-1]
DR   EnsemblPlants; AT2G29890.1; AT2G29890.1; AT2G29890. [O81643-1]
DR   EnsemblPlants; AT2G29890.5; AT2G29890.5; AT2G29890. [O81643-1]
DR   GeneID; 817539; -.
DR   Gramene; AT2G29890.1; AT2G29890.1; AT2G29890. [O81643-1]
DR   Gramene; AT2G29890.5; AT2G29890.5; AT2G29890. [O81643-1]
DR   KEGG; ath:AT2G29890; -.
DR   Araport; AT2G29890; -.
DR   eggNOG; KOG0443; Eukaryota.
DR   InParanoid; O81643; -.
DR   OMA; FNWDYSK; -.
DR   PhylomeDB; O81643; -.
DR   PRO; PR:O81643; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O81643; baseline and differential.
DR   Genevisible; O81643; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IEA:UniProt.
DR   GO; GO:0051014; P:actin filament severing; IEA:InterPro.
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; IPR030010; Villin-1-like_plant.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   PANTHER; PTHR11977; PTHR11977; 1.
DR   PANTHER; PTHR11977:SF25; PTHR11977:SF25; 1.
DR   Pfam; PF00626; Gelsolin; 4.
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   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Alternative splicing; Calcium; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..909
FT                   /note="Villin-1"
FT                   /id="PRO_0000218732"
FT   REPEAT          29..79
FT                   /note="Gelsolin-like 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          149..189
FT                   /note="Gelsolin-like 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          262..305
FT                   /note="Gelsolin-like 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          391..448
FT                   /note="Gelsolin-like 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          529..569
FT                   /note="Gelsolin-like 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          631..672
FT                   /note="Gelsolin-like 6"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          844..909
FT                   /note="HP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT   REGION          733..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         780
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O65570"
FT   CONFLICT        8
FT                   /note="I -> F (in Ref. 1; AAC31605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347..353
FT                   /note="QTVESSL -> SDRWSLAF (in Ref. 1; AAC31605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585
FT                   /note="I -> T (in Ref. 1; AAC31605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="L -> V (in Ref. 1; AAC31605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   909 AA;  102950 MW;  4F04501BC4523FCC CRC64;
     MSRLSKDIDS AFQGVGTKSG LEIWCVYNKQ LISIPKSSFG KFHSGNAYLV LRTFLRKIES
     PQYDIHYWLG IDANEVDSIL ASDKALDLDA ALGCCTVQYR EVQGQETEKF LSYFKPCIIP
     VEGKYSPKTG IAGETYQVTL LRCKGDHVVR VKEVPFLRSS LNHDDVFILD TASKVFLFAG
     CNSSTQEKAK AMEVVEYIKD NKHDGRCEVA TIEDGKFSGD SDAGEFWSFF GGYAPIPKLS
     SSTTQEQTQT PCAELFWIDT KGNLHPTGTS SLDKDMLEKN KCYMLDCHSE VFVWMGRNTS
     LTERKTSISS SEEFLRKEGR STTTSLVLLT EGLENARFRS FFNKWPQTVE SSLYNEGREK
     VAALFKQKGY DVEELPDEED DPLYTNCRDN LKVWRVDGDD VSLLSIPDQT KLFTGDCYLV
     QYKYTYKERT EHLLYVWIGC ESIQQDRADA ITNASAIVGT TKGESVLCHI YQGNEPSRFF
     PMFQSLVVFK GGLSRRYKVL LAEKEKIGEE YNENKASLFR VVGTSPRNMQ AIQVNLVATS
     LNSSYSYILQ YGASAFTWIG KLSSDSDHEV LDRMLYFLDT SCQPIYIREG NETDTFWNLL
     GGKSEYPKEK EMRKQIEEPH LFTCSCSSDV LKVKEIYNFV QDDLTTEDVF LLDCQSEVYV
     WIGSNSNIKS KEEALTLGLK FLEMDILEEG LTMRTPVYVV TEGHEPPFFT RFFEWVPEKA
     NMHGNSFERK LASLKGKKTS TKRSSGSQYR SQSKDNASRD LQSRSVSSNG SERGVSPCSS
     EKLLSLSSAE DMTNSSNSTP VVKKLFSESL LVDPNDGVAR QESSSKSDIS KQKPRVGINS
     DLSSLESLAY SYEQLRVDSQ KPVTDIDATR REAYLTEKEF EERFGMAKSE FYALPKWKQN
     KLKISLHLF
 
 
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