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VLN5_ORYSJ
ID   VLN5_ORYSJ              Reviewed;         955 AA.
AC   Q0J716;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Villin-5 {ECO:0000303|PubMed:20807878};
GN   Name=VLN5 {ECO:0000303|PubMed:20807878};
GN   OrderedLocusNames=LOC_Os08g14230 {ECO:0000305},
GN   Os08g0240800 {ECO:0000312|EMBL:BAF23249.1};
GN   ORFNames=OSNPB_080240800 {ECO:0000312|EMBL:BAT04494.1};
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   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 (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 (By similarity).
CC       {ECO:0000250|UniProtKB:O81644, ECO:0000250|UniProtKB:Q10L71}.
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; AP008214; BAF23249.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04494.1; -; Genomic_DNA.
DR   RefSeq; XP_015650776.1; XM_015795290.1.
DR   AlphaFoldDB; Q0J716; -.
DR   SMR; Q0J716; -.
DR   STRING; 4530.OS08T0240800-01; -.
DR   PaxDb; Q0J716; -.
DR   PRIDE; Q0J716; -.
DR   EnsemblPlants; Os08t0240800-01; Os08t0240800-01; Os08g0240800.
DR   GeneID; 4345036; -.
DR   Gramene; Os08t0240800-01; Os08t0240800-01; Os08g0240800.
DR   KEGG; osa:4345036; -.
DR   eggNOG; KOG0443; Eukaryota.
DR   HOGENOM; CLU_002568_2_1_1; -.
DR   InParanoid; Q0J716; -.
DR   OMA; DNRTKTH; -.
DR   OrthoDB; 1376537at2759; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
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; 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; 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   SUPFAM; SSF82754; SSF82754; 1.
DR   PROSITE; PS51089; HP; 1.
PE   3: Inferred from homology;
KW   Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW   Reference proteome; Repeat.
FT   CHAIN           1..955
FT                   /note="Villin-5"
FT                   /id="PRO_0000438168"
FT   REPEAT          29..111
FT                   /note="Gelsolin-like 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          152..218
FT                   /note="Gelsolin-like 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          274..339
FT                   /note="Gelsolin-like 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          644..712
FT                   /note="Gelsolin-like 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          890..955
FT                   /note="HP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT   REGION          741..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   955 AA;  107343 MW;  1824027EE30EF6FA CRC64;
     MSVSMKDLDP AFRGAGQKEG LEIWRIENFK PVPIPASSYG KFFMGDSYII LKTTALKNGS
     LRHDIHYWIG KDTSQDESGT AAILTVELDA ALGGRAVQYR EIQGNETDKF LSYFRPCIMP
     QPGGVASGFK HVEVNEQEHE TRLYVCTGNR VVHVKEVPFA RSSLNHDDIF ILDTKSKIFQ
     FNGSNSSIQE RAKALEVVQY IKDTFHEGKC EVAAVEDGRL MADAEAGEFW GFFGGFAPLP
     RRAPVEDNEK YEETVFKLLC FNQGKLEPIN YESLLHELLK TNKCYLLDCG VELFVWMGRT
     TSLQERKSAS EAAEKLLSDD NRTKTHVIKV IEGFETVMFK SKFKEWPQTP DLKLSSEDGR
     GKVAALLKRQ GLNVKGLMKA APAKEEPQAY IDCTGSLQVW RINDKDKILL PSADQSKFYT
     GDCYIFQYMY PGDDKEECLI GSWFGKKSIE EDRVTAISLA SKMVESAKFQ AVQTRLYEGK
     EPIQFFVIFQ SFQVFKGGLS SGYKKFIAEN GIDDDTYLED GLALFRIQGS GPENMQAIQV
     DAAASSLNSS YSYILHDGNT VFTWTGNLTT SLDQEVVERQ LDIIKPNSQS RSQKEGSETD
     QFWSLLGGKS EYPSQKIGRA NESDPHLFSC ILPKGNLKIK EIYHFTQDDL MTEDVFILDC
     HSDIFVWVGQ QVDVKVRLQA LDIGEKFVKL DFLMENLSSD TPIFVIMEGS EPTFFTRFFT
     WDSAKSLMHG NSYQRKLSIV KGGGSPALDK PKRRTPTYSG RSTVQDKSQR SRSMSFSPER
     VRVRGRSPAF TALAANFESA NSRNLSTPPP VVKKLYPKSA TPDSSSAPSK SSATASLTGS
     FDRPKSVKDG SELEKPKQEE DAKEGINTMT SRVESLTINE DVKENEPEDD EGLPVYPYDR
     LITTAADPVT EIDVTRRETY LSSAEFKDKF GMTKEAFSKL PKWKQNRMKI ALQLF
 
 
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