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TGB3_BSMV
ID   TGB3_BSMV               Reviewed;         155 AA.
AC   P04868;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   23-FEB-2022, entry version 59.
DE   RecName: Full=Movement protein TGB3;
DE   AltName: Full=17 kDa protein;
DE   AltName: Full=Beta-C protein;
DE   AltName: Full=Triple gene block 3 protein;
DE            Short=TGBp3;
OS   Barley stripe mosaic virus (BSMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Hordeivirus.
OX   NCBI_TaxID=12327;
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH   NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=ATCC PV43;
RX   PubMed=3754962; DOI=10.1093/nar/14.9.3895;
RA   Gustafson G., Armour S.L.;
RT   "The complete nucleotide sequence of RNA beta from the type strain of
RT   barley stripe mosaic virus.";
RL   Nucleic Acids Res. 14:3895-3909(1986).
RN   [2]
RP   INTERACTION WITH MOVEMENT PROTEIN TGB1, INTERACTION WITH MOVEMENT PROTEIN
RP   TGB2, AND FUNCTION.
RX   PubMed=18353960; DOI=10.1128/jvi.02586-07;
RA   Lim H.S., Bragg J.N., Ganesan U., Lawrence D.M., Yu J., Isogai M.,
RA   Hammond J., Jackson A.O.;
RT   "Triple gene block protein interactions involved in movement of Barley
RT   stripe mosaic virus.";
RL   J. Virol. 82:4991-5006(2008).
RN   [3]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-155, AND FUNCTION.
RX   PubMed=19570874; DOI=10.1128/jvi.00739-09;
RA   Lim H.S., Bragg J.N., Ganesan U., Ruzin S., Schichnes D., Lee M.Y.,
RA   Vaira A.M., Ryu K.H., Hammond J., Jackson A.O.;
RT   "Subcellular localization of the barley stripe mosaic virus triple gene
RT   block proteins.";
RL   J. Virol. 83:9432-9448(2009).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25288925; DOI=10.5423/ppj.oa.09.2012.0144;
RA   Lim H.S., Lee M.Y., Moon J.S., Moon J.K., Yu Y.M., Cho I.S., Bae H.,
RA   deBoer M., Ju H., Hammond J., Jackson A.O.;
RT   "Actin Cytoskeleton and Golgi Involvement in Barley stripe mosaic virus
RT   Movement and Cell Wall Localization of Triple Gene Block Proteins.";
RL   Plant Pathol. J. 29:17-30(2013).
RN   [5]
RP   IDENTIFICATION IN THE TGB1-TGB2-TGB3 COMPLEX.
RX   PubMed=32730331; DOI=10.1371/journal.ppat.1008709;
RA   Jiang Z., Zhang K., Li Z., Li Z., Yang M., Jin X., Cao Q., Wang X., Yue N.,
RA   Li D., Zhang Y.;
RT   "The Barley stripe mosaic virus gammab protein promotes viral cell-to-cell
RT   movement by enhancing ATPase-mediated assembly of ribonucleoprotein
RT   movement complexes.";
RL   PLoS Pathog. 16:e1008709-e1008709(2020).
CC   -!- FUNCTION: Participates in the transport of viral genome to neighboring
CC       plant cells directly through plasmodesmata, without any budding
CC       (PubMed:18353960). TGBp2 and TGBp3 are necessary for intracellular
CC       delivery of TGBp1-containing vRNPs to plasmodesmata (Probable). Can
CC       gate plasmodesmata and increase their size exclusion limit
CC       (PubMed:19570874). Induces host actin cytoskeleton network thickening,
CC       which probably plays a major role in virus cell-to-cell movement
CC       (PubMed:25288925). {ECO:0000269|PubMed:18353960,
CC       ECO:0000269|PubMed:19570874, ECO:0000269|PubMed:25288925,
CC       ECO:0000305|PubMed:19570874}.
CC   -!- SUBUNIT: Interacts with movement proteins TGB1 and TGB2
CC       (PubMed:18353960). TGB1-TGB3-TGB2 complex formation is enhanced by ATP
CC       hydrolysis (PubMed:32730331). {ECO:0000269|PubMed:18353960,
CC       ECO:0000269|PubMed:32730331}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC       {ECO:0000269|PubMed:19570874}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:25288925}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9IV52}. Host cytoplasm, host cytoskeleton
CC       {ECO:0000269|PubMed:25288925}. Note=Probably localizes to
CC       plasmodesmata-associated membrane compartments called peripheral
CC       membrane bodies (PMBs) (PubMed:19570874). Associates with host actin
CC       filaments (PubMed:25288925). {ECO:0000269|PubMed:19570874,
CC       ECO:0000269|PubMed:25288925}.
CC   -!- DOMAIN: The 2nd transmembrane domain is involved in plasmodesmata
CC       targeting. {ECO:0000250|UniProtKB:Q9IV52}.
CC   -!- MISCELLANEOUS: The genome of this virus consists of three linear,
CC       positive, single-stranded RNAs encapsidated in separate virions
CC       designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A,
CC       beta-A and gamma-A) are translated directly from these genomic RNAs and
CC       the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D)
CC       and RNA-gamma (gamma-B) are expressed via three subgenomic messenger
CC       RNAs. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the virgaviridae TGB3 movement protein family.
CC       {ECO:0000305}.
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DR   EMBL; X03854; CAA27487.1; -; Genomic_RNA.
DR   PIR; A04193; WMBV7B.
DR   RefSeq; NP_604489.1; NC_003481.1.
DR   GeneID; 962679; -.
DR   KEGG; vg:962679; -.
DR   Proteomes; UP000001667; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR   InterPro; IPR007617; Viral_beta_CD.
DR   Pfam; PF04530; Viral_Beta_CD; 1.
PE   1: Evidence at protein level;
KW   Host cell junction; Host cytoplasm; Host cytoskeleton;
KW   Host endoplasmic reticulum; Host membrane; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Viral movement protein.
FT   CHAIN           1..155
FT                   /note="Movement protein TGB3"
FT                   /id="PRO_0000222490"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   TOPO_DOM        81..130
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   TOPO_DOM        152..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   REGION          150..155
FT                   /note="Required for attachment to the host plasmodesmata-
FT                   associated membrane compartments"
FT                   /evidence="ECO:0000305|PubMed:19570874"
FT   MOTIF           89..93
FT                   /note="Involved in plasmodesmata targeting and virus cell-
FT                   to-cell movement"
FT                   /evidence="ECO:0000250|UniProtKB:Q9IV52"
FT   MUTAGEN         155
FT                   /note="R->A: Reduced cell-to-cell movement."
FT                   /evidence="ECO:0000269|PubMed:19570874"
SQ   SEQUENCE   155 AA;  17377 MW;  0AA04829728D027B CRC64;
     MAMPHPLECC CPQCLPSSES FPIYGEQEIP CSETQAETTP VEKTVRANVL TDILDDHYYA
     ILASLFIIAL WLLYIYLSSI PTETGPYFYQ DLNSVKIYGI GATNPEVIAA IHHWQKYPFG
     ESPMWGGLIS VLSILLKPLT LVFALSFFLL LSSKR
 
 
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