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TGB3_PMTVS
ID   TGB3_PMTVS              Reviewed;         190 AA.
AC   Q9IV52;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   23-FEB-2022, entry version 38.
DE   RecName: Full=Movement protein TGB3;
DE   AltName: Full=P21;
DE   AltName: Full=Triple gene block 3 protein;
DE            Short=TGBp3;
OS   Potato mop-top virus (isolate Potato/Sweden/Sw) (PMTV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Pomovirus.
OX   NCBI_TaxID=652839;
OH   NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12655103; DOI=10.1099/vir.0.18813-0;
RA   Savenkov E.I., Germundsson A., Zamyatnin A.A. Jr., Sandgren M.,
RA   Valkonen J.P.;
RT   "Potato mop-top virus: the coat protein-encoding RNA and the gene for
RT   cysteine-rich protein are dispensable for systemic virus movement in
RT   Nicotiana benthamiana.";
RL   J. Gen. Virol. 84:1001-1005(2003).
RN   [2]
RP   INTERACTION WITH TGB2, AND SUBCELLULAR LOCATION.
RX   PubMed=12093178; DOI=10.1006/viro.2002.1435;
RA   Cowan G.H., Lioliopoulou F., Ziegler A., Torrance L.;
RT   "Subcellular localisation, protein interactions, and RNA binding of Potato
RT   mop-top virus triple gene block proteins.";
RL   Virology 298:106-115(2002).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGB2, AND MUTAGENESIS OF
RP   TYR-89.
RX   PubMed=15608333; DOI=10.1105/tpc.104.027821;
RA   Haupt S., Cowan G.H., Ziegler A., Roberts A.G., Oparka K.J., Torrance L.;
RT   "Two plant-viral movement proteins traffic in the endocytic recycling
RT   pathway.";
RL   Plant Cell 17:164-181(2005).
RN   [4]
RP   FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-89.
RX   PubMed=20350737; DOI=10.1016/j.virol.2010.03.008;
RA   Tilsner J., Cowan G.H., Roberts A.G., Chapman S.N., Ziegler A.,
RA   Savenkov E., Torrance L.;
RT   "Plasmodesmal targeting and intercellular movement of potato mop-top
RT   pomovirus is mediated by a membrane anchored tyrosine-based motif on the
RT   lumenal side of the endoplasmic reticulum and the C-terminal transmembrane
RT   domain in the TGB3 movement protein.";
RL   Virology 402:41-51(2010).
RN   [5]
RP   PHOSPHORYLATION AT TYR-89 AND TYR-120, AND MUTAGENESIS OF 87-TYR--TYR-89
RP   AND TYR-120.
RX   PubMed=23365450; DOI=10.1128/jvi.03388-12;
RA   Samuilova O., Santala J., Valkonen J.P.;
RT   "Tyrosine phosphorylation of the triple gene block protein 3 regulates
RT   cell-to-cell movement and protein interactions of Potato mop-top virus.";
RL   J. Virol. 87:4313-4321(2013).
CC   -!- FUNCTION: Participates in the transport of viral genome to neighboring
CC       plant cells directly through plasmodesmata, without any budding (By
CC       similarity). TGBp2 and TGBp3 are necessary for intracellular delivery
CC       of TGBp1-containing vRNPs to plasmodesmata (By similarity). Can gate
CC       plasmodesmata and increase their size exclusion limit
CC       (PubMed:15608333). Induces host actin cytoskeleton network thickening,
CC       which probably plays a major role in virus cell-to-cell movement (By
CC       similarity). {ECO:0000250|UniProtKB:P04868,
CC       ECO:0000269|PubMed:15608333}.
CC   -!- SUBUNIT: Interacts with movement protein TGB2 (PubMed:12093178,
CC       PubMed:15608333). TGB1-TGB3-TGB2 complex formation is enhanced by ATP
CC       hydrolysis (By similarity). {ECO:0000250|UniProtKB:P04868,
CC       ECO:0000269|PubMed:12093178, ECO:0000269|PubMed:15608333}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC       {ECO:0000269|PubMed:12093178, ECO:0000269|PubMed:20350737}. Host
CC       endoplasmic reticulum membrane {ECO:0000269|PubMed:15608333,
CC       ECO:0000269|PubMed:20350737}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:20350737}. Host cytoplasm, host cytoskeleton
CC       {ECO:0000250|UniProtKB:P04868}. Note=Probably localizes to
CC       plasmodesmata-associated membrane compartments called peripheral
CC       membrane bodies (PMBs). Associates with host actin filaments.
CC       {ECO:0000250|UniProtKB:P04868}.
CC   -!- DOMAIN: The 2nd transmembrane domain is involved in plasmodesmata
CC       targeting. {ECO:0000269|PubMed:20350737}.
CC   -!- SIMILARITY: Belongs to the virgaviridae TGB3 movement protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ277556; CAB91103.1; -; Genomic_RNA.
DR   RefSeq; NP_620440.1; NC_003725.1.
DR   SMR; Q9IV52; -.
DR   TCDB; 9.B.308.6.1; the lettuce infectious yellows virus p5 (liyv-p5) family.
DR   iPTMnet; Q9IV52; -.
DR   GeneID; 991176; -.
DR   KEGG; vg:991176; -.
DR   Proteomes; UP000006715; 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..190
FT                   /note="Movement protein TGB3"
FT                   /id="PRO_0000410611"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   TOPO_DOM        74..166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   TOPO_DOM        188..190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   MOTIF           89..93
FT                   /note="Involved in plasmodesmata targeting and virus cell-
FT                   to-cell movement"
FT                   /evidence="ECO:0000269|PubMed:20350737"
FT   MOD_RES         89
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:23365450"
FT   MOD_RES         120
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:23365450"
FT   MUTAGEN         87..89
FT                   /note="YYY->AAA: Inhibition of cell-to-cell movement and
FT                   enhanced interaction between TGBp3 and TGBp2."
FT                   /evidence="ECO:0000269|PubMed:23365450"
FT   MUTAGEN         89
FT                   /note="Y->G: Complete loss of plamodesmal localization. 50%
FT                   loss of plasmodesmata gating efficiency."
FT                   /evidence="ECO:0000269|PubMed:15608333,
FT                   ECO:0000269|PubMed:20350737"
FT   MUTAGEN         120
FT                   /note="Y->A: Complete loss of infectivity but no effect on
FT                   the interaction between TGBp3 and TGBp2."
FT                   /evidence="ECO:0000269|PubMed:23365450"
SQ   SEQUENCE   190 AA;  21015 MW;  F633E747BFD694E1 CRC64;
     MDPPVILHSP NCSCQFCSSE LPSTHTCGSQ DRTVPLHVEA TAAGHMEAKN FSLQYVLLVA
     FVSVLLGFSF CVYLKSMSND EASDMTYYYQ DLNSVEIKLG KNPLDPEVIK AIHSFQEFPY
     GNIPSIRREA EFDVQNDESS AVVLSGSNNN RRQVASTPCE NNVLLKLWKD DLSFTIIAVT
     VLVGAMLARC
 
 
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