MVP_BYDVP
ID MVP_BYDVP Reviewed; 153 AA.
AC P09513;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Movement protein;
DE Short=MP;
DE AltName: Full=17 kDa protein;
GN ORFNames=ORF4;
OS Barley yellow dwarf virus (isolate PAV) (BYDV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Luteovirus.
OX NCBI_TaxID=2169986;
OH NCBI_TaxID=146531; Avena byzantina.
OH NCBI_TaxID=4498; Avena sativa (Oat).
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=4521; Lolium multiflorum (Italian ryegrass) (Lolium perenne subsp. multiflorum).
OH NCBI_TaxID=4522; Lolium perenne (Perennial ryegrass).
OH NCBI_TaxID=4530; Oryza sativa (Rice).
OH NCBI_TaxID=4550; Secale cereale (Rye).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3399386; DOI=10.1093/nar/16.13.6097;
RA Miller W.A., Waterhouse P.M., Gerlach W.L.;
RT "Sequence and organization of barley yellow dwarf virus genomic RNA.";
RL Nucleic Acids Res. 16:6097-6111(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3388774; DOI=10.1016/0042-6822(88)90690-3;
RA Miller W.A., Waterhouse P.M., Kortt A.A., Gerlach W.L.;
RT "Sequence and identification of the barley yellow dwarf virus coat protein
RT gene.";
RL Virology 165:306-309(1988).
RN [3]
RP FUNCTION.
RX PubMed=8623554; DOI=10.1006/viro.1996.0222;
RA Chay C.A., Gunasinge U.B., Dinesh-Kumar S.P., Miller W.A., Gray S.M.;
RT "Aphid transmission and systemic plant infection determinants of barley
RT yellow dwarf luteovirus-PAV are contained in the coat protein readthrough
RT domain and 17-kDa protein, respectively.";
RL Virology 219:57-65(1996).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15971210; DOI=10.1002/bip.20334;
RA Liu K., Xia Z., Zhang Y., Wen Y., Wang D., Brandenburg K., Harris F.,
RA Phoenix D.A.;
RT "Interaction between the movement protein of barley yellow dwarf virus and
RT the cell nuclear envelope: role of a putative amphiphilic alpha-helix at
RT the N-terminus of the movement protein.";
RL Biopolymers 79:86-96(2005).
RN [5]
RP DOMAIN.
RX PubMed=17897753; DOI=10.1016/j.peptides.2007.08.015;
RA Dennison S.R., Harris F., Brandenburg K., Phoenix D.A.;
RT "Characterization of the N-terminal segment used by the barley yellow dwarf
RT virus movement protein to promote interaction with the nuclear membrane of
RT host plant cells.";
RL Peptides 28:2091-2097(2007).
RN [6]
RP FUNCTION.
RX PubMed=28994713; DOI=10.3390/v9100294;
RA Fusaro A.F., Barton D.A., Nakasugi K., Jackson C., Kalischuk M.L.,
RA Kawchuk L.M., Vaslin M.F.S., Correa R.L., Waterhouse P.M.;
RT "The Luteovirus P4 Movement Protein Is a Suppressor of Systemic RNA
RT Silencing.";
RL Viruses 9:0-0(2017).
CC -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC through plasmosdesmata, without any budding (PubMed:8623554). The
CC movement protein allows efficient cell to cell propagation, by
CC bypassing the host cell wall barrier (PubMed:8623554). Acts as a
CC suppressor of RNA-mediated gene silencing, also known as post-
CC transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs (PubMed:28994713).
CC {ECO:0000269|PubMed:28994713, ECO:0000269|PubMed:8623554}.
CC -!- SUBCELLULAR LOCATION: Host nucleus envelope
CC {ECO:0000269|PubMed:15971210}.
CC -!- DOMAIN: The N-terminus forms a amphiphilic alpha-helix, which
CC partitions into the nuclear membrane. {ECO:0000269|PubMed:17897753}.
CC -!- SIMILARITY: Belongs to the luteoviruses movement protein family.
CC {ECO:0000305}.
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DR EMBL; M21347; AAA87367.1; -; Genomic_RNA.
DR EMBL; X07653; CAA30494.1; -; Genomic_RNA.
DR Proteomes; UP000006722; Genome.
DR GO; GO:0044199; C:host cell nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR InterPro; IPR001964; Luteo_VPG.
DR Pfam; PF01659; Luteo_Vpg; 1.
DR PRINTS; PR00912; LVIRUSORF5.
PE 3: Inferred from homology;
KW Host nucleus; Reference proteome; Suppressor of RNA silencing; Transport;
KW Viral movement protein.
FT CHAIN 1..153
FT /note="Movement protein"
FT /id="PRO_0000222420"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 153 AA; 17147 MW; 640A9FC646A8A25E CRC64;
MAQEGGAVEQ FGQWLWSNPI EQDPDDEMVD AREEEGQILY LDQQAGLRYS YSQLTTLKPT
PPGQSNSAPV YRNAQRFQTE YSSPTIVTRS QVSELSLSHT RPPIRQALSL LSSTPRASNQ
PWVATLIPSP SARPPPRPSG QRQLMGRNSR NQR
