MVP2_BYVU
ID MVP2_BYVU Reviewed; 54 AA.
AC Q08542;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=Movement protein p6;
DE AltName: Full=6 kDa protein;
DE Short=p6;
GN ORFNames=ORF2;
OS Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Closteroviridae; Closterovirus.
OX NCBI_TaxID=478555;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1990061; DOI=10.1099/0022-1317-72-1-15;
RA Agranovsky A.A., Boyko V.P., Karasev A.V., Lunina N.A., Koonin E.V.,
RA Dolja V.V.;
RT "Nucleotide sequence of the 3'-terminal half of beet yellows closterovirus
RT RNA genome: unique arrangement of eight virus genes.";
RL J. Gen. Virol. 72:15-23(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8259666; DOI=10.1006/viro.1994.1034;
RA Agranovsky A.A., Koonin E.V., Boyko V.P., Maiss E., Froetschl R.,
RA Lunina N.A., Atabekov J.G.;
RT "Beet yellows closterovirus: complete genome structure and identification
RT of a leader papain-like thiol protease.";
RL Virology 198:311-324(1994).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DISULFIDE BOND, AND
RP MUTAGENESIS OF ASP-2; CYS-3; ARG-6; GLY-14; CYS-18; CYS-23; TRP-29; LYS-33;
RP ARG-38; GLU-45; ARG-47; HIS-50 AND VAL-54.
RX PubMed=15016890; DOI=10.1128/jvi.78.7.3704-3709.2004;
RA Peremyslov V.V., Pan Y.-W., Dolja V.V.;
RT "Movement protein of a closterovirus is a type III integral transmembrane
RT protein localized to the endoplasmic reticulum.";
RL J. Virol. 78:3704-3709(2004).
CC -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC through plasmosdesmata, without any budding. The movement protein
CC allows efficient cell to cell propagation, by bypassing the host cell
CC wall barrier. Two movement proteins, p6, Hsp70h and three structural
CC proteins, CP, CPm, and P64 are essential for cell-cell movement. Also
CC plays a role in virion formation. Together with CPm and p64,
CC encapsidates the 5'-terminal portion of the viral genome (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15016890}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15016890}.
CC -!- SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53462; CAA37550.1; -; Genomic_RNA.
DR EMBL; X73476; CAA51864.1; -; Genomic_RNA.
DR PIR; S28711; S28711.
DR RefSeq; NP_041871.1; NC_001598.1.
DR SMR; Q08542; -.
DR TCDB; 9.B.308.3.2; the lettuce infectious yellows virus p5 (liyv-p5) family.
DR GeneID; 1724785; -.
DR KEGG; vg:1724785; -.
DR Proteomes; UP000000359; Genome.
DR GO; GO:0044169; C:host cell rough endoplasmic reticulum membrane; 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; IPR009591; Beet_yellows_virus_p6.
DR Pfam; PF06716; MP_p6; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Host endoplasmic reticulum; Host membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Viral movement protein.
FT CHAIN 1..54
FT /note="Movement protein p6"
FT /id="PRO_0000312565"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:15016890"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 3
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 2
FT /note="D->A: Strong reduction of virus ability to move from
FT cell to cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 3
FT /note="C->A: Complete loss of homodimerization. Complete
FT loss of virus ability to move from cell to cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 6
FT /note="R->A: Strong reduction of virus ability to move from
FT cell to cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 14
FT /note="G->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 18
FT /note="C->A: No effect on homodimerization. Reduces virus
FT ability to move from cell to cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 23
FT /note="C->A: No effect on homodimerization. Reduces virus
FT ability to move from cell to cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 29
FT /note="W->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 33
FT /note="K->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 38
FT /note="R->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 45
FT /note="E->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 47
FT /note="R->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 50
FT /note="H->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
FT MUTAGEN 54
FT /note="V->A: Reduces virus ability to move from cell to
FT cell."
FT /evidence="ECO:0000269|PubMed:15016890"
SQ SEQUENCE 54 AA; 6389 MW; 9B579142335C846D CRC64;
MDCVLRSYLL LAFGFLICLF LFCLVVFIWF VYKQILFRTT AQSNEARHNH STVV
