MP_RCNMV
ID MP_RCNMV Reviewed; 317 AA.
AC P10838;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Movement protein;
DE Short=MP;
GN ORFNames=ORF3;
OS Red clover necrotic mosaic virus (RCNMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Regressovirinae; Dianthovirus.
OX NCBI_TaxID=12267;
OH NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH NCBI_TaxID=47083; Melilotus officinalis (Yellow sweet clover) (Trifolium officinale).
OH NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Australian;
RX PubMed=3047682; DOI=10.1093/nar/16.17.8587;
RA Lommel S.A., Weston Fina M., Xiong Z., Lomonossoff G.P.;
RT "The nucleotide sequence and gene organization of red clover necrotic
RT mosaic virus RNA-2.";
RL Nucleic Acids Res. 16:8587-8602(1988).
RN [2]
RP FUNCTION, AND SSRNA AND SSDNA-BINDING.
RX PubMed=1538188; DOI=10.1099/0022-1317-73-2-223;
RA Osman T.A., Hayes R.J., Buck K.W.;
RT "Cooperative binding of the red clover necrotic mosaic virus movement
RT protein to single-stranded nucleic acids.";
RL J. Gen. Virol. 73:223-227(1992).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15708588; DOI=10.1016/j.virol.2004.12.019;
RA Tremblay D., Vaewhongs A.A., Turner K.A., Sit T.L., Lommel S.A.;
RT "Cell wall localization of Red clover necrotic mosaic virus movement
RT protein is required for cell-to-cell movement.";
RL Virology 333:10-21(2005).
RN [4]
RP FUNCTION.
RX PubMed=18838152; DOI=10.1016/j.virol.2008.09.004;
RA Powers J.G., Sit T.L., Heinsohn C., George C.G., Kim K.-H., Lommel S.A.;
RT "The Red clover necrotic mosaic virus RNA-2 encoded movement protein is a
RT second suppressor of RNA silencing.";
RL Virology 381:277-286(2008).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19819513; DOI=10.1016/j.virol.2009.09.022;
RA Kaido M., Tsuno Y., Mise K., Okuno T.;
RT "Endoplasmic reticulum targeting of the Red clover necrotic mosaic virus
RT movement protein is associated with the replication of viral RNA1 but not
RT that of RNA2.";
RL Virology 395:232-242(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=21377183; DOI=10.1016/j.virol.2011.02.008;
RA Kaido M., Funatsu N., Tsuno Y., Mise K., Okuno T.;
RT "Viral cell-to-cell movement requires formation of cortical punctate
RT structures containing Red clover necrotic mosaic virus movement protein.";
RL Virology 413:205-215(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST NBGAPDH-A.
RX PubMed=25411849; DOI=10.1371/journal.ppat.1004505;
RA Kaido M., Abe K., Mine A., Hyodo K., Taniguchi T., Taniguchi H., Mise K.,
RA Okuno T.;
RT "GAPDH--a recruits a plant virus movement protein to cortical virus
RT replication complexes to facilitate viral cell-to-cell movement.";
RL PLoS Pathog. 10:E1004505-E1004505(2014).
CC -!- FUNCTION: Plays an essential role in cell-to-cell movement and long-
CC distance transport of the viral genome. Mechanistically, movement
CC protein is recruited by viral replicase complexes formed on RNA1 to
CC punctate structures on the host cortical endoplasmic reticulum. In
CC turn, interacts with the viral genome and mediates virion movement from
CC cell to cell. Acts also as a suppressor of RNA-mediated gene silencing,
CC also known as post-transcriptional gene silencing (PTGS), a mechanism
CC of plant viral defense that limits the accumulation of viral RNAs.
CC {ECO:0000269|PubMed:1538188, ECO:0000269|PubMed:15708588,
CC ECO:0000269|PubMed:18838152, ECO:0000269|PubMed:19819513,
CC ECO:0000269|PubMed:21377183, ECO:0000269|PubMed:25411849}.
CC -!- SUBUNIT: Interacts with host glyceraldehyde 3-phosphate dehydrogenase-
CC A/NbGAPDH-A; this interaction plays a positive role in cell-to-cell
CC movement of the virus. {ECO:0000269|PubMed:25411849}.
CC -!- SUBCELLULAR LOCATION: Host cell wall {ECO:0000269|PubMed:15708588}.
CC Host endoplasmic reticulum membrane {ECO:0000269|PubMed:19819513,
CC ECO:0000269|PubMed:21377183}. Note=Targeting of virus movement protein
CC to the host endoplasmic reticulum membrane is associated with the
CC replication of viral RNA-1 but not that of RNA-2.
CC {ECO:0000269|PubMed:19819513}.
CC -!- DOMAIN: The C-terminal domain is essential for localization to cortical
CC punctate structures at an early stage of infection.
CC {ECO:0000269|PubMed:21377183}.
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DR EMBL; X08021; CAA30822.1; -; Genomic_RNA.
DR PIR; S01412; S01412.
DR RefSeq; NP_620546.1; NC_003775.1.
DR GeneID; 956633; -.
DR KEGG; vg:956633; -.
DR Proteomes; UP000008651; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044158; C:host cell wall; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR InterPro; IPR000603; MPV.
DR Pfam; PF00803; 3A; 1.
PE 1: Evidence at protein level;
KW Host endoplasmic reticulum; Host membrane; Membrane; Reference proteome;
KW Suppressor of RNA silencing; Transport; Viral movement protein.
FT CHAIN 1..317
FT /note="Movement protein"
FT /id="PRO_0000222898"
FT REGION 223..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34647 MW; D35D428028740AA1 CRC64;
MAVHVENLSD LAKTNDGVAV SLNRYTDWKC RSGVSEAPLI PASMMSKITD YAKTTAKGNS
VALNYTHVVL SLAPTIGVAI PGHVTVELIN PNVEGPFQVM SGQTLSWSPG AGKPCLMIFS
VHHQLNSDHE PFRVRITNTG IPTKKSYARC HAYWGFDVGT RHRYYKSEPA RLIELEVGYQ
RTLLSSIKAV EAYVQFTFDT SRMEKNPQLC TKSNVNIIPP KAETGSIRGI APPLSVVPNQ
GRESKVLKQK GGTGSKTTKL PSLEPSSGSS SGLSMSRRSH RNVLNSSIPI KRNQDGNWLG
DHLSDKGRVT DPNPERL