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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
 
 
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