MVP_PLRV
ID MVP_PLRV Reviewed; 156 AA.
AC P10471;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Movement protein P17;
DE Short=MP;
DE AltName: Full=17 kDa protein;
DE AltName: Full=MP17;
GN ORFNames=ORF4;
OS Potato leafroll virus (PLrV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Polerovirus.
OX NCBI_TaxID=12045;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2922295; DOI=10.1093/nar/17.4.1768;
RA Prill B., Maiss E., Timpe V., Casper R.;
RT "Nucleotide sequence of the potato leafroll virus coat protein gene.";
RL Nucleic Acids Res. 17:1768-1768(1989).
RN [2]
RP RNA-BINDING, AND DOMAIN.
RX PubMed=1908517; DOI=10.1099/0022-1317-72-8-2035;
RA Tacke E., Pruefer D., Schmitz J., Rohde W.;
RT "The potato leafroll luteovirus 17K protein is a single-stranded nucleic
RT acid-binding protein.";
RL J. Gen. Virol. 72:2035-2038(1991).
RN [3]
RP PHOSPHORYLATION, DOMAIN, AND SUBUNIT.
RX PubMed=8212563; DOI=10.1006/viro.1993.1588;
RA Tacke E., Schmitz J., Pruefer D., Rohde W.;
RT "Mutational analysis of the nucleic acid-binding 17 kDa phosphoprotein of
RT potato leafroll luteovirus identifies an amphipathic alpha-helix as the
RT domain for protein/protein interactions.";
RL Virology 197:274-282(1993).
RN [4]
RP PHOSPHORYLATION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=9001398; DOI=10.1016/s0014-5793(96)01380-4;
RA Sokolova M., Pruefer D., Tacke E., Rohde W.;
RT "The potato leafroll virus 17K movement protein is phosphorylated by a
RT membrane-associated protein kinase from potato with biochemical features of
RT protein kinase C.";
RL FEBS Lett. 400:201-205(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17631001; DOI=10.1111/j.1600-0854.2007.00608.x;
RA Vogel F., Hofius D., Sonnewald U.;
RT "Intracellular trafficking of Potato leafroll virus movement protein in
RT transgenic Arabidopsis.";
RL Traffic 8:1205-1214(2007).
RN [6]
RP PHOSPHORYLATION AT SER-71; SER-79; SER-137 AND SER-140, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22645527; DOI=10.3389/fpls.2011.00018;
RA Link K., Vogel F., Sonnewald U.;
RT "PD Trafficking of Potato Leaf Roll Virus Movement Protein in Arabidopsis
RT Depends on Site-specific Protein Phosphorylation.";
RL Front. Plant Sci. 2:18-18(2011).
CC -!- FUNCTION: Together with movement protein P3a, facilitates long-distance
CC movement of virions in host (By similarity). Transports viral genome to
CC neighboring plant cells directly through plasmosdesmata, without any
CC budding (Probable). The movement protein allows efficient cell to cell
CC propagation, by bypassing the host cell wall barrier (Probable). Binds
CC ssRNA (PubMed:1908517). {ECO:0000250|UniProtKB:P17524,
CC ECO:0000269|PubMed:1908517, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8212563}.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:17631001, ECO:0000269|PubMed:22645527}. Host
CC chloroplast envelope {ECO:0000269|PubMed:22645527}. Host Golgi
CC apparatus {ECO:0000250|UniProtKB:P09511}. Host mitochondrion outer
CC membrane {ECO:0000250|UniProtKB:P17524}. Note=Localizes to secondary
CC branched plasmodesmata in source organs. Targeted to plasmodesmata in
CC an actin- and endoplasmic reticulum-Golgi-dependent manner
CC (PubMed:17631001). P3a directs P17 to the mitochondrial outer membrane
CC while P17 regulates the localization of the P3a-P17 heterodimer to
CC plastids (By similarity). {ECO:0000250|UniProtKB:P17524,
CC ECO:0000269|PubMed:17631001}.
CC -!- DOMAIN: The N-terminus is involved in homodimerization
CC (PubMed:8212563). The C-terminus binds ssRNA (PubMed:1908517). The C-
CC terminus is phosphorylated (PubMed:9001398, PubMed:22645527).
CC {ECO:0000269|PubMed:1908517, ECO:0000269|PubMed:22645527,
CC ECO:0000269|PubMed:8212563, ECO:0000269|PubMed:9001398}.
CC -!- PTM: Expressed as a nonphosphorylated 20kDa form and a phosphorylated
CC 22kDa form (PubMed:8212563) (Probable). Phosphorylated by a host PKC-
CC related kinase (PubMed:9001398). Serine phosphorylation is required for
CC plamodesma targeting (PubMed:22645527). {ECO:0000269|PubMed:22645527,
CC ECO:0000269|PubMed:8212563, ECO:0000269|PubMed:9001398,
CC ECO:0000305|PubMed:22645527}.
CC -!- SIMILARITY: Belongs to the polerovirus movement protein family.
CC {ECO:0000305}.
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DR EMBL; X13906; CAA32107.1; -; Genomic_RNA.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044219; C:host cell plasmodesma; 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; IPR001964; Luteo_VPG.
DR Pfam; PF01659; Luteo_Vpg; 1.
DR PRINTS; PR00912; LVIRUSORF5.
PE 1: Evidence at protein level;
KW Host cell junction; Host Golgi apparatus; Host membrane;
KW Host mitochondrion; Host mitochondrion outer membrane; Membrane;
KW Phosphoprotein; Transport; Viral movement protein.
FT CHAIN 1..156
FT /note="Movement protein P17"
FT /id="PRO_0000222422"
FT REGION 38..54
FT /note="Homodimerization"
FT /evidence="ECO:0000303|PubMed:22645527"
FT REGION 57..156
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:1908517"
FT REGION 106..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22645527"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22645527"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22645527"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22645527"
SQ SEQUENCE 156 AA; 17285 MW; 783C6F5274333074 CRC64;
MSMVVYNNQG GEEGNPFAGA LTEFSQWLWS RPLGNPGAED VEEEAIAAQE ELEFPEDEAQ
ARHSCLQRTT SWATPKEVSP SGRVYQTVRL SRMEYSRPTM SIRSQASYFS SSARPLPPPP
APSLMSWTPI AKYHPSSPTS TSSKLRRAAP KLIKRG
