MVP_PLRVR
ID MVP_PLRVR Reviewed; 156 AA.
AC P17523;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Movement protein P17 {ECO:0000303|PubMed:12437307};
DE Short=MP;
DE AltName: Full=17 kDa protein;
DE AltName: Full=MP17;
GN ORFNames=ORF4;
OS Potato leafroll virus (strain Potato/Canada/Rowhani/1979) (PLrV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Polerovirus.
OX NCBI_TaxID=12047;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732704; DOI=10.1099/0022-1317-70-3-783;
RA Kawchuk L.M., Martin R.R., Rochon D.M., McPherson J.;
RT "Identification and characterization of the potato leafroll virus putative
RT coat protein gene.";
RL J. Gen. Virol. 70:783-788(1989).
RN [2]
RP FUNCTION.
RX PubMed=12437307; DOI=10.1094/mpmi.2002.15.10.1086;
RA Lee L., Palukaitis P., Gray S.M.;
RT "Host-dependent requirement for the Potato leafroll virus 17-kda protein in
RT virus movement.";
RL Mol. Plant Microbe Interact. 15:1086-1094(2002).
CC -!- FUNCTION: Together with movement protein P3a, facilitates long-distance
CC movement of virions in host (Probable). 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 (By similarity). {ECO:0000250|UniProtKB:P10471, ECO:0000305,
CC ECO:0000305|PubMed:12437307}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P10471}.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000250|UniProtKB:P10471}. Host chloroplast envelope
CC {ECO:0000250|UniProtKB:P10471}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:P09511}. Host mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P17524}. Note=Localizes to secondary branched
CC plasmodesmata in source organs. Targeted to plasmodesmata in an
CC actin- and endoplasmic reticulum-Golgi-dependent manner (By
CC similarity). P3a directs P17 to the mitochondrial outer membrane while
CC P17 regulates the localization of the P3a-P17 heterodimer to plastids
CC (By similarity). {ECO:0000250|UniProtKB:P10471,
CC ECO:0000250|UniProtKB:P17524}.
CC -!- DOMAIN: The N-terminus is involved in homodimerization. The C-terminus
CC binds ssRNA. The C-terminus is phosphorylated.
CC {ECO:0000250|UniProtKB:P10471}.
CC -!- PTM: Expressed as a nonphosphorylated 20kDa form and a phosphorylated
CC 22kDa form. Phosphorylated by a host PKC-related kinase (By
CC similarity). Serine phosphorylation is required for plamodesma
CC targeting (By similarity). {ECO:0000250|UniProtKB:P10471}.
CC -!- MISCELLANEOUS: Poleroviruses are transmitted by aphids directly into
CC phloem tissue. The virus replicates most efficiently in phloem
CC companion cells and then moves through plasmodesmata between companion
CC cells or into sieve elements for long distance transport.
CC {ECO:0000250|UniProtKB:P17524}.
CC -!- SIMILARITY: Belongs to the polerovirus movement protein family.
CC {ECO:0000305}.
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DR EMBL; D13753; BAA02901.1; -; Genomic_RNA.
DR PIR; JQ0002; GNVQL2.
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 3: Inferred from homology;
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_0000222423"
FT REGION 38..54
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P10471"
FT REGION 55..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..156
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P10471"
FT REGION 106..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
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:0000250|UniProtKB:P10471"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10471"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10471"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10471"
SQ SEQUENCE 156 AA; 17381 MW; DA0B4A12B1E66B02 CRC64;
MSMVVYNNQE GEEGNPFAGA LTEFSQWLWS RPLGNPGAED AEEEAIAAQE ELEFPEDEAQ
ARHSCLQRTT SWATPKEVSP SGRVYQTVRH SRMEYSRPTM SIRSQASYFS SSARPLPPPP
VPSLMSWTPI AKYHPSSPTS TSSKLRRAAP KLIKRG
