ID   MVP_PLRVW               Reviewed;         156 AA.
AC   P11625;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Movement protein P17 {ECO:0000250|UniProtKB:P17523};
DE            Short=MP;
DE   AltName: Full=17 kDa protein;
DE   AltName: Full=MP17;
GN   ORFNames=ORF4;
OS   Potato leafroll virus (strain Potato/Netherlands/Wageningen/1989) (PLrV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Polerovirus.
OX   NCBI_TaxID=12048;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2466700; DOI=10.1016/0014-5793(89)80190-5;
RA   van der Wilk F., Huisman M.J., Cornelissen B.J.C., Huttinga H.,
RA   Goldbach R.W.;
RT   "Nucleotide sequence and organization of potato leafroll virus genomic
RT   RNA.";
RL   FEBS Lett. 245:51-56(1989).
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 (By similarity). {ECO:0000250|UniProtKB:P10471,
CC       ECO:0000250|UniProtKB:P17524, ECO:0000305}.
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; Y07496; CAA68798.1; -; Genomic_RNA.
DR   PIR; S03550; GNVQWA.
DR   Proteomes; UP000000474; Genome.
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_0000222425"
FT   REGION          38..54
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P10471"
FT   REGION          55..81
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          133..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..81
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;  17344 MW;  8C8ACC9D74E67D73 CRC64;
     MSMAVYNNQE GEEGNPFAGA LTEFSQWLWS RPLGNPGAED AEEEAIAAQE ELEFPEDEAQ
     ARHSCLQRTT SWATPKEVSP SGRVYQTVRH SRMEYSRPTM SIRSQASYFS SSARPLPPPP
     VPSLMSWTPI AKYHPSSPTS TSSKFLRAAP KLIKRG