MCAPS_PLRV1
ID MCAPS_PLRV1 Reviewed; 716 AA.
AC P17525; Q84813; Q84829;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Readthrough protein P3-RTD;
DE AltName: Full=P3-P5 readthrough protein;
DE AltName: Full=P74;
DE AltName: Full=Readthrough protein;
DE Short=RT protein;
DE Contains:
DE RecName: Full=Minor capsid readthrough protein {ECO:0000250|UniProtKB:P09514};
DE Short=Minor capsid RT protein {ECO:0000250|UniProtKB:P09514};
DE AltName: Full=54 kDa protein;
DE Contains:
DE RecName: Full=Cleaved product {ECO:0000305};
GN ORFNames=ORF3/ORF5;
OS Potato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Polerovirus.
OX NCBI_TaxID=12046;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732710; DOI=10.1099/0022-1317-70-5-1037;
RA Mayo M.A., Robinson D.J., Jolly C.A., Hyman L.;
RT "Nucleotide sequence of potato leafroll luteovirus RNA.";
RL J. Gen. Virol. 70:1037-1051(1989).
RN [2]
RP SUBCELLULAR LOCATION (MINOR CAPSID READTHROUGH PROTEIN), READTHROUGH
RP (ISOFORM READTHROUGH PROTEIN P3-RTD), AND PROTEOLYTIC CLEAVAGE (ISOFORM
RP READTHROUGH PROTEIN P3-RTD).
RX PubMed=2230732; DOI=10.1099/0022-1317-71-10-2251;
RA Bahner I., Lamb J., Mayo M.A., Hay R.T.;
RT "Expression of the genome of potato leafroll virus: readthrough of the coat
RT protein termination codon in vivo.";
RL J. Gen. Virol. 71:2251-2256(1990).
RN [3]
RP PROTEOLYTIC CLEAVAGE (ISOFORM READTHROUGH PROTEIN P3-RTD), AND SUBCELLULAR
RP LOCATION (P7).
RX PubMed=7513925; DOI=10.1006/viro.1994.1283;
RA Jolly C.A., Mayo M.A.;
RT "Changes in the amino acid sequence of the coat protein readthrough domain
RT of potato leafroll luteovirus affect the formation of an epitope and aphid
RT transmission.";
RL Virology 201:182-185(1994).
RN [4]
RP FUNCTION (MINOR CAPSID READTHROUGH PROTEIN).
RX PubMed=18632976; DOI=10.1099/vir.0.83625-0;
RA Peter K.A., Liang D., Palukaitis P., Gray S.M.;
RT "Small deletions in the potato leafroll virus readthrough protein affect
RT particle morphology, aphid transmission, virus movement and accumulation.";
RL J. Gen. Virol. 89:2037-2045(2008).
RN [5]
RP FUNCTION (MINOR CAPSID READTHROUGH PROTEIN).
RX PubMed=19297484; DOI=10.1128/jvi.02312-08;
RA Peter K.A., Gildow F., Palukaitis P., Gray S.M.;
RT "The C terminus of the polerovirus p5 readthrough domain limits virus
RT infection to the phloem.";
RL J. Virol. 83:5419-5429(2009).
RN [6]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=23433865; DOI=10.1016/j.virol.2012.12.012;
RA Hwang Y.T., Kalischuk M., Fusaro A.F., Waterhouse P.M., Kawchuk L.;
RT "Small RNA sequencing of Potato leafroll virus-infected plants reveals an
RT additional subgenomic RNA encoding a sequence-specific RNA-binding
RT protein.";
RL Virology 438:61-69(2013).
RN [7]
RP READTHROUGH (ISOFORM READTHROUGH PROTEIN P3-RTD).
RX PubMed=29514911; DOI=10.1128/jvi.01544-17;
RA Xu Y., Ju H.J., DeBlasio S., Carino E.J., Johnson R., MacCoss M.J.,
RA Heck M., Miller W.A., Gray S.M.;
RT "A Stem-Loop Structure in Potato Leafroll Virus Open Reading Frame 5 (ORF5)
RT Is Essential for Readthrough Translation of the Coat Protein ORF Stop Codon
RT 700 Bases Upstream.";
RL J. Virol. 92:0-0(2018).
RN [8]
RP SUBCELLULAR LOCATION (MINOR CAPSID READTHROUGH PROTEIN).
RX PubMed=30440046; DOI=10.1371/journal.ppat.1007451;
RA Xu Y., Da Silva W.L., Qian Y., Gray S.M.;
RT "An aromatic amino acid and associated helix in the C-terminus of the
RT potato leafroll virus minor capsid protein regulate systemic infection and
RT symptom expression.";
RL PLoS Pathog. 14:e1007451-e1007451(2018).
RN [9]
RP FUNCTION (ISOFORM P7).
RX PubMed=31758809; DOI=10.1111/pce.13684;
RA Patton M.F., Bak A., Sayre J.M., Heck M.L., Casteel C.L.;
RT "A polerovirus, Potato leafroll virus, alters plant-vector interactions
RT using three viral proteins.";
RL Plant Cell Environ. 43:387-399(2020).
CC -!- FUNCTION: [Minor capsid readthrough protein]: Minor component of the
CC viral capsid involved in aphid transmission and virus accumulation in
CC the host (Probable). Required for the virus to move through the aphid
CC (By similarity). The RTD domain of the protein is exposed on the
CC surface of the particle and determines the vector specificity and
CC intestinal tropism in the aphid (By similarity). This domain might also
CC determine the limitation of the virus to the host phloem
CC (PubMed:19297484). {ECO:0000250|UniProtKB:P09514,
CC ECO:0000250|UniProtKB:P09516, ECO:0000269|PubMed:19297484,
CC ECO:0000305|PubMed:18632976}.
CC -!- FUNCTION: [Isoform P7]: Participates, together with the proteins P0 and
CC P1, in the inhibition of the induction of aphid-induced host
CC phytohormones (PubMed:31758809). This could play a role in the
CC attraction to the infected plants by aphids (PubMed:31758809).
CC {ECO:0000269|PubMed:31758809}.
CC -!- SUBCELLULAR LOCATION: [Minor capsid readthrough protein]: Virion
CC {ECO:0000305|PubMed:2230732}. Host cell junction, host plasmodesma
CC {ECO:0000305|PubMed:30440046}. Host periplasm
CC {ECO:0000305|PubMed:30440046}.
CC -!- SUBCELLULAR LOCATION: [Cleaved product]: Virion
CC {ECO:0000305|PubMed:7513925}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Comment=P7 is the translated product of subgenomic RNA sgRNA3.
CC {ECO:0000269|PubMed:23433865};
CC Name=Readthrough protein P3-RTD;
CC IsoId=P17525-1; Sequence=Displayed;
CC Name=P7; Synonyms=ORF7 protein;
CC IsoId=P17525-2; Sequence=VSP_038673;
CC -!- DOMAIN: [Isoform Readthrough protein P3-RTD]: The N-terminus is highly
CC basic like those of many plant virus capsid proteins. It has been
CC suggested that these regions may be involved in protein-RNA interaction
CC (Probable). The RTD N-terminus is responsible for aphid transmission
CC and aphid endosymbiont interaction (By similarity). The readthrough
CC domain is required for transport of virus through membranes of the
CC aphid salivary glands (By similarity). {ECO:0000250|UniProtKB:P09514,
CC ECO:0000250|UniProtKB:P09516, ECO:0000305}.
CC -!- PTM: [Isoform Readthrough protein P3-RTD]: In virus particles, more
CC than 200 amino acids are proteolytically cleaved releasing the C-
CC terminus part of the RTD domain (PubMed:7513925, PubMed:2230732). The
CC cleaved product remains attached to the virus particle
CC (PubMed:7513925). {ECO:0000269|PubMed:2230732,
CC ECO:0000269|PubMed:7513925}.
CC -!- MISCELLANEOUS: [Isoform Readthrough protein P3-RTD]: This protein is
CC translated as a fusion protein by episodic readthrough of the major
CC coat protein termination codon. It is composed of the major capsid
CC protein fused to a long C-terminal extension called the readthrough
CC domain (RTD). Readthrough of the terminator codon TAG occurs between
CC the codons for 208-Lys and 210-Val. {ECO:0000269|PubMed:2230732,
CC ECO:0000269|PubMed:29514911}.
CC -!- SIMILARITY: Belongs to the luteoviruses readthrough protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D00530; BAA00421.1; ALT_SEQ; Genomic_RNA.
DR PIR; JA0122; WMVQ53.
DR PIR; S24594; S24594.
DR SMR; P17525; -.
DR Proteomes; UP000006723; Genome.
DR GO; GO:0044229; C:host cell periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 2.60.120.20; -; 1.
DR InterPro; IPR001517; Luteo_coat.
DR InterPro; IPR002929; PLrV_ORF5.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00894; Luteo_coat; 1.
DR Pfam; PF01690; PLRV_ORF5; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Capsid protein; Host cell junction;
KW Host periplasm; Reference proteome; RNA suppression of termination; Virion.
FT CHAIN 1..716
FT /note="Readthrough protein P3-RTD"
FT /id="PRO_0000222429"
FT CHAIN 1..?443
FT /note="Minor capsid readthrough protein"
FT /id="PRO_0000455345"
FT CHAIN ?444..716
FT /note="Cleaved product"
FT /id="PRO_0000455346"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..716
FT /note="Readthrough domain (RTD)"
FT REGION 438..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..698
FT /note="Involved in the efficient long distance movement of
FT the virus and the periplasmic subcellular location"
FT /evidence="ECO:0000269|PubMed:30440046"
FT COMPBIAS 43..62
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 443..444
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P09514"
FT VAR_SEQ 1..591
FT /note="Missing (in isoform P7)"
FT /evidence="ECO:0000305"
FT /id="VSP_038673"
SQ SEQUENCE 716 AA; 79761 MW; 6B65E9AE10449C42 CRC64;
MSTVVVKGNV NGGVQQPRMR RRQSLRRRAN RVQPVVMVTA PGQPRRRRRR RGGNRRSRRT
GVPRGRGSSE TFVFTKDNLV GNTQGSFTFG PSLSDCPAFK DGILKAYHEY KITSILLQFV
SEASSTSSGS IAYELDPHCK VSSLQSYVNK FQITKGGAKT YQARMINGVE WHDSSEDQCR
ILWKGNGKSS DSAGSFRVTI KVALQNPKYD SGSEPSPSPQ PTPTPTPQKH ERFIAYVGIP
MLTIQAREND DQIILGSLGS QRMKYIEDEN QNYTKFSSEY YSQSSMQAVP MYYFNVPKGQ
WSVDISCEGY QPTSSTSDPN RGRSDGMIAY SNADSDYWNV GEADGVKISK LRNDNTYRQG
HPELEINSCH FREGQLLERD ATISFHVEAP TDGRFFLVGP AIQKTAKYNY TISYGDWTDR
DMELGLITVV LDEHLEGTGS ANRVRRPPRE GHTYMASPHE PEGKPVGNKP RDETPIQTQE
RQPDQTPSDD VSDAGSVNSG GPTESLRLEF GVNSDSTYDA TVDGTDWPRI PPPRHPPEPR
VSGNSRTVTD FSSKADLLEN WDAEHFDPGY SKEDVAAATI IAHGSIQDGR SMLEKREENV
KNKTSSWKPP SLKAVSPAIA KLRSIRKSQP LEGGTLNKDA TDGVSSIGSG SLTGGTLKRK
ATIEERLLQT LTTEQRLWYE NFKKTNPPAA TQWLFEYQPP PQVDRNIAEK PFQGRK
