P1_PLRV1
ID P1_PLRV1 Reviewed; 639 AA.
AC P17519;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein P1;
DE AltName: Full=69.7 kDa protein;
DE AltName: Full=Genome-linked protein precursor;
DE AltName: Full=Protein ORF1;
DE Contains:
DE RecName: Full=Serine protease;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=VPg/P1-C25;
DE Flags: Precursor;
GN ORFNames=ORF1;
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 RIBOSOMAL FRAMESHIFTING.
RX PubMed=1547775; DOI=10.1002/j.1460-2075.1992.tb05151.x;
RA Prufer D., Tacke E., Schmitz J., Kull B., Kaufmann A., Rohde W.;
RT "Ribosomal frameshifting in plants: a novel signal directs the -1
RT frameshift in the synthesis of the putative viral replicase of potato
RT leafroll luteovirus.";
RL EMBO J. 11:1111-1117(1992).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, IDENTIFICATION OF VPG, AND PROTEIN
RP SEQUENCE OF 400-431.
RX PubMed=9268161; DOI=10.1006/viro.1997.8654;
RA van der Wilk F., Verbeek M., Dullemans A.M., van den Heuvel J.F.J.M.;
RT "The genome-linked protein of potato leafroll virus is located downstream
RT of the putative protease domain of the ORF1 product.";
RL Virology 234:300-303(1997).
RN [4]
RP RNA-BINDING.
RX PubMed=9862960; DOI=10.1093/nar/27.2.421;
RA Prufer D., Kawchuk L., Monecke M., Nowok S., Fischer R., Rohde W.;
RT "Immunological analysis of potato leafroll luteovirus (PLRV) P1 expression
RT identifies a 25 kDa RNA-binding protein derived via P1 processing.";
RL Nucleic Acids Res. 27:421-425(1999).
RN [5]
RP ACTIVE SITES OF SERINE PROTEASE, AND MUTAGENESIS OF HIS-255; ASP-286 AND
RP SER-354.
RC STRAIN=Isolate Polish;
RX PubMed=11369899; DOI=10.1099/0022-1317-82-6-1517;
RA Sadowy E., Juszczuk M., David C., Gronenborn B., Hulanicka M.D.;
RT "Mutational analysis of the proteinase function of Potato leafroll virus.";
RL J. Gen. Virol. 82:1517-1527(2001).
RN [6]
RP FUNCTION.
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: Precursor from which the VPg molecule is probably released at
CC the onset of the RNA synthesis. Essential for virus replication.
CC Participates, together with the proteins P0 and P7, in the inhibition
CC of the induction of aphid-induced host phytohormones (PubMed:31758809).
CC This could play a role in the attraction to the infected plants by
CC aphids (PubMed:31758809). {ECO:0000269|PubMed:31758809}.
CC -!- SUBCELLULAR LOCATION: [Protein P1]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The isoform P1 is produced by conventional translation,
CC whereas the isoform RNA-directed RNA polymerase is produced by -1
CC ribosomal frameshifting between codons 487 and 488. {ECO:0000305};
CC Name=Protein P1;
CC IsoId=P17519-1; Sequence=Displayed;
CC Name=RNA-directed RNA polymerase;
CC IsoId=P17520-1; Sequence=External;
CC -!- DOMAIN: The C-terminus part of protein P1 and VPg/P1-C25 displays RNA-
CC binding properties.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC protease probably cleaves itself and releases the VPg protein. The VPg
CC protein is probably further cleaved in its C-terminus.
CC {ECO:0000269|PubMed:9268161}.
CC -!- SIMILARITY: Belongs to the peptidase S39B family. {ECO:0000305}.
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DR EMBL; D00530; BAA00417.1; -; Genomic_RNA.
DR PIR; JA0118; WMVQ70.
DR RefSeq; NP_056747.1; NC_001747.1.
DR MEROPS; S39.002; -.
DR GeneID; 1493894; -.
DR KEGG; vg:1493894; -.
DR Proteomes; UP000006723; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR018019; Luteovirus_Orf2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR Pfam; PF02122; Peptidase_S39; 1.
DR PRINTS; PR00913; LVIRUSORF2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Membrane; Protease;
KW Reference proteome; Ribosomal frameshifting; RNA-binding; Serine protease;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..639
FT /note="Protein P1"
FT /id="PRO_0000222396"
FT CHAIN 205..399
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390899"
FT CHAIN 400..639
FT /note="VPg/P1-C25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390900"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 207..399
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT REGION 455..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216,
FT ECO:0000305|PubMed:11369899"
FT ACT_SITE 286
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216,
FT ECO:0000305|PubMed:11369899"
FT ACT_SITE 354
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216,
FT ECO:0000305|PubMed:11369899"
FT SITE 204..205
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 399..400
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000305"
FT MUTAGEN 255
FT /note="H->L: Complete loss of viral genomic or subgenomic
FT RNA production."
FT /evidence="ECO:0000269|PubMed:11369899"
FT MUTAGEN 286
FT /note="D->A: Complete loss of viral genomic or subgenomic
FT RNA production."
FT /evidence="ECO:0000269|PubMed:11369899"
FT MUTAGEN 354
FT /note="S->A: Complete loss of viral genomic or subgenomic
FT RNA production."
FT /evidence="ECO:0000269|PubMed:11369899"
SQ SEQUENCE 639 AA; 69629 MW; AFCF2FB393BEE097 CRC64;
MNRFTAYAAL FFMFSLCSTA KEAGFLHPAF NFRGTSTMSA SSGDYSAAPT PLYKSWALPS
SLNLTTQPPP PLTDRSYYEL VQALTSKMRL DCQTVGDMTW RHLSEMLFAS WNSVKEVSLK
AASVTLWAII NIWFGLYWTL ARLITLFLWT FSIEALCLIL LGCITSLIYK GALSLSEHLP
VFLFMSPLKI IWRAAFSKRN YKNERAVEGY KGFSVPQKPP KSAVIELQHE NGSHLGYANC
IRLYSGENAL VTAEHCLEGA FATSLKTGNR IPMSTFFPIF KSARNDISIL VGPPNWEGLL
SVKGAHFITA DKIGKGPASF YTLEKGEWMC HSATIDGAHH QFVSVLCNTG PGYSGTGFWS
SKNLLGVLKG FPLEEECNYN VMSVIPSIPG ITSPNYVFES TAVKGRVFSD EAVKELEREA
SEAVKKLARF KSLTDKNWAD DYDSDEDYGL EREAATNAPA EKTAQTNSAE KTAPSTSAEK
TALTNKPLNG QAAPSAKTNG NSDIPDAATS APPMDKMVEQ IITAMVGRIN LSEIEEKIVS
RVSQKALQKP KQKKRGRRGG KNKQNSLPPT STQSTSGAPK KEAAPQASGS AGTSRATTTP
APEAKPSGGK NSAKFTPSWR IKQQDSAGQK PDLKLNSKA
