ID   CAPSD_PLRV1             Reviewed;         208 AA.
AC   P17522;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Major capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
DE   AltName: Full=P3 {ECO:0000303|PubMed:18944480};
GN   ORFNames=ORF3;
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.
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   SUBCELLULAR LOCATION.
RX   PubMed=18944480; DOI=10.1094/phyto.2000.90.10.1153;
RA   Gildow F.E., Reavy B., Mayo M.A., Duncan G.H., Woodford J.A., Lamb J.W.,
RA   Hay R.T.;
RT   "Aphid Acquisition and Cellular Transport of Potato leafroll virus-like
RT   Particles Lacking P5 Readthrough Protein.";
RL   Phytopathology 90:1153-1161(2000).
RN   [4] {ECO:0007744|PDB:6SCO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND FUNCTION.
RX   PubMed=31611039; DOI=10.1016/j.str.2019.09.010;
RA   Byrne M.J., Steele J.F.C., Hesketh E.L., Walden M., Thompson R.F.,
RA   Lomonossoff G.P., Ranson N.A.;
RT   "Combining Transient Expression and Cryo-EM to Obtain High-Resolution
RT   Structures of Luteovirid Particles.";
RL   Structure 27:1761-1770.e3(2019).
RN   [5] {ECO:0007744|PDB:7RLM}
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 68-208, AND FUNCTION.
RX   PubMed=34813955; DOI=10.1016/j.jsb.2021.107811;
RA   Adams M.C., Schiltz C.J., Heck M.L., Chappie J.S.;
RT   "Crystal structure of the potato leafroll virus coat protein and
RT   implications for viral assembly.";
RL   J. Struct. Biol. 214:107811-107811(2021).
CC   -!- FUNCTION: Major capsid protein that self-assembles to form an
CC       icosahedral capsid with a T=3 symmetry, about 23 nm in diameter, and
CC       consisting of 180 capsid proteins monomers (PubMed:31611039,
CC       PubMed:34813955). Most of the 180 monomers are the major capsid
CC       protein, but a small percentage contain the minor capsid protein, which
CC       has a long C-terminal extension (PubMed:31611039).
CC       {ECO:0000269|PubMed:31611039, ECO:0000269|PubMed:34813955}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:18944480,
CC       ECO:0000269|PubMed:2230732}.
CC   -!- DOMAIN: The N-terminus like those of many plant virus capsid proteins
CC       is highly basic. These regions may be involved in protein-RNA
CC       interaction. {ECO:0000250|UniProtKB:P17525}.
CC   -!- SIMILARITY: Belongs to the luteoviruses capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00530; BAA00419.1; -; Genomic_RNA.
DR   PIR; JA0122; WMVQ53.
DR   PIR; S24593; S24593.
DR   RefSeq; NP_056749.1; NC_001747.1.
DR   PDB; 6SCO; EM; 3.30 A; A/B/C=1-208.
DR   PDB; 7RLM; X-ray; 3.30 A; A=68-208.
DR   PDBsum; 6SCO; -.
DR   PDBsum; 7RLM; -.
DR   SMR; P17522; -.
DR   GeneID; 1493891; -.
DR   KEGG; vg:1493891; -.
DR   Proteomes; UP000006723; Genome.
DR   GO; GO:0039617; C:T=3 icosahedral 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; IPR029053; Viral_coat.
DR   Pfam; PF00894; Luteo_coat; 1.
DR   PRINTS; PR00915; LUTEOGP1COAT.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Reference proteome;
KW   T=3 icosahedral capsid protein; Virion.
FT   CHAIN           1..208
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000222412"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..62
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          107..119
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   TURN            163..167
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:6SCO"
FT   STRAND          197..204
FT                   /evidence="ECO:0007829|PDB:6SCO"
SQ   SEQUENCE   208 AA;  23153 MW;  E3A35A7DA37571CD CRC64;
     MSTVVVKGNV NGGVQQPRMR RRQSLRRRAN RVQPVVMVTA PGQPRRRRRR RGGNRRSRRT
     GVPRGRGSSE TFVFTKDNLV GNTQGSFTFG PSLSDCPAFK DGILKAYHEY KITSILLQFV
     SEASSTSSGS IAYELDPHCK VSSLQSYVNK FQITKGGAKT YQARMINGVE WHDSSEDQCR
     ILWKGNGKSS DSAGSFRVTI KVALQNPK