POL2_CPMVS
ID POL2_CPMVS Reviewed; 1046 AA.
AC P03599; Q66170; Q84103; Q9WJE1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=RNA2 polyprotein;
DE AltName: Full=Genome polyprotein M;
DE AltName: Full=M RNA polyprotein;
DE AltName: Full=Middle component RNA polyprotein;
DE AltName: Full=P2;
DE Contains:
DE RecName: Full=VP58;
DE AltName: Full=P58;
DE Contains:
DE RecName: Full=Movement protein;
DE Short=MP;
DE AltName: Full=48 kDa protein;
DE Contains:
DE RecName: Full=Large capsid protein;
DE Short=LCP;
DE AltName: Full=Coat protein VP37;
DE AltName: Full=L subunit;
DE AltName: Full=Large coat protein;
DE Contains:
DE RecName: Full=Small capsid protein precursor;
DE AltName: Full=S subunit;
DE Contains:
DE RecName: Full=Mature small capsid protein;
DE Short=SCP;
DE AltName: Full=Coat protein VP23;
DE AltName: Full=Small capsid protein, N-terminus part;
DE AltName: Full=Small coat protein, N-terminus part;
DE Contains:
DE RecName: Full=Small capsid protein C-terminus part;
DE AltName: Full=Small coat protein C-terminus part;
OS Cowpea mosaic virus (strain SB) (CPMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=928299;
OH NCBI_TaxID=3821; Cajanus cajan (Pigeon pea) (Cajanus indicus).
OH NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ISOFORM 1), AND ACETYLATION AT MET-460.
RC STRAIN=SB;
RX PubMed=6641721;
RA van Wezenbeek P., Verver J., Harmsen J., Vos P., van Kammen A.;
RT "Primary structure and gene organization of the middle-component RNA of
RT cowpea mosaic virus.";
RL EMBO J. 2:941-946(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RC STRAIN=SB;
RX PubMed=16453487; DOI=10.1002/j.1460-2075.1983.tb01731.x;
RA Lomonossoff G.P., Shanks M.;
RT "The nucleotide sequence of cowpea mosaic virus B RNA.";
RL EMBO J. 2:2253-2258(1983).
RN [3]
RP PROTEOLYTIC CLEAVAGE (RNA2 POLYPROTEIN).
RX PubMed=16789216; DOI=10.1128/jvi.41.1.8-17.1982;
RA Franssen H., Goldbach R., Broekhuijsen M., Moerman M., van Kammen A.;
RT "Expression of Middle-Component RNA of Cowpea Mosaic Virus: In Vitro
RT Generation of a Precursor to Both Capsid Proteins by a Bottom-Component
RT RNA-Encoded Protease from Infected Cells.";
RL J. Virol. 41:8-17(1982).
RN [4]
RP ALTERNATIVE INITIATION.
RX PubMed=2773321; DOI=10.1016/0042-6822(89)90133-5;
RA Holness C.L., Lomonossoff G.P., Evans D., Maule A.J.;
RT "Identification of the initiation codons for translation of cowpea mosaic
RT virus middle component RNA using site-directed mutagenesis of an infectious
RT cDNA clone.";
RL Virology 172:311-320(1989).
RN [5]
RP ALTERNATIVE INITIATION.
RX PubMed=1765773; DOI=10.1099/0022-1317-72-12-3109;
RA Belsham G.J., Lomonossoff G.P.;
RT "The mechanism of translation of cowpea mosaic virus middle component RNA:
RT no evidence for internal initiation from experiments in an animal cell
RT transient expression system.";
RL J. Gen. Virol. 72:3109-3113(1991).
RN [6]
RP FUNCTION (MOVEMENT PROTEIN), AND SUBCELLULAR LOCATION (VP58).
RX PubMed=8497075; DOI=10.1128/jvi.67.6.3660-3664.1993;
RA Wellink J., van Lent J.W., Verver J., Sijen T., Goldbach R.W.,
RA van Kammen A.;
RT "The cowpea mosaic virus M RNA-encoded 48-kilodalton protein is responsible
RT for induction of tubular structures in protoplasts.";
RL J. Virol. 67:3660-3664(1993).
RN [7]
RP FUNCTION (MOVEMENT PROTEIN).
RX PubMed=9501035; DOI=10.1006/viro.1997.8982;
RA Verver J., Wellink J., Van Lent J., Gopinath K., Van Kammen A.;
RT "Studies on the movement of cowpea mosaic virus using the jellyfish green
RT fluorescent protein.";
RL Virology 242:22-27(1998).
RN [8]
RP MASS SPECTROMETRY, FUNCTION (SMALL CAPSID PROTEIN PRECURSOR), PROTEOLYTIC
RP CLEAVAGE (SMALL CAPSID PROTEIN PRECURSOR), AND DOMAIN (SMALL CAPSID PROTEIN
RP PRECURSOR).
RX PubMed=10049828; DOI=10.1006/viro.1998.9567;
RA Taylor K.M., Spall V.E., Butler P.J.G., Lomonossoff G.P.;
RT "The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic
RT virus is involved in RNA encapsidation.";
RL Virology 255:129-137(1999).
RN [9]
RP LACK OF GLYCOSYLATION (LARGE CAPSID PROTEIN), AND LACK OF GLYCOSYLATION
RP (MATURE SMALL CAPSID PROTEIN).
RX PubMed=10725439; DOI=10.1099/0022-1317-81-4-1111;
RA Altmann F., Lomonossoff G.P.;
RT "Glycosylation of the capsid proteins of cowpea mosaic virus: a
RT reinvestigation shows the absence of sugar residues.";
RL J. Gen. Virol. 81:1111-1114(2000).
RN [10]
RP MUTAGENESIS OF 126-ILE-PRO-127; 209-PRO-VAL-210; 220-SER-ASP-221;
RP 238-ILE-GLU-239; 259-VAL-ASP-260; 279-ARG-GLY-280; 409-LEU-LYS-410 AND
RP 448-LEU-ASP-449.
RX PubMed=10662615; DOI=10.1006/viro.1999.0087;
RA Bertens P., Wellink J., Goldbach R., van Kammen A.;
RT "Mutational analysis of the cowpea mosaic virus movement protein.";
RL Virology 267:199-208(2000).
RN [11]
RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN).
RX PubMed=10864669; DOI=10.1128/jvi.74.14.6556-6563.2000;
RA Carette J.E., Stuiver M., Van Lent J., Wellink J., Van Kammen A.;
RT "Cowpea mosaic virus infection induces a massive proliferation of
RT endoplasmic reticulum but not Golgi membranes and is dependent on de novo
RT membrane synthesis.";
RL J. Virol. 74:6556-6563(2000).
RN [12]
RP DOMAIN (MOVEMENT PROTEIN), AND FUNCTION (MOVEMENT PROTEIN).
RX PubMed=12556992; DOI=10.1007/s00705-002-0918-z;
RA Bertens P., Heijne W., van der Wel N., Wellink J., van Kammen A.;
RT "Studies on the C-terminus of the Cowpea mosaic virus movement protein.";
RL Arch. Virol. 148:265-279(2003).
RN [13]
RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN), AND FUNCTION (MOVEMENT PROTEIN).
RX PubMed=14579172; DOI=10.1007/s00705-003-0180-z;
RA Gopinath K., Bertens P., Pouwels J., Marks H., Van Lent J., Wellink J.,
RA Van Kammen A.;
RT "Intracellular distribution of cowpea mosaic virus movement protein as
RT visualised by green fluorescent protein fusions.";
RL Arch. Virol. 148:2099-2114(2003).
RN [14]
RP DOMAIN (MOVEMENT PROTEIN), INTERACTION WITH THE LARGE CAPSID PROTEIN
RP (MOVEMENT PROTEIN), AND INTERACTION WITH THE MOVEMENT PROTEIN (LARGE CAPSID
RP PROTEIN).
RX PubMed=12867661; DOI=10.1099/vir.0.19101-0;
RA Carvalho C.M., Wellink J., Ribeiro S.G., Goldbach R.W., Van Lent J.W.;
RT "The C-terminal region of the movement protein of Cowpea mosaic virus is
RT involved in binding to the large but not to the small coat protein.";
RL J. Gen. Virol. 84:2271-2277(2003).
RN [15]
RP FUNCTION (SMALL CAPSID PROTEIN C-TERMINUS PART), AND FUNCTION (SMALL CAPSID
RP PROTEIN PRECURSOR).
RX PubMed=15483261; DOI=10.1099/vir.0.80454-0;
RA Canizares M.C., Taylor K.M., Lomonossoff G.P.;
RT "Surface-exposed C-terminal amino acids of the small coat protein of Cowpea
RT mosaic virus are required for suppression of silencing.";
RL J. Gen. Virol. 85:3431-3435(2004).
RN [16]
RP FUNCTION (SMALL CAPSID PROTEIN C-TERMINUS PART), AND FUNCTION (SMALL CAPSID
RP PROTEIN PRECURSOR).
RX PubMed=15165817; DOI=10.1016/j.virol.2004.02.013;
RA Liu L., Grainger J., Canizares M.C., Angell S.M., Lomonossoff G.P.;
RT "Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be
RT counteracted by a RNA-2-encoded suppressor of silencing.";
RL Virology 323:37-48(2004).
RN [17]
RP FUNCTION (MOVEMENT PROTEIN), AND MUTAGENESIS OF VAL-259 AND ASP-260.
RX PubMed=14722313; DOI=10.1128/jvi.78.3.1591-1594.2004;
RA Carvalho C.M., Pouwels J., van Lent J.W., Bisseling T., Goldbach R.W.,
RA Wellink J.;
RT "The movement protein of cowpea mosaic virus binds GTP and single-stranded
RT nucleic acid in vitro.";
RL J. Virol. 78:1591-1594(2004).
RN [18]
RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN).
RX PubMed=27339685; DOI=10.1007/s00705-016-2936-2;
RA den Hollander P.W., Kieper S.N., Borst J.W., van Lent J.W.;
RT "The role of plasmodesma-located proteins in tubule-guided virus transport
RT is limited to the plasmodesmata.";
RL Arch. Virol. 161:2431-2440(2016).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 460-1022, INTERACTION WITH THE
RP MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION WITH THE
RP LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), FUNCTION (LARGE CAPSID
RP PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN), SUBCELLULAR LOCATION
RP (LARGE CAPSID PROTEIN), AND SUBCELLULAR LOCATION (MATURE SMALL CAPSID
RP PROTEIN).
RC STRAIN=Bi1 mutant;
RX PubMed=10603314; DOI=10.1006/viro.1999.0038;
RA Lin T., Chen Z., Usha R., Stauffacher C.V., Dai J.B., Schmidt T.,
RA Johnson J.E.;
RT "The refined crystal structure of cowpea mosaic virus at 2.8 A
RT resolution.";
RL Virology 265:20-34(1999).
RN [20] {ECO:0007744|PDB:2BFU}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 460-828 AND 834-1022.
RX PubMed=16873025; DOI=10.1016/j.chembiol.2006.05.014;
RA Ochoa W.F., Chatterji A., Lin T., Johnson J.E.;
RT "Generation and structural analysis of reactive empty particles derived
RT from an icosahedral virus.";
RL Chem. Biol. 13:771-778(2006).
RN [21] {ECO:0007744|PDB:5A32, ECO:0007744|PDB:5A33}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 ANGSTROMS) OF 460-828 AND 834-1046,
RP FUNCTION (SMALL CAPSID PROTEIN PRECURSOR), MUTAGENESIS OF ARG-476; TRP-649;
RP VAL-942; GLU-980; PHE-1025; ARG-1026 AND PHE-1027, INTERACTION WITH THE
RP MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION WITH THE
RP LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), SUBUNIT (LARGE CAPSID
RP PROTEIN), FUNCTION (LARGE CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID
RP PROTEIN), SUBCELLULAR LOCATION (LARGE CAPSID PROTEIN), AND SUBCELLULAR
RP LOCATION (MATURE SMALL CAPSID PROTEIN).
RX PubMed=26657148; DOI=10.1038/ncomms10113;
RA Hesketh E.L., Meshcheriakova Y., Dent K.C., Saxena P., Thompson R.F.,
RA Cockburn J.J., Lomonossoff G.P., Ranson N.A.;
RT "Mechanisms of assembly and genome packaging in an RNA virus revealed by
RT high-resolution cryo-EM.";
RL Nat. Commun. 6:10113-10113(2015).
RN [22] {ECO:0007744|PDB:5FMO}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 460-833 AND 834-1046, INTERACTION
RP WITH THE MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION
RP WITH THE LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), SUBUNIT (LARGE
RP CAPSID PROTEIN), PROTEOLYTIC CLEAVAGE (SMALL CAPSID PROTEIN PRECURSOR),
RP FUNCTION (LARGE CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN),
RP SUBCELLULAR LOCATION (LARGE CAPSID PROTEIN), AND SUBCELLULAR LOCATION
RP (MATURE SMALL CAPSID PROTEIN).
RX PubMed=27021160; DOI=10.1016/j.str.2016.02.011;
RA Huynh N.T., Hesketh E.L., Saxena P., Meshcheriakova Y., Ku Y.C.,
RA Hoang L.T., Johnson J.E., Ranson N.A., Lomonossoff G.P., Reddy V.S.;
RT "Crystal Structure and Proteomics Analysis of Empty Virus-like Particles of
RT Cowpea Mosaic Virus.";
RL Structure 24:567-575(2016).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.25 ANGSTROMS) OF 460-828 AND 834-1046,
RP MUTAGENESIS OF ASN-633, INTERACTION WITH THE MATURE SMALL CAPSID PROTEIN
RP (LARGE CAPSID PROTEIN), INTERACTION WITH THE LARGE CAPSID PROTEIN (MATURE
RP SMALL CAPSID PROTEIN), SUBUNIT (LARGE CAPSID PROTEIN), FUNCTION (LARGE
RP CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN), SUBCELLULAR
RP LOCATION (LARGE CAPSID PROTEIN), SUBCELLULAR LOCATION (MATURE SMALL CAPSID
RP PROTEIN), DOMAIN (MATURE SMALL CAPSID PROTEIN), AND DOMAIN (LARGE CAPSID
RP PROTEIN).
RX PubMed=28373698; DOI=10.1038/s41598-017-00533-w;
RA Hesketh E.L., Meshcheriakova Y., Thompson R.F., Lomonossoff G.P.,
RA Ranson N.A.;
RT "The structures of a naturally empty cowpea mosaic virus particle and its
RT genome-containing counterpart by cryo-electron microscopy.";
RL Sci. Rep. 7:539-539(2017).
CC -!- FUNCTION: [VP58]: Responsible for viral RNA2 accumulation. May function
CC by recruiting the RNA1-encoded polyprotein that contains the
CC replication protein to RNA2 and enable its replication.
CC {ECO:0000250|UniProtKB:P23009}.
CC -!- FUNCTION: [Movement protein]: Transports the viral genome to
CC neighboring plant cells directly through plasmosdesmata, without any
CC budding (PubMed:9501035). The movement protein allows efficient cell to
CC cell propagation, by bypassing the host cell wall barrier. Acts by
CC forming a tubular structure at the host plasmodesmata, enlarging it
CC enough to allow free passage of virion capsids (PubMed:12556992,
CC PubMed:14579172) (Probable). Binds to GTP and to single-stranded RNA
CC and single-stranded DNA in a non-sequence-specific manner
CC (PubMed:14722313). {ECO:0000269|PubMed:12556992,
CC ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:14722313,
CC ECO:0000269|PubMed:9501035, ECO:0000305|PubMed:8497075}.
CC -!- FUNCTION: [Large capsid protein]: Together with the mature small capsid
CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive
CC strand RNA genome, with a diameter of approximately 300 Angstroms
CC (PubMed:28373698, PubMed:10603314, PubMed:26657148, PubMed:27021160).
CC The capsid is formed from 60 copies each of the large and the small
CC capsid protein (PubMed:28373698, PubMed:10603314, PubMed:26657148,
CC PubMed:27021160). The large capsid protein interacts with the viral RNA
CC (PubMed:28373698, PubMed:26657148). {ECO:0000269|PubMed:10603314,
CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160,
CC ECO:0000269|PubMed:28373698}.
CC -!- FUNCTION: [Mature small capsid protein]: Together with the large capsid
CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive
CC strand RNA genome, with a diameter of approximately 300 Angstroms. The
CC capsid is formed from 60 copies each of the large and the small capsid
CC protein. The mature small capsid protein forms the turrets at the
CC fivefold axes of the viral particle. {ECO:0000269|PubMed:10603314,
CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160,
CC ECO:0000269|PubMed:28373698}.
CC -!- FUNCTION: [Small capsid protein precursor]: The cleavable C-terminus of
CC small capsid protein seems to be involved in viral assembly and RNA
CC packaging (PubMed:10049828). After virus assembly, these amino acids
CC are cleaved off during the normal maturation of the virus
CC (PubMed:26657148, PubMed:10049828). Also seems to act as suppressor of
CC post-transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs (PubMed:15483261,
CC PubMed:15165817). {ECO:0000269|PubMed:10049828,
CC ECO:0000269|PubMed:15165817, ECO:0000269|PubMed:15483261,
CC ECO:0000269|PubMed:26657148}.
CC -!- FUNCTION: [Small capsid protein C-terminus part]: Acts as a suppressor
CC of RNA-mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. {ECO:0000269|PubMed:15165817,
CC ECO:0000269|PubMed:15483261}.
CC -!- SUBUNIT: [Mature small capsid protein]: Interacts with the large capsid
CC protein (PubMed:26657148, PubMed:10603314).
CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148}.
CC -!- SUBUNIT: [Large capsid protein]: Interacts with the mature small capsid
CC protein (PubMed:26657148, PubMed:27021160, PubMed:28373698,
CC PubMed:10603314). Homomultimer; assembles as pentons (PubMed:26657148,
CC PubMed:27021160, PubMed:28373698). Interacts with the movement protein
CC (via C-terminus) (PubMed:12867661). {ECO:0000269|PubMed:12867661,
CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160,
CC ECO:0000269|PubMed:28373698}.
CC -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the large
CC capsid protein (PubMed:12867661). {ECO:0000269|PubMed:12867661}.
CC -!- SUBCELLULAR LOCATION: [VP58]: Host nucleus
CC {ECO:0000269|PubMed:8497075}.
CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host
CC plasmodesma {ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}.
CC Note=Assembles in tubules that are embedded within modified
CC plasmodesmata. {ECO:0000269|PubMed:10864669,
CC ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}.
CC -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion
CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148,
CC ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.
CC -!- SUBCELLULAR LOCATION: [Mature small capsid protein]: Virion
CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148,
CC ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=RNA2 polyprotein;
CC IsoId=P03599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P03599-2; Sequence=VSP_059978;
CC -!- DOMAIN: [Small capsid protein precursor]: The C-terminus is required
CC for efficient assembly and RNA packaging.
CC {ECO:0000269|PubMed:10049828}.
CC -!- DOMAIN: [Large capsid protein]: Contains a beta-sheet structure called
CC beta-barrel jelly roll. {ECO:0000269|PubMed:28373698}.
CC -!- DOMAIN: [Mature small capsid protein]: Contains a beta-sheet structure
CC called beta-barrel jelly roll. {ECO:0000269|PubMed:28373698}.
CC -!- DOMAIN: [Movement protein]: The C-terminus is involved in binding to
CC the large capsid protein, and hence to the virion.
CC {ECO:0000269|PubMed:12556992, ECO:0000269|PubMed:12867661}.
CC -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC like protease in vivo yield mature proteins.
CC {ECO:0000269|PubMed:16789216}.
CC -!- PTM: [Small capsid protein precursor]: The C-terminal 24 amino acids of
CC the small capsid protein are specifically cleaved by the RNA1 encoded
CC picornain 3C-like protease during maturation.
CC {ECO:0000269|PubMed:10049828, ECO:0000269|PubMed:27021160}.
CC -!- PTM: [Large capsid protein]: Not glycosylated.
CC {ECO:0000269|PubMed:10725439}.
CC -!- PTM: [Mature small capsid protein]: Not glycosylated.
CC {ECO:0000269|PubMed:10725439}.
CC -!- MASS SPECTROMETRY: [Mature small capsid protein]: Mass=21121.8;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10049828};
CC -!- MISCELLANEOUS: [Isoform 2]: The 2 isoforms probably arise from
CC alternative initiation (leaky scanning). {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-118 is the initiator.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ny7";
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DR EMBL; X00729; CAA25314.1; -; Genomic_RNA.
DR EMBL; X00729; CAA25315.1; -; Genomic_RNA.
DR EMBL; X00729; CAA25317.1; -; Genomic_RNA.
DR RefSeq; NP_613285.1; NC_003550.1.
DR PDB; 1NY7; X-ray; 3.00 A; 1=834-1022, 2=460-828.
DR PDB; 2BFU; X-ray; 4.00 A; L=460-828, S=834-1022.
DR PDB; 5A32; EM; 3.44 A; A=834-1022, B=460-828.
DR PDB; 5A33; EM; 3.04 A; A=834-1046, B=460-828.
DR PDB; 5FMO; X-ray; 2.30 A; L=460-833, S=834-1046.
DR PDBsum; 1NY7; -.
DR PDBsum; 2BFU; -.
DR PDBsum; 5A32; -.
DR PDBsum; 5A33; -.
DR PDBsum; 5FMO; -.
DR SMR; P03599; -.
DR iPTMnet; P03599; -.
DR PRIDE; P03599; -.
DR GeneID; 956626; -.
DR KEGG; vg:956626; -.
DR EvolutionaryTrace; P03599; -.
DR Proteomes; UP000008589; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IDA:UniProtKB.
DR Gene3D; 2.60.120.20; -; 2.
DR InterPro; IPR003181; Como_LCP.
DR InterPro; IPR003182; RNA2_polyprotein.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF02247; Como_LCP; 1.
DR Pfam; PF02248; Como_SCP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Capsid protein;
KW DNA-binding; GTP-binding; Host cell junction; Host nucleus;
KW Nucleotide-binding; Reference proteome; RNA-binding;
KW Suppressor of RNA silencing; T=3 icosahedral capsid protein; Transport;
KW Viral movement protein; Virion.
FT CHAIN 1..1046
FT /note="RNA2 polyprotein"
FT /id="PRO_0000445839"
FT CHAIN 1..459
FT /note="VP58"
FT /id="PRO_0000037024"
FT CHAIN 118..459
FT /note="Movement protein"
FT /id="PRO_0000445840"
FT CHAIN 460..833
FT /note="Large capsid protein"
FT /id="PRO_0000037025"
FT CHAIN 834..1046
FT /note="Small capsid protein precursor"
FT /id="PRO_0000445841"
FT CHAIN 834..1022
FT /note="Mature small capsid protein"
FT /id="PRO_0000037026"
FT CHAIN 1023..1046
FT /note="Small capsid protein C-terminus part"
FT /id="PRO_0000037027"
FT REGION 62..84
FT /note="Hydrophobic"
FT /evidence="ECO:0000255"
FT REGION 409..415
FT /note="Involved in tubule formation by the movement
FT protein"
FT /evidence="ECO:0000269|PubMed:12556992"
FT SITE 459..460
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10049828"
FT SITE 476
FT /note="Interaction with the viral RNA"
FT /evidence="ECO:0000269|PubMed:26657148"
FT SITE 633
FT /note="Interaction with the viral RNA; probable role in
FT viral RNA packaging"
FT /evidence="ECO:0000269|PubMed:28373698"
FT SITE 649
FT /note="Interaction with the viral RNA; probable role in
FT viral RNA packaging"
FT /evidence="ECO:0000269|PubMed:26657148,
FT ECO:0000269|PubMed:28373698"
FT SITE 833..834
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10049828"
FT SITE 1022..1023
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:27021160"
FT SITE 1025
FT /note="Involved in viral capsid assembly and RNA binding"
FT /evidence="ECO:0000269|PubMed:26657148"
FT MOD_RES 460
FT /note="N-acetylmethionine; by host"
FT /evidence="ECO:0000269|PubMed:6641721"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2)"
FT /id="VSP_059978"
FT MUTAGEN 126..127
FT /note="IP->AA: No effect on the formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 209..210
FT /note="PV->AA: Strong decrease in the formation of tubules
FT induced by the movement protein; complete loss of
FT infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 220..221
FT /note="SD->AA: No effect on the formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 238..239
FT /note="IE->AA: Complete loss of formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 259..260
FT /note="VD->AA: Complete loss of formation of tubules
FT induced by the movement protein and complete loss of GTP
FT binding; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615,
FT ECO:0000269|PubMed:14722313"
FT MUTAGEN 259
FT /note="V->A: Complete loss of GTP binding; when associated
FT with A-260."
FT /evidence="ECO:0000269|PubMed:14722313"
FT MUTAGEN 260
FT /note="D->A: Complete loss of GTP binding; when associated
FT with A-259."
FT /evidence="ECO:0000269|PubMed:14722313"
FT MUTAGEN 279..280
FT /note="RG->AA: Complete loss of formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 409..410
FT /note="LK->AA: No effect on the formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 448..449
FT /note="LD->AA: No effect on the formation of tubules
FT induced by the movement protein; No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:10662615"
FT MUTAGEN 476
FT /note="R->D,E: Complete loss of RNA packaging and decreased
FT capsid assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 476
FT /note="R->G,K,W: No effect on viral yield and virus
FT systemic transport."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 633
FT /note="N->A: Loss of hability to cause a systemic infection
FT in the host plant; no effect on encapsidation."
FT /evidence="ECO:0000269|PubMed:28373698"
FT MUTAGEN 633
FT /note="N->D: Markedly reduced viral yield and loss of
FT hability to cause a systemic infection in the host plant
FT probably due to reduced RNA encapsidation."
FT /evidence="ECO:0000269|PubMed:28373698"
FT MUTAGEN 649
FT /note="W->A,D: No effect."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 649
FT /note="W->F: Complete loss of viral RNA binding and capsid
FT assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 942
FT /note="V->W: Loss of capsid assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 980
FT /note="E->R: Complete loss of capsid assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 1025
FT /note="F->W: Strongly reduces the efficiency of RNA
FT packaging. No effect on particle assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 1026
FT /note="R->D: Complete loss of capsid assembly."
FT /evidence="ECO:0000269|PubMed:26657148"
FT MUTAGEN 1027
FT /note="F->W: Slightly reduced viral particle yield."
FT /evidence="ECO:0000269|PubMed:26657148"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:1NY7"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 482..491
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 518..522
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 546..555
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:5FMO"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 597..602
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 606..613
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 623..635
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 645..661
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:1NY7"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 690..695
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 698..711
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:5FMO"
FT TURN 777..779
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 784..791
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 801..818
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 846..851
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 861..866
FT /evidence="ECO:0007829|PDB:5FMO"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 881..884
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 888..895
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 896..911
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 923..929
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 932..935
FT /evidence="ECO:0007829|PDB:5A32"
FT STRAND 938..943
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 949..957
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 960..963
FT /evidence="ECO:0007829|PDB:5FMO"
FT TURN 970..973
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 978..984
FT /evidence="ECO:0007829|PDB:5FMO"
FT TURN 986..988
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 989..998
FT /evidence="ECO:0007829|PDB:5FMO"
FT STRAND 1003..1009
FT /evidence="ECO:0007829|PDB:5FMO"
FT HELIX 1027..1032
FT /evidence="ECO:0007829|PDB:5A33"
SQ SEQUENCE 1046 AA; 116218 MW; 350EBECBF6558A1E CRC64;
MFSFTEAKSK ISLWTRSAAP LNNVYLSYSC RCGLGKRKLA GGCCSAPYIT CYDSADFRRV
QYLYFCLTRY CCLYFFLLLL ADWFYKKSSI FFETEFSRGF RTWRKIVKLL YILPKFEMES
IMSRGIPSGI LEEKAIQFKR AKEGNKPLKD EIPKPEDMYV SHTSKWNVLR KMSQKTVDLS
KAAAGMGFIN KHMLTGNILA QPTTVLDIPV TKDKTLAMAS DFIRKENLKT SAIHIGAIEI
IIQSFASPES DLMGGFLLVD SLHTDTANAI RSIFVAPMRG GRPVRVVTFP NTLAPVSCDL
NNRFKLICSL PNCDIVQGSQ VAEVSVNVAG CATSIEKSHT PSQLYTEEFE KEGAVVVEYL
GRQTYCAQPS NLPTEEKLRS LKFDFHVEQP SVLKLSNSCN AHFVKGESLK YSISGKEAEN
HAVHATVVSR EGASAAPKQY DPILGRVLDP RNGNVAFPQM EQNLFALSLD DTSSVRGSLL
DTKFAQTRVL LSKAMAGGDV LLDEYLYDVV NGQDFRATVA FLRTHVITGK IKVTATTNIS
DNSGCCLMLA INSGVRGKYS TDVYTICSQD SMTWNPGCKK NFSFTFNPNP CGDSWSAEMI
SRSRVRMTVI CVSGWTLSPT TDVIAKLDWS IVNEKCEPTI YHLADCQNWL PLNRWMGKLT
FPQGVTSEVR RMPLSIGGGA GATQAFLANM PNSWISMWRY FRGELHFEVT KMSSPYIKAT
VTFLIAFGNL SDAFGFYESF PHRIVQFAEV EEKCTLVFSQ QEFVTAWSTQ VNPRTTLEAD
GCPYLYAIIH DSTTGTISGD FNLGVKLVGI KDFCGIGSNP GIDGSRLLGA IAQGPVCAEA
SDVYSPCMIA STPPAPFSDV TAVTFDLING KITPVGDDNW NTHIYNPPIM NVLRTAAWKS
GTIHVQLNVR GAGVKRADWD GQVFVYLRQS MNPESYDART FVISQPGSAM LNFSFDIIGP
NSGFEFAESP WANQTTWYLE CVATNPRQIQ QFEVNMRFDP NFRVAGNILM PPFPLSTETP
PLLKFRFRDI ERSKRSVMVG HTATAA
