ID   POL2_APMV               Reviewed;         997 AA.
AC   P38485;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-DEC-2020, entry version 86.
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   Contains:
DE     RecName: Full=Movement protein;
DE              Short=MP;
DE   Contains:
DE     RecName: Full=Large capsid protein;
DE              Short=LCP;
DE     AltName: Full=Coat protein VP42;
DE     AltName: Full=L subunit;
DE     AltName: Full=Large coat protein;
DE   Contains:
DE     RecName: Full=Small capsid protein;
DE              Short=SCP;
DE     AltName: Full=Coat protein VP22;
DE     AltName: Full=S subunit;
OS   Andean potato mottle virus (APMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX   NCBI_TaxID=12259;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 414-425 AND
RP   801-810.
RC   STRAIN=C;
RX   PubMed=8150598; DOI=10.1159/000150337;
RA   Shindo N., Vicente A.C.P., Krengiel R., de Oliveira D.E.;
RT   "Nucleotide sequence analysis of an Andean potato mottle virus middle
RT   component RNA cDNA clone: comparisons of the encoded proteins with those of
RT   other comoviruses.";
RL   Intervirology 36:169-180(1993).
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. The movement protein allows efficient cell to cell
CC       propagation, by bypassing the host cell wall barrier. Acts by forming a
CC       tubular structure at the host plasmodesmata, enlarging it enough to
CC       allow free passage of virion capsids. Binds to GTP and to single-
CC       stranded RNA and single-stranded DNA in a non-sequence-specific manner.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- FUNCTION: [Large capsid protein]: Together with the 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. The
CC       capsid is formed from 60 copies each of the large and the small capsid
CC       protein. The large capsid protein interacts with the viral RNA.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- FUNCTION: [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 small capsid protein forms the turrets at the fivefold
CC       axes of the viral particle. Also seems to act as suppressor of post-
CC       transcriptional gene silencing (PTGS), a mechanism of plant viral
CC       defense that limits the accumulation of viral RNAs.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Small capsid protein]: Interacts with the large capsid
CC       protein. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Large capsid protein]: Interacts with the small capsid
CC       protein. Homomultimer; assembles as pentons. Interacts with the
CC       movement protein (via C-terminus). {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the large
CC       capsid protein. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host
CC       plasmodesma {ECO:0000250|UniProtKB:P03599}. Note=Assembles in tubules
CC       that are embedded within modified plasmodesmata.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Small capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=RNA2 polyprotein;
CC         IsoId=P38485-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P38485-2; Sequence=VSP_059977;
CC   -!- DOMAIN: [Large capsid protein]: Contains a beta-sheet structure called
CC       beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}.
CC   -!- DOMAIN: [Small capsid protein]: Contains a beta-sheet structure called
CC       beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}.
CC   -!- DOMAIN: [Movement protein]: The C-terminus is involved in binding to
CC       the large capsid protein, and hence to the virion.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC       like protease in vivo yield mature proteins.
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-75 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; L16239; AAA42421.1; -; Genomic_RNA.
DR   SMR; P38485; -.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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   Alternative initiation; Capsid protein; Direct protein sequencing;
KW   DNA-binding; GTP-binding; Host cell junction; Nucleotide-binding;
KW   RNA-binding; Suppressor of RNA silencing; T=3 icosahedral capsid protein;
KW   Transport; Viral movement protein; Virion.
FT   CHAIN           1..997
FT                   /note="RNA2 polyprotein"
FT                   /id="PRO_0000445837"
FT   CHAIN           1..413
FT                   /note="VP58"
FT                   /id="PRO_0000445838"
FT   CHAIN           75..413
FT                   /note="Movement protein"
FT                   /id="PRO_0000037021"
FT   CHAIN           414..800
FT                   /note="Large capsid protein"
FT                   /id="PRO_0000037022"
FT   CHAIN           801..997
FT                   /note="Small capsid protein"
FT                   /id="PRO_0000037023"
FT   REGION          370..376
FT                   /note="Involved in tubule formation by the movement
FT                   protein"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   SITE            413..414
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   SITE            430
FT                   /note="Interaction with the viral RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   SITE            800..801
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_059977"
SQ   SEQUENCE   997 AA;  110329 MW;  2AE0A1CB291DBB46 CRC64;
     MSELIVSDVV ALSVWGLLTV VKVYQGNFSL SVLFSEAQTL GFLFFISCHW LQSILLPWVV
     KIKCATRFDI DLVEMEMRAE KYLNSIPANV LEDRAKAYNV SKMTSIKNQI PSGKALYQNG
     KSLASMIKSQ FQPISKVLKG GEVKSYNYIP VGSFTAGEHC ELAVPIMPEE ELAAIVPDSD
     FALVTKEDNK AKSVHVGAVE IVMECMTSPD CDIYGGAMFV DTFHEDPKNA VRALFVTQLK
     GGVSPRCLFF PDTQVEIKKG MNERFRLILS SGNSDFKPGE NLAYLKANVA MCGISMNKGY
     VPTAFHESYA RKERASVIEY LGRYSAVIHH RNEFKPEMLK RDGLSFRFGG KTKLIEKGPL
     QYEWSETASK VVSVKGTGPP TKEDETISKE VSETLGATEH VVFPTRNVVA QAQMEVAQFG
     RLLDDTKSLK LQSLLNSRIA AGRFSIPMTA VKGTVVFDGL LASLIGTTLR GAPMFRHTYR
     QSTKLRFIFT INVPISTGIG LMVGYNSVTS DKHLTNEYTI SSEESVVWNP ACQGVLEFSV
     SPNPCGMYWS YDYFRQTGSR LSICVISPWS ATPTTDCAVA WQIHVDDEQM TMSIFNPTQA
     PAVLPVKRWM GNLIFKQGAQ EQVKKMPLAI GAAVGDDKTA VMTMPNSLAA MWNYQIGTFN
     FEFTKLSSPF IKGTLLAFIA MDQDVSYSLE ELQNFPNKIV QFDEKDGRAY VSFGEEHFAQ
     AWSTQVSGAV TSAKRGCPYL YVVSKDCIAS TICGDFQVGV KLLSIENYSP CGYNPGLVVA
     STIVQNTAGS NSTSLLAWPQ FCSPCINVWS EFCALDIPVV DTTKVNFAQY SLDLVNPTVS
     ANASGRNWRF VLIPSPMVYL LQTSDWKRGK LHFKLKILGK SNVKRSEWSS TSRIDVRRAP
     GTEYLNAITV FTAEPHADEI NFEIEICGPN NGFEMWNADF GNQLSWMANV VIGNPDQAGI
     HQWYVRPGEN FEVAGNRMVQ PLALSGEDGT GMLPILK