ID   POL2_GFLVN              Reviewed;        1110 AA.
AC   Q91HK5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=RNA2 polyprotein;
DE   AltName: Full=P2;
DE   Contains:
DE     RecName: Full=Protein 2A;
DE              Short=P2A;
DE   Contains:
DE     RecName: Full=Movement protein;
DE     AltName: Full=2B-MP;
DE   Contains:
DE     RecName: Full=Coat protein;
DE     AltName: Full=2C-CP;
OS   Grapevine fanleaf virus (isolate NW) (GFLV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX   NCBI_TaxID=282370;
OH   NCBI_TaxID=29760; Vitis vinifera (Grape).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11325468; DOI=10.1016/s0168-1702(01)00235-0;
RA   Wetzel T., Meunier L., Jaeger U., Reustle G.M., Krczal G.;
RT   "Complete nucleotide sequences of the RNAs 2 of German isolates of
RT   Grapevine fanleaf and Arabis mosaic nepoviruses.";
RL   Virus Res. 75:139-145(2001).
CC   -!- FUNCTION: [Protein 2A]: Implicated in RNA2 replication. Could also be
CC       required for nematode transmission of the virus (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: [Movement protein]: Transports viral genome to neighboring
CC       plant cells directly through plasmosdesmata, without any budding. The
CC       movement protein allows efficient cell to cell propagation, by
CC       bypassing the host cell wall barrier. Acts by forming a tubular
CC       structure at the host plasmodesmata, enlarging it enough to allow free
CC       passage of virion capsids (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma.
CC       Note=Assembles in tubules that are embedded within modified
CC       plasmodesmata (By similarity). Movement proteins are targeted
CC       preferentially to calreticulin-labeled foci within the youngest cross
CC       walls, where they assemble into tubules. During cell division, they
CC       colocalize in the cell plate with KNOLLE, a cytokinesis-specific
CC       syntaxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2A]: Host cytoplasm. Host nucleus.
CC       Note=Cytoplasmic early in infection. Later in infection, it becomes
CC       progressively concentrated around the nucleus, where it forms large
CC       aggregates.
CC   -!- SUBCELLULAR LOCATION: [Coat protein]: Virion {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages in vivo by the P1 encoded 3C-like
CC       protease yield mature proteins. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Virions are comprised of 60 copies of the coat protein.
CC   -!- SIMILARITY: Belongs to the nepoviruses RNA2 polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY017338; AAK07727.1; -; Genomic_RNA.
DR   SMR; Q91HK5; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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:0019028; C:viral capsid; 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; IPR005054; Nepo_coat.
DR   InterPro; IPR005305; Nepo_coat_C.
DR   InterPro; IPR005306; Nepo_coat_N.
DR   InterPro; IPR021081; Nepovirus_subgr_A_2A.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF12312; NeA_P2; 1.
DR   Pfam; PF03391; Nepo_coat; 1.
DR   Pfam; PF03688; Nepo_coat_C; 1.
DR   Pfam; PF03689; Nepo_coat_N; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cell junction; Host cytoplasm; Host nucleus;
KW   Transport; Viral movement protein; Virion.
FT   CHAIN           1..258
FT                   /note="Protein 2A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037103"
FT   CHAIN           259..606
FT                   /note="Movement protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037104"
FT   CHAIN           607..1110
FT                   /note="Coat protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037105"
SQ   SEQUENCE   1110 AA;  122787 MW;  5BF0E466838E42E9 CRC64;
     MGKFYYSNRR LACWAAGKNP HLGGSVEQWL AAINTDSSFR QTVKEDVQDN REQPTAIRMF
     SWKVGFGPID NPEKCDWHFV LTGERPAQPT RPVKADEVVV VPQLKKVVIP SPPPPPAVYF
     RAVGAFAPTR SGFIRATVER LSREREESRA AALFAELPLE YPQGAPLKLS LAMKFAMLKH
     TTWRKWYDTS DERLSEAHPG GPCLPPPPPI QNPPFFQERV REFCRMKSCA RAFALETSLG
     LNRAWVGLVD IPSTSVCCAD GRTTGGQTIA QEADPLQHRV STSVAPGRAQ WISERRQALR
     RREQANSLQG LAAQTDMTFE QARNAYLGAA DMIEQGLPLL PPLRSAYAPR GLWRGPSTRA
     NYTLDFRLNG IPTGTNTLEI LYNPVSEEEM EEYRDRGMSA VVIDALEIAI NPFGMPGNPT
     DLTVVATYGH ERDMTRAFIG SASTFLGNGL ARAIFFPGLQ YSQEEPRRES IIRLYVASTN
     ATVDTDSVLA AISVGTLRQH VGSMHYRTVA STVHQAQVQG TTLRATMMGN TVVVSPEGSL
     VTGTPEARVE IGGGSSIRMV GPLQWESVEE PGQTFSIRSR SRSVRIDRNV DLPQLEAEPR
     LSSTVRGLAG RGVVYIPKDC QANRYLGTLN IRDMISDFKG VQYEKWITAG LVMPTFKIVI
     RLPANAFTGL TWVMSFDAYN RITSRITTSA DPVYTLSVPH WLIHHKLGTF SCEIDYGELC
     GHAMWFKSTT FESPKLHFTC LTGNNKELAA DWQAVVELYA ELEEASSFLG KPTLVFDPGV
     FNGKFQFLTC PPIFFDLTAV TALKSAGLTL GQVPMVGTTK VYNLNSALVS CVLGMGGTIR
     GRVHICAPIF YSIVLWVVSE WNGTTMDWNE LFKYPGVYVE EDGSFEVKIR SPYHRTPARL
     LAGQSQRDMS SLNFYAIAGP IAPSGETARL PIVVQIDEIV RPDLALPSFE DDYFVWVDFS
     EFTLDKEELE IGSRFFDFTS STCRVIMGEN PFAAMIACHG LHSGVLDLKL QWSLNTDFGK
     SSGSVTVTKL VGDKATGLDG PSQVFAIQKL EGVTDLLIGN FAGANPNTHF SLYSRWMAIK
     LDQAKSIKVL RVLCKPRPGF SFYGRTSFPV