POL2_GFLV
ID POL2_GFLV Reviewed; 1109 AA.
AC P18474; Q83857;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 113.
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 (GFLV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=12274;
OH NCBI_TaxID=103352; Vitis rupestris.
OH NCBI_TaxID=29760; Vitis vinifera (Grape).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 606-632, AND
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=F13;
RX PubMed=2374004; DOI=10.1099/0022-1317-71-7-1433;
RA Serghini M.A., Fuchs M., Pinck M., Reinbolt J., Walter B., Pinck L.;
RT "RNA2 of grapevine fanleaf virus: sequence analysis and coat protein
RT cistron location.";
RL J. Gen. Virol. 71:1433-1441(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 258-272, AND
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=F13;
RX PubMed=8376967; DOI=10.1099/0022-1317-74-9-1919;
RA Margis R., Ritzenthaler C., Reinbolt J., Pinck M., Pinck L.;
RT "Genome organization of grapevine fanleaf nepovirus RNA2 deduced from the
RT 122K polyprotein P2 in vitro cleavage products.";
RL J. Gen. Virol. 74:1919-1926(1993).
RN [3]
RP FUNCTION OF PROTEIN 2A, AND SUBCELLULAR LOCATION OF PROTEIN 2A.
RX PubMed=10544127; DOI=10.1006/viro.1999.9927;
RA Gaire F., Schmitt C., Stussi-Garaud C., Pinck L., Ritzenthaler C.;
RT "Protein 2A of grapevine fanleaf nepovirus is implicated in RNA2
RT replication and colocalizes to the replication site.";
RL Virology 264:25-36(1999).
RN [4]
RP FUNCTION OF MOVEMENT PROTEIN, AND SUBCELLULAR LOCATION OF MOVEMENT PROTEIN.
RX PubMed=12953111; DOI=10.1105/tpc.013896;
RA Laporte C., Vetter G., Loudes A.-M., Robinson D.G., Hillmer S.,
RA Stussi-Garaud C., Ritzenthaler C.;
RT "Involvement of the secretory pathway and the cytoskeleton in intracellular
RT targeting and tubule assembly of Grapevine fanleaf virus movement protein
RT in tobacco BY-2 cells.";
RL Plant Cell 15:2058-2075(2003).
CC -!- FUNCTION: [Protein 2A]: Implicated in RNA2 replication. Could also be
CC required for nematode transmission of the virus.
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.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:10544127, ECO:0000269|PubMed:12953111}.
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:0000269|PubMed:2374004,
CC ECO:0000269|PubMed:8376967}.
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; X16907; CAA34779.1; -; Genomic_RNA.
DR EMBL; X16907; CAA34780.1; -; Genomic_RNA.
DR RefSeq; NP_619706.1; NC_003623.1.
DR RefSeq; NP_619707.1; NC_003623.1.
DR PDB; 2Y26; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=606-1109.
DR PDB; 4V5T; X-ray; 3.00 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ/CK/CL/CM/CN/CO/CP/CQ/CR/CS/CT=606-1109.
DR PDB; 4V5W; X-ray; 3.70 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ/CK/CL/CM/CN/CO/CP/CQ/CR/CS/CT=606-1109.
DR PDB; 5FOJ; EM; 2.80 A; B=606-1109.
DR PDBsum; 2Y26; -.
DR PDBsum; 4V5T; -.
DR PDBsum; 4V5W; -.
DR PDBsum; 5FOJ; -.
DR SMR; P18474; -.
DR PRIDE; P18474; -.
DR ABCD; P18474; 1 sequenced antibody.
DR GeneID; 1494094; -.
DR KEGG; vg:1494094; -.
DR Proteomes; UP000009160; Genome.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing;
KW Host cell junction; Host cytoplasm; Host nucleus; Transport;
KW Viral movement protein; Virion.
FT CHAIN 1..257
FT /note="Protein 2A"
FT /id="PRO_0000037100"
FT CHAIN 258..605
FT /note="Movement protein"
FT /id="PRO_0000037101"
FT CHAIN 606..1109
FT /note="Coat protein"
FT /id="PRO_0000037102"
FT STRAND 607..615
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 630..637
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 640..648
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 654..660
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 670..676
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 682..685
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 696..703
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 708..714
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:5FOJ"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 751..758
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 799..806
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 818..822
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 823..828
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 831..844
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 851..862
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 867..870
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 880..887
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 893..898
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 908..920
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 929..943
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 953..959
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 963..965
FT /evidence="ECO:0007829|PDB:5FOJ"
FT STRAND 966..971
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 980..986
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 990..996
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 998..1015
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 1017..1019
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1023..1031
FT /evidence="ECO:0007829|PDB:2Y26"
FT TURN 1033..1035
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1042..1045
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 1046..1048
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1050..1057
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1060..1062
FT /evidence="ECO:0007829|PDB:5FOJ"
FT STRAND 1064..1067
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1074..1082
FT /evidence="ECO:0007829|PDB:2Y26"
FT HELIX 1083..1085
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1086..1095
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1100..1104
FT /evidence="ECO:0007829|PDB:2Y26"
FT STRAND 1106..1109
FT /evidence="ECO:0007829|PDB:2Y26"
SQ SEQUENCE 1109 AA; 122707 MW; 2A2A639B32CA34AE CRC64;
MGKFYYSNRR LACWAAGKNP HLGGSVEQWL AAINTDPSFR QTVKEDVQEN REQPTAVRMF
SWKVGSGPID NPEKCDWHFV LTGERPAPSR PVKADEVVVV PQPKKVVIPT PPPPPAPYFR
AVGAFAPTRS EFVRAIVERL TRLREESRAA ALFAELPLEY PQGAPLKLSL AAKFAMLKHT
TWRKWYDTSD ERLLEAHPGG PCLPPPPPIQ NPPSFQERVR EFCRMKSCTK AFALETSLGL
NKAWVGLVDI PSTSVCCADG KTTGGQTIAQ EADPLQHRIS TSVAPGRAQW ISERRQALRR
REQANSFEGL AAQTDMTFEQ ARNAYLGAAD MIEQGLPLLP PLRSAYAPRG LWRGPSTRAN
YTLDFRLNGI PTGTNTLEIL YNPVSEEEME EYRDRGMSAV VIDALEIAIN PFGMPGNPTD
LTVVATYGHE RDMTRAFIGS ASTFLGNGLA RAIFFPGLQY SQEEPRRESI IRLYVASTNA
TVDTDSVLAA ISVGTLRQHV GSMHYRTVAS TVHQAQVQGT TLRATMMGNT VVVSPEGSLV
TGTPEARVEI GGGSSIRMVG PLQWESVEEP GQTFSIRSRS RSVRIDRNVD LPQLEAEPRL
SSTVRGLAGR GVIYIPKDCQ ANRYLGTLNI RDMISDFKGV QYEKWITAGL VMPTFKIVIR
LPANAFTGLT WVMSFDAYNR ITSRITASAD PVYTLSVPHW LIHHKLGTFS CEIDYGELCG
HAMWFKSTTF ESPRLHFTCL TGNNKELAAD WQAVVELYAE LEEATSFLGK PTLVFDPGVF
NGKFQFLTCP PIFFDLTAVT ALRSAGLTLG QVPMVGTTKV YNLNSTLVSC VLGMGGTVRG
RVHICAPIFY SIVLWVVSEW NGTTMDWNEL FKYPGVYVEE DGSFEVKIRS PYHRTPARLL
AGQSQRDMSS LNFYAIAGPI APSGETAQLP IVVQIDEIVR PDLSLPSFED DYFVWVDFSE
FTLDKEEIEI GSRFFDFTSN TCRVSMGENP FAAMIACHGL HSGVLDLKLQ WSLNTEFGKS
SGSVTITKLV GDKAMGLDGP SHVFAIQKLE GTTELLVGNF AGANPNTRFS LYSRWMAIKL
DQAKSIKVLR VLCKPRPGFS FYGRTSFPV
