POL2_BBWV2
ID POL2_BBWV2 Reviewed; 1065 AA.
AC Q9Q2Q3; Q9Q2Q2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 23-FEB-2022, entry version 52.
DE RecName: Full=RNA2 polyprotein;
DE AltName: Full=119kDa protein;
DE AltName: Full=Genome polyprotein M;
DE Contains:
DE RecName: Full=VP53;
DE AltName: Full=53 kDa protein;
DE Contains:
DE RecName: Full=Movement protein;
DE Short=MP;
DE AltName: Full=37 kDa protein;
DE AltName: Full=VP37;
DE Contains:
DE RecName: Full=Large capsid protein;
DE Short=LCP;
DE AltName: Full=44 kDa protein;
DE Contains:
DE RecName: Full=Small capsid protein;
DE Short=SCP;
DE AltName: Full=22 kDa protein;
OS Broad bean wilt virus 2 (BBWV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Fabavirus.
OX NCBI_TaxID=76875;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=B935;
RA Qi Y., Zhou X., Xue C., Li D.;
RT "Nucleotide sequence of RNA2 and polyprotein processing sites of a Chinese
RT isolate of broad bean wilt virus 2.";
RL Prog. Nat. Sci. 10:680-686(2000).
RN [2]
RP RNA-BINDING, AND FUNCTION (MOVEMENT PROTEIN).
RX PubMed=12021864; DOI=10.1007/s00705-001-0782-2;
RA Qi Y.J., Zhou X.P., Huang X.Z., Li G.X.;
RT "In vivo accumulation of Broad bean wilt virus 2 VP37 protein and its
RT ability to bind single-stranded nucleic acid.";
RL Arch. Virol. 147:917-928(2002).
RN [3]
RP FUNCTION (MOVEMENT PROTEIN), INTERACTION WITH THE SMALL CAPSID PROTEIN
RP (MOVEMENT PROTEIN), INTERACTION WITH THE MOVEMENT PROTEIN (SMALL CAPSID
RP PROTEIN), SUBCELLULAR LOCATION (MOVEMENT PROTEIN), AND DOMAIN (MOVEMENT
RP PROTEIN).
RX PubMed=19463725; DOI=10.1016/j.virusres.2009.03.009;
RA Liu C., Meng C., Xie L., Hong J., Zhou X.;
RT "Cell-to-cell trafficking, subcellular distribution, and binding to coat
RT protein of Broad bean wilt virus 2 VP37 protein.";
RL Virus Res. 143:86-93(2009).
RN [4]
RP FUNCTION (MOVEMENT PROTEIN), AND SUBCELLULAR LOCATION (MOVEMENT PROTEIN).
RX PubMed=20832435; DOI=10.1016/j.virusres.2010.08.013;
RA Liu C., Ye L., Lang G., Zhang C., Hong J., Zhou X.;
RT "The VP37 protein of Broad bean wilt virus 2 induces tubule-like structures
RT in both plant and insect cells.";
RL Virus Res. 155:42-47(2011).
RN [5]
RP FUNCTION (MOVEMENT PROTEIN), FUNCTION (LARGE CAPSID PROTEIN), FUNCTION
RP (VP53), DOMAIN (VP53), RNA-BINDING (LARGE CAPSID PROTEIN), AND RNA-BINDING
RP (VP53).
RX PubMed=25173697; DOI=10.1016/j.virusres.2014.08.010;
RA Kong L., Wang Y., Yang X., Sunter G., Zhou X.;
RT "Broad bean wilt virus 2 encoded VP53, VP37 and large capsid protein
RT orchestrate suppression of RNA silencing in plant.";
RL Virus Res. 192:62-73(2014).
RN [6]
RP FUNCTION (MOVEMENT PROTEIN), AND SUBCELLULAR LOCATION (MOVEMENT PROTEIN).
RX PubMed=26903400; DOI=10.1038/srep21552;
RA Xie L., Shang W., Liu C., Zhang Q., Sunter G., Hong J., Zhou X.;
RT "Mutual association of Broad bean wilt virus 2 VP37-derived tubules and
RT plasmodesmata obtained from cytological observation.";
RL Sci. Rep. 6:21552-21552(2016).
CC -!- FUNCTION: [VP53]: Acts as suppressor of post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs (PubMed:25173697). Binds ssRNA
CC (PubMed:25173697). {ECO:0000269|PubMed:25173697}.
CC -!- FUNCTION: [Movement protein]: Transports the viral genome to
CC neighboring plant cells directly through plasmosdesmata, without any
CC budding (PubMed:19463725). The movement protein allows efficient cell
CC to cell propagation, by bypassing the host cell wall barrier
CC (PubMed:19463725). Acts by forming a tubular structure at the host
CC plasmodesmata, enlarging it enough to allow free passage of virion
CC capsids (PubMed:20832435, PubMed:26903400). Binds to GTP and to single-
CC stranded RNA and single-stranded DNA in a non-sequence-specific manner
CC (PubMed:12021864). Also acts as suppressor of post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs (PubMed:25173697).
CC {ECO:0000269|PubMed:12021864, ECO:0000269|PubMed:19463725,
CC ECO:0000269|PubMed:20832435, ECO:0000269|PubMed:25173697,
CC ECO:0000269|PubMed:26903400}.
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 (By
CC similarity). The large capsid protein interacts with the viral RNA (By
CC similarity). Also acts as suppressor of post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs (PubMed:25173697). Binds ssRNA
CC (PubMed:25173697). {ECO:0000250|UniProtKB:P03599,
CC ECO:0000269|PubMed:25173697}.
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 (By
CC similarity). The capsid is formed from 60 copies each of the large and
CC the small capsid protein. The small capsid protein forms the turrets at
CC the fivefold axes of the viral particle (By similarity).
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Small capsid protein]: Interacts with the large capsid
CC protein (By similarity). Interacts with the movement protein (via C-
CC terminus) (PubMed:19463725). {ECO:0000250|UniProtKB:P03599,
CC ECO:0000269|PubMed:19463725}.
CC -!- SUBUNIT: [Large capsid protein]: Interacts with the small capsid
CC protein (By similarity). Homomultimer; assembles as pentons (By
CC similarity). {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the small
CC capsid protein (PubMed:19463725). {ECO:0000269|PubMed:19463725}.
CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host endoplasmic reticulum
CC {ECO:0000269|PubMed:19463725}. Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:19463725, ECO:0000269|PubMed:20832435,
CC ECO:0000269|PubMed:26903400}. Note=Assembles in tubules that are
CC embedded within modified plasmodesmata. {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=RNA2 polyprotein; Synonyms=119kDa protein;
CC IsoId=Q9Q2Q3-1; Sequence=Displayed;
CC Name=RNA2 polyprotein 104kDa; Synonyms=104kDa protein;
CC IsoId=Q9Q2Q3-2; Sequence=VSP_059983;
CC -!- DOMAIN: [Movement protein]: The C-terminus is important for targeting
CC the movement protein to the plasmodesmata.
CC {ECO:0000269|PubMed:19463725}.
CC -!- DOMAIN: [VP53]: The N-terminus is involved in ssRNA-binding.
CC {ECO:0000269|PubMed:25173697}.
CC -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC like protease in vivo yield mature proteins.
CC {ECO:0000250|UniProtKB:P03599}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ132844; CAB63086.1; -; Genomic_RNA.
DR EMBL; AJ132844; CAB63085.1; -; Genomic_RNA.
DR SMR; Q9Q2Q3; -.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
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: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; DNA-binding; Host cell junction;
KW Host endoplasmic reticulum; RNA-binding; Suppressor of RNA silencing;
KW T=3 icosahedral capsid protein; Transport; Viral movement protein; Virion.
FT CHAIN 1..1065
FT /note="RNA2 polyprotein"
FT /id="PRO_0000445863"
FT CHAIN 1..466
FT /note="VP53"
FT /id="PRO_0000445864"
FT CHAIN 129..466
FT /note="Movement protein"
FT /id="PRO_0000445865"
FT CHAIN 467..868
FT /note="Large capsid protein"
FT /id="PRO_0000445866"
FT CHAIN 869..1065
FT /note="Small capsid protein"
FT /id="PRO_0000445867"
FT SITE 466..467
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 868..869
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform RNA2 polyprotein 104kDa)"
FT /id="VSP_059983"
SQ SEQUENCE 1065 AA; 119214 MW; C3B9CDF05AF74A7D CRC64;
MRPELVAVLD RYFSEIISCF FLGWLLNFLL VWFCSTKSTF LLWSVFLYIC YYILRIEFAY
IVAPFLKTIY TNSSQYHTVD WAYAYTALPK GLWEQITDYN YCYNFPPPRV EGFVSDFSPR
FTLKELEIMN EANITPVHTI PKDTLLKRAS DYKLAVESKK SILPRVQDLY EMDKWHNLRS
KLSKNAPSYV TTSEIAVGAM SGAGNTKLAI PVVEKYTEEV ADDRLPDRVR AKADQIMVAA
IELVADGFAS VNSDVTMAGA LYDKRHKTIA SSFKGAFASR ASGVPSHVIY FPMHRVPACD
DPNTTLELSM VSRDSDFDEG YTLANISART LYVRAKGPEK VTETRHLLKA KTEDVVKARQ
FASEAQVVFA TPRLFPEVNL DNYNLPGPSN AQQTEAITTD RGILFPKPKF KGNEVVLNYT
GSGKIRNVGS QRFETKKNAT GEQFVRSVDD LGCLSDEDGK DYRYGQGLME EDVLNVQTNN
FAIESATETM RLLFSGYASI PLNVIPGTKI TVAYLNELSK HSAVHTGLLN MLSKIPGSLK
VKINCQVAPT CGIGLAVSYV EGNESANLGS SLGRLLGIQH YKWNPAIEPY VEFVFKPFSC
ADWWNMHYLG SFKFAPVVVI QTLSKWLNAP KVDARISFAI YYEPTVVLPK QIATLEHAPA
FMFRKEVGTL AFKQGERVAY SFEVNLGKPQ TDGKEVTSTF ASSYCGLSQY MQSDVILDFT
LMSSPMIGGT FSIAYVAGAY IEKVGNMQIL DSLPHIDFTF SSGSKSTRSV RFPKEVFGVY
QALDRWDLDS ARGDDVSGNF VLYQRDAVSS ALEGELTFRI AARLSGDISF TGVSAGYPTT
ITRIGKGKTI GRSLDPEIRK PLRYMLGQAH ATPKDFSSVR FVMGHWKYRA GLYPGSKSDE
DIHPFSLKMR LDGSKSSENF EIIHSPFVRL LQNCAWMRGT LRFYVVARAS SDYMSYRRTS
QLTVSAHENS LSSNQFYSGV LTSPSGELSF SREVVGPVDG FASMGWNVRG SKKFYKIHVE
MGNVHEYDTV VLYGQFDSNV EFAGQRKGGH YLLEKETPIF KTIKY
