POL2_RCMV
ID POL2_RCMV Reviewed; 996 AA.
AC P13561;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 02-JUN-2021, entry version 93.
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 AltName: Full=43 kDa protein;
DE Contains:
DE RecName: Full=Large capsid protein;
DE Short=LCP;
DE AltName: Full=Coat protein VP40;
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 VP22;
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 Red clover mottle virus (RCMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=12262;
OH NCBI_TaxID=57577; Trifolium pratense (Red clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], ALTERNATIVE INITIATION, AND PROTEOLYTIC
RP CLEAVAGE (RNA2 POLYPROTEIN).
RC STRAIN=S;
RA Shanks M., Stanley J., Lomonossoff G.P.;
RT "The primary structure of red clover mottle virus middle component RNA.";
RL Virology 155:697-706(1986).
RN [2]
RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN), AND IDENTIFICATION (MOVEMENT
RP PROTEIN).
RC STRAIN=S;
RX PubMed=2596020; DOI=10.1016/0042-6822(89)90552-7;
RA Shanks M., Tomenius K., Clapham D., Huskisson N.S., Barker P.J.,
RA Wilson I.G., Maule A.J., Lomonossoff G.P.;
RT "Identification and subcellular localization of a putative cell-to-cell
RT transport protein from red clover mottle virus.";
RL Virology 173:400-407(1989).
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 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. The
CC capsid is formed from 60 copies each of the large and the mature small
CC capsid protein. The large capsid protein interacts with the viral RNA.
CC {ECO:0000250|UniProtKB:P03599}.
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 mature small
CC capsid protein. The mature small capsid protein forms the turrets at
CC the fivefold axes of the viral particle.
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Mature 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:0000269|PubMed:2596020}. Note=Assembles in tubules
CC that are embedded within modified plasmodesmata.
CC {ECO:0000269|PubMed:2596020}.
CC -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBCELLULAR LOCATION: [Mature 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, 109 kDa protein;
CC IsoId=P13561-1; Sequence=Displayed;
CC Name=2; Synonyms=101 kDa protein;
CC IsoId=P13561-2; Sequence=VSP_059981;
CC -!- DOMAIN: [Large capsid protein]: Contains a beta-sheet structure called
CC beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}.
CC -!- DOMAIN: [Mature small capsid protein]: Contains a beta-sheet structure
CC called 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-70 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M14913; AAA47230.1; -; Genomic_RNA.
DR RefSeq; NP_620464.1; NC_003738.1. [P13561-1]
DR SMR; P13561; -.
DR PRIDE; P13561; -.
DR GeneID; 1502335; -.
DR KEGG; vg:1502335; -.
DR Proteomes; UP000006361; Genome.
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; DNA-binding; GTP-binding;
KW Host cell junction; Nucleotide-binding; RNA-binding;
KW Suppressor of RNA silencing; T=3 icosahedral capsid protein; Transport;
KW Viral movement protein; Virion.
FT CHAIN 1..996
FT /note="RNA2 polyprotein"
FT /id="PRO_0000445850"
FT CHAIN 1..406
FT /note="VP58"
FT /id="PRO_0000445851"
FT CHAIN 70..406
FT /note="Movement protein"
FT /id="PRO_0000037034"
FT CHAIN 407..782
FT /note="Large capsid protein"
FT /id="PRO_0000037035"
FT CHAIN 783..996
FT /note="Small capsid protein precursor"
FT /id="PRO_0000037036"
FT CHAIN 783..972
FT /note="Mature small capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT /id="PRO_0000445852"
FT CHAIN 973..994
FT /note="Small capsid protein C-terminus part"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT /id="PRO_0000445853"
FT REGION 363..369
FT /note="Involved in tubule formation by the movement
FT protein"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT REGION 368..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 406..407
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 423
FT /note="Interaction with the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 782..783
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 972..973
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /id="VSP_059981"
SQ SEQUENCE 996 AA; 109469 MW; CCA87D5C129B71FF CRC64;
MLGISNLCRY YQGQRRVCAN KFYQKYVNHS DLYFFDLWEI SANNLWIKLA FVLLLCLFEI
ISGLEYLGKM AQEILKQGIP ANVLQEKANL FKKASANNKI KDEMPNALSL YQNHSFFQKL
KHLADKKNLD ITSLPGGREV EYKHLDAGHL LADTNVVIDV PLVPQLAART PTDYNFGTSR
DKSATALHVG AIEVVIQSYA SSECDLMAGM MLVDTFHSRP ENAIRSVYIV PIRGGMFMRA
LCFPNTLVPM DSDINNRFKV VFSLPNNDFP QGSKLGHVSI NMAGCTTSLS KTYVPSPLLT
EELGREAATV IQYLGRDTYA MQTSNVPTSD EISRMVFNFH MEGKLSMHKT GSLSSILSKS
KSLRYTIGGS KPKNKLADKA HNEEAETSDS KGIIDPKDGN VFANPQTDTD LFKLSLDDTS
SPKGSLLDTR FAQKKVLIPK AMAGGADLLS SNLYDVLSGS SFRASLALAR THVVEGKIRC
ICTINLPENT GCCLAITVNS SNRGQFSTDI YTTGSQDRIL WNPACSKNCD FSFNPNPCGT
AWSLEFLRRT KFHLSVTCVS GWSAQPQTDI AMTMDWYVSN KPCVPCIYNV GTPGQNVWVN
RWMGKLSFPQ GSQNQLKQMP LAIGGGAGAK NSILMNMTNA FLSLWRYFHG DLVFEVQKMS
SPFIKSTVTF FIGFGGLPFS ENLEDFPNKL IQFGEVQERV EITFTRKEFL TAWSTQVDPA
GPVAGDGCPY LCAMVHDSTA STITGDFNLG VTLLRIENFV GIGRNPGIQG ARLLGSMQAE
AQGGVVRTTD GVYSTCFRVR TPLALKDSGS FTCDLIGGGI TTDSNTGWNL TALNTPVANL
LRTAAWKRGT IHVQVAMFGS TVKRSDWTST VQLFLRQSMN TSSYDARVWV ISKPGAAILE
FSFDVEGPNN GFEMWEANWA SQTSWFLEFL ISNVTQNTLF EVSMKLDSNF CVAGTTLMPP
FSVTASPDSR PLLGVKTSTP AKKYVGGSLQ AGPSPD
