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P03599 (POL2_CPMVS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA2 polyprotein
Alternative name(s):
Genome polyprotein M
P2

Cleaved into the following 4 chains:

  1. Movement protein
    Short name=MP
  2. Large coat protein
    Short name=LCP
    Alternative name(s):
    Coat protein VP37
  3. Small coat protein, N-terminus part
    Short name=SCP
    Alternative name(s):
    Coat protein VP23
  4. Small coat protein, C-terminus part
OrganismCowpea mosaic virus (strain SB) (CPMV) [Reference proteome]
Taxonomic identifier928299 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesSecoviridaeComovirinaeComovirus
Virus hostCajanus cajan (Pigeon pea) (Cajanus indicus) [TaxID: 3821]
Crotalaria juncea (Sunn hemp) [TaxID: 3829]
Vigna unguiculata (Cowpea) [TaxID: 3917]

Protein attributes

Sequence length1046 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner. Ref.2 Ref.4 Ref.5 Ref.6

The cleavable C-terminus of small coat protein seems to be involved in the packaging of the virion RNAs. Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. Ref.2 Ref.4 Ref.5 Ref.6

Subcellular location

Movement protein: Host cell junctionhost plasmodesma. Note: Assembles in tubules that are embedded within modified plasmodesmata.

Large coat protein: Virion Potential.

Post-translational modification

Specific enzymatic cleavages by RNA1 encoded picornain 3C-like protease in vivo yield mature proteins By similarity. The C-terminal 24 amino acids of small coat protein are cleaved. Ref.2

Miscellaneous

The virus capsid is composed of 60 icosahedral units, each of which is composed of one copy each of the two coat proteins.

Sequence similarities

Belongs to the comoviridae genome polyprotein M family.

Caution

It is uncertain whether Met-1 or Met-118 is the initiator.

Mass spectrometry

Molecular mass is 21121.8 Da from positions 834 - 1022. Determined by ESI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Movement protein By similarity
PRO_0000037024
Chain460 – 833374Large coat protein By similarity
PRO_0000037025
Chain834 – 1022189Small coat protein, N-terminus part
PRO_0000037026
Chain1023 – 104624Small coat protein, C-terminus part
PRO_0000037027

Sites

Site459 – 4602Cleavage By similarity
Site833 – 8342Cleavage By similarity
Site1022 – 10232Cleavage

Experimental info

Mutagenesis2591V → A: Complete loss of GTP binding; when associated with A-260. Ref.6
Mutagenesis2601D → A: Complete loss of GTP binding; when associated with A-259. Ref.6

Secondary structure

............................................................................................... 1046
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03599 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 350EBECBF6558A1E

FASTA1,046116,218
        10         20         30         40         50         60 
MFSFTEAKSK ISLWTRSAAP LNNVYLSYSC RCGLGKRKLA GGCCSAPYIT CYDSADFRRV 

        70         80         90        100        110        120 
QYLYFCLTRY CCLYFFLLLL ADWFYKKSSI FFETEFSRGF RTWRKIVKLL YILPKFEMES 

       130        140        150        160        170        180 
IMSRGIPSGI LEEKAIQFKR AKEGNKPLKD EIPKPEDMYV SHTSKWNVLR KMSQKTVDLS 

       190        200        210        220        230        240 
KAAAGMGFIN KHMLTGNILA QPTTVLDIPV TKDKTLAMAS DFIRKENLKT SAIHIGAIEI 

       250        260        270        280        290        300 
IIQSFASPES DLMGGFLLVD SLHTDTANAI RSIFVAPMRG GRPVRVVTFP NTLAPVSCDL 

       310        320        330        340        350        360 
NNRFKLICSL PNCDIVQGSQ VAEVSVNVAG CATSIEKSHT PSQLYTEEFE KEGAVVVEYL 

       370        380        390        400        410        420 
GRQTYCAQPS NLPTEEKLRS LKFDFHVEQP SVLKLSNSCN AHFVKGESLK YSISGKEAEN 

       430        440        450        460        470        480 
HAVHATVVSR EGASAAPKQY DPILGRVLDP RNGNVAFPQM EQNLFALSLD DTSSVRGSLL 

       490        500        510        520        530        540 
DTKFAQTRVL LSKAMAGGDV LLDEYLYDVV NGQDFRATVA FLRTHVITGK IKVTATTNIS 

       550        560        570        580        590        600 
DNSGCCLMLA INSGVRGKYS TDVYTICSQD SMTWNPGCKK NFSFTFNPNP CGDSWSAEMI 

       610        620        630        640        650        660 
SRSRVRMTVI CVSGWTLSPT TDVIAKLDWS IVNEKCEPTI YHLADCQNWL PLNRWMGKLT 

       670        680        690        700        710        720 
FPQGVTSEVR RMPLSIGGGA GATQAFLANM PNSWISMWRY FRGELHFEVT KMSSPYIKAT 

       730        740        750        760        770        780 
VTFLIAFGNL SDAFGFYESF PHRIVQFAEV EEKCTLVFSQ QEFVTAWSTQ VNPRTTLEAD 

       790        800        810        820        830        840 
GCPYLYAIIH DSTTGTISGD FNLGVKLVGI KDFCGIGSNP GIDGSRLLGA IAQGPVCAEA 

       850        860        870        880        890        900 
SDVYSPCMIA STPPAPFSDV TAVTFDLING KITPVGDDNW NTHIYNPPIM NVLRTAAWKS 

       910        920        930        940        950        960 
GTIHVQLNVR GAGVKRADWD GQVFVYLRQS MNPESYDART FVISQPGSAM LNFSFDIIGP 

       970        980        990       1000       1010       1020 
NSGFEFAESP WANQTTWYLE CVATNPRQIQ QFEVNMRFDP NFRVAGNILM PPFPLSTETP 

      1030       1040 
PLLKFRFRDI ERSKRSVMVG HTATAA 

« Hide

References

[1]"Primary structure and gene organization of the middle-component RNA of cowpea mosaic virus."
van Wezenbeek P., Verver J., Harmsen J., Vos P., van Kammen A.
EMBO J. 2:941-946(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation."
Taylor K.M., Spall V.E., Butler P.J.G., Lomonossoff G.P.
Virology 255:129-137(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY, FUNCTION, CLEAVAGE OF SMALL COAT PROTEIN.
[3]"Glycosylation of the capsid proteins of cowpea mosaic virus: a reinvestigation shows the absence of sugar residues."
Altmann F., Lomonossoff G.P.
J. Gen. Virol. 81:1111-1114(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSENCE OF GLYCOSYLATION AT COAT PROTEINS.
[4]"Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing."
Canizares M.C., Taylor K.M., Lomonossoff G.P.
J. Gen. Virol. 85:3431-3435(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SMALL COAT PROTEIN C-TERMINUS AS SUPPRESSOR OF RNA SILENCING.
[5]"Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2-encoded suppressor of silencing."
Liu L., Grainger J., Canizares M.C., Angell S.M., Lomonossoff G.P.
Virology 323:37-48(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SMALL COAT PROTEIN C-TERMINUS AS SUPPRESSOR OF RNA SILENCING.
[6]"The movement protein of cowpea mosaic virus binds GTP and single-stranded nucleic acid in vitro."
Carvalho C.M., Pouwels J., van Lent J.W., Bisseling T., Goldbach R.W., Wellink J.
J. Virol. 78:1591-1594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF MOVEMENT PROTEIN, MUTAGENESIS OF VAL-259 AND ASP-260.
[7]"The refined crystal structure of cowpea mosaic virus at 2.8 A resolution."
Lin T., Chen Z., Usha R., Stauffacher C.V., Dai J.B., Schmidt T., Johnson J.E.
Virology 265:20-34(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 460-1022.
Strain: Bi1 mutant.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00729 Genomic RNA. Translation: CAA25314.1.
RefSeqNP_613285.1. NC_003550.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NY7X-ray3.001834-1022[»]
2460-828[»]
2BFUX-ray4.00L460-828[»]
S834-1022[»]
ProteinModelPortalP03599.
SMRP03599. Positions 460-828, 834-1022.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956626.

Family and domain databases

InterProIPR003181. Como_LCP.
IPR003182. RNA2_polyprotein.
[Graphical view]
PfamPF02247. Como_LCP. 1 hit.
PF02248. Como_SCP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03599.
PMAP-CutDBP03599.

Entry information

Entry namePOL2_CPMVS
AccessionPrimary (citable) accession number: P03599
Secondary accession number(s): Q84103
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references