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P03599

- POL2_CPMVS

UniProt

P03599 - POL2_CPMVS

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Protein

RNA2 polyprotein

Gene
N/A
Organism
Cowpea mosaic virus (strain SB) (CPMV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei459 – 4602CleavageBy similarity
Sitei833 – 8342CleavageBy similarity
Sitei1022 – 10232Cleavage

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. GTP binding Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW
  4. structural molecule activity Source: InterPro

GO - Biological processi

  1. transport of virus in host, cell to cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Suppressor of RNA silencing, Viral movement protein

Keywords - Biological processi

Transport

Keywords - Ligandi

DNA-binding, GTP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA2 polyprotein
Alternative name(s):
Genome polyprotein M
P2
Cleaved into the following 4 chains:
Movement protein
Short name:
MP
Large coat protein
Short name:
LCP
Alternative name(s):
Coat protein VP37
Alternative name(s):
Coat protein VP23
OrganismiCowpea mosaic virus (strain SB) (CPMV)
Taxonomic identifieri928299 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesSecoviridaeComovirinaeComovirus
Virus hostiCajanus cajan (Pigeon pea) (Cajanus indicus) [TaxID: 3821]
Crotalaria juncea (Sunn hemp) [TaxID: 3829]
Vigna unguiculata (Cowpea) [TaxID: 3917]
ProteomesiUP000008589: Genome

Subcellular locationi

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

GO - Cellular componenti

  1. host cell plasmodesma Source: InterPro
  2. viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell junction, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi259 – 2591V → A: Complete loss of GTP binding; when associated with A-260. 1 Publication
Mutagenesisi260 – 2601D → A: Complete loss of GTP binding; when associated with A-259. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Movement proteinBy similarityPRO_0000037024Add
BLAST
Chaini460 – 833374Large coat proteinBy similarityPRO_0000037025Add
BLAST
Chaini834 – 1022189Small coat protein, N-terminus partPRO_0000037026Add
BLAST
Chaini1023 – 104624Small coat protein, C-terminus partPRO_0000037027Add
BLAST

Post-translational modificationi

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.By similarity1 Publication

Miscellaneous databases

PMAP-CutDBP03599.

Structurei

Secondary structure

1
1046
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi464 – 4663
Helixi468 – 4703
Turni479 – 4824
Beta strandi483 – 4919
Beta strandi500 – 5056
Helixi506 – 5105
Helixi518 – 5236
Beta strandi525 – 5273
Beta strandi529 – 5368
Beta strandi546 – 55510
Helixi563 – 5664
Beta strandi569 – 5746
Turni576 – 5783
Beta strandi580 – 5867
Helixi597 – 6026
Beta strandi606 – 6138
Beta strandi623 – 63412
Beta strandi645 – 66117
Beta strandi663 – 6664
Beta strandi669 – 6746
Beta strandi680 – 6823
Beta strandi685 – 6873
Helixi690 – 6956
Beta strandi698 – 71114
Beta strandi721 – 7277
Helixi737 – 7393
Beta strandi742 – 7454
Beta strandi753 – 7586
Helixi760 – 7623
Beta strandi767 – 7693
Helixi777 – 7793
Beta strandi782 – 79110
Beta strandi801 – 81818
Beta strandi845 – 8517
Beta strandi861 – 8666
Turni867 – 8704
Beta strandi871 – 8744
Beta strandi881 – 8844
Helixi888 – 8958
Beta strandi896 – 91116
Helixi916 – 9183
Beta strandi923 – 9297
Beta strandi938 – 9436
Beta strandi949 – 9579
Turni960 – 9623
Turni970 – 9734
Beta strandi978 – 9847
Turni986 – 9883
Beta strandi989 – 99810
Beta strandi1003 – 10097

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NY7X-ray3.001834-1022[»]
2460-828[»]
2BFUX-ray4.00L460-828[»]
S834-1022[»]
ProteinModelPortaliP03599.
SMRiP03599. Positions 460-828, 834-1022.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03599.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.20. 2 hits.
InterProiIPR003181. Como_LCP.
IPR003182. RNA2_polyprotein.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF02247. Como_LCP. 1 hit.
PF02248. Como_SCP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03599-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSFTEAKSK ISLWTRSAAP LNNVYLSYSC RCGLGKRKLA GGCCSAPYIT
60 70 80 90 100
CYDSADFRRV QYLYFCLTRY CCLYFFLLLL ADWFYKKSSI FFETEFSRGF
110 120 130 140 150
RTWRKIVKLL YILPKFEMES IMSRGIPSGI LEEKAIQFKR AKEGNKPLKD
160 170 180 190 200
EIPKPEDMYV SHTSKWNVLR KMSQKTVDLS KAAAGMGFIN KHMLTGNILA
210 220 230 240 250
QPTTVLDIPV TKDKTLAMAS DFIRKENLKT SAIHIGAIEI IIQSFASPES
260 270 280 290 300
DLMGGFLLVD SLHTDTANAI RSIFVAPMRG GRPVRVVTFP NTLAPVSCDL
310 320 330 340 350
NNRFKLICSL PNCDIVQGSQ VAEVSVNVAG CATSIEKSHT PSQLYTEEFE
360 370 380 390 400
KEGAVVVEYL GRQTYCAQPS NLPTEEKLRS LKFDFHVEQP SVLKLSNSCN
410 420 430 440 450
AHFVKGESLK YSISGKEAEN HAVHATVVSR EGASAAPKQY DPILGRVLDP
460 470 480 490 500
RNGNVAFPQM EQNLFALSLD DTSSVRGSLL DTKFAQTRVL LSKAMAGGDV
510 520 530 540 550
LLDEYLYDVV NGQDFRATVA FLRTHVITGK IKVTATTNIS DNSGCCLMLA
560 570 580 590 600
INSGVRGKYS TDVYTICSQD SMTWNPGCKK NFSFTFNPNP CGDSWSAEMI
610 620 630 640 650
SRSRVRMTVI CVSGWTLSPT TDVIAKLDWS IVNEKCEPTI YHLADCQNWL
660 670 680 690 700
PLNRWMGKLT FPQGVTSEVR RMPLSIGGGA GATQAFLANM PNSWISMWRY
710 720 730 740 750
FRGELHFEVT KMSSPYIKAT VTFLIAFGNL SDAFGFYESF PHRIVQFAEV
760 770 780 790 800
EEKCTLVFSQ QEFVTAWSTQ VNPRTTLEAD GCPYLYAIIH DSTTGTISGD
810 820 830 840 850
FNLGVKLVGI KDFCGIGSNP GIDGSRLLGA IAQGPVCAEA SDVYSPCMIA
860 870 880 890 900
STPPAPFSDV TAVTFDLING KITPVGDDNW NTHIYNPPIM NVLRTAAWKS
910 920 930 940 950
GTIHVQLNVR GAGVKRADWD GQVFVYLRQS MNPESYDART FVISQPGSAM
960 970 980 990 1000
LNFSFDIIGP NSGFEFAESP WANQTTWYLE CVATNPRQIQ QFEVNMRFDP
1010 1020 1030 1040
NFRVAGNILM PPFPLSTETP PLLKFRFRDI ERSKRSVMVG HTATAA
Length:1,046
Mass (Da):116,218
Last modified:July 21, 1986 - v1
Checksum:i350EBECBF6558A1E
GO

Mass spectrometryi

Molecular mass is 21121.8 Da from positions 834 - 1022. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00729 Genomic RNA. Translation: CAA25314.1.
RefSeqiNP_613285.1. NC_003550.1.

Genome annotation databases

GeneIDi956626.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00729 Genomic RNA. Translation: CAA25314.1 .
RefSeqi NP_613285.1. NC_003550.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NY7 X-ray 3.00 1 834-1022 [» ]
2 460-828 [» ]
2BFU X-ray 4.00 L 460-828 [» ]
S 834-1022 [» ]
ProteinModelPortali P03599.
SMRi P03599. Positions 460-828, 834-1022.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956626.

Miscellaneous databases

EvolutionaryTracei P03599.
PMAP-CutDB P03599.

Family and domain databases

Gene3Di 2.60.120.20. 2 hits.
InterProi IPR003181. Como_LCP.
IPR003182. RNA2_polyprotein.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF02247. Como_LCP. 1 hit.
PF02248. Como_SCP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPOL2_CPMVS
AccessioniPrimary (citable) accession number: P03599
Secondary accession number(s): Q84103
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3