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Protein

RNA2 polyprotein

Gene
N/A
Organism
Cowpea mosaic virus (strain SB) (CPMV)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA 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]
Proteomesi
  • UP000008589 Componenti: Genome

Subcellular locationi

Movement protein :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell junction, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi259V → A: Complete loss of GTP binding; when associated with A-260. 1 Publication1
Mutagenesisi260D → A: Complete loss of GTP binding; when associated with A-259. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000370241 – 459Movement proteinBy similarityAdd BLAST459
ChainiPRO_0000037025460 – 833Large coat proteinBy similarityAdd BLAST374
ChainiPRO_0000037026834 – 1022Small coat protein, N-terminus partAdd BLAST189
ChainiPRO_00000370271023 – 1046Small coat protein, C-terminus partAdd BLAST24

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei459 – 460CleavageBy similarity2
Sitei833 – 834CleavageBy similarity2
Sitei1022 – 1023Cleavage2

Proteomic databases

PRIDEiP03599.

Miscellaneous databases

PMAP-CutDBP03599.

Structurei

Secondary structure

11046
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi465 – 467Combined sources3
Helixi468 – 470Combined sources3
Turni479 – 481Combined sources3
Beta strandi482 – 491Combined sources10
Beta strandi499 – 505Combined sources7
Helixi506 – 510Combined sources5
Helixi518 – 522Combined sources5
Beta strandi525 – 527Combined sources3
Beta strandi529 – 536Combined sources8
Beta strandi546 – 555Combined sources10
Helixi563 – 566Combined sources4
Beta strandi569 – 574Combined sources6
Turni576 – 578Combined sources3
Beta strandi579 – 586Combined sources8
Helixi597 – 602Combined sources6
Beta strandi606 – 613Combined sources8
Beta strandi623 – 635Combined sources13
Beta strandi645 – 661Combined sources17
Beta strandi663 – 665Combined sources3
Beta strandi669 – 674Combined sources6
Beta strandi680 – 682Combined sources3
Beta strandi685 – 687Combined sources3
Helixi690 – 695Combined sources6
Beta strandi698 – 711Combined sources14
Beta strandi721 – 726Combined sources6
Helixi736 – 739Combined sources4
Beta strandi742 – 745Combined sources4
Beta strandi753 – 758Combined sources6
Helixi760 – 762Combined sources3
Beta strandi767 – 770Combined sources4
Turni777 – 779Combined sources3
Beta strandi784 – 791Combined sources8
Beta strandi796 – 798Combined sources3
Beta strandi801 – 818Combined sources18
Beta strandi846 – 851Combined sources6
Beta strandi861 – 866Combined sources6
Turni867 – 869Combined sources3
Beta strandi872 – 877Combined sources6
Beta strandi881 – 884Combined sources4
Helixi888 – 895Combined sources8
Beta strandi896 – 911Combined sources16
Helixi916 – 918Combined sources3
Beta strandi923 – 929Combined sources7
Beta strandi938 – 943Combined sources6
Beta strandi949 – 957Combined sources9
Beta strandi960 – 963Combined sources4
Turni970 – 973Combined sources4
Beta strandi978 – 984Combined sources7
Turni986 – 988Combined sources3
Beta strandi989 – 998Combined sources10
Beta strandi1003 – 1009Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NY7X-ray3.001834-1022[»]
2460-828[»]
2BFUX-ray4.00L460-828[»]
S834-1022[»]
5A32electron microscopy3.44A834-1022[»]
B460-828[»]
5A33electron microscopy3.04A834-1046[»]
B460-828[»]
5FMOX-ray2.30L460-833[»]
S834-1046[»]
ProteinModelPortaliP03599.
SMRiP03599.
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:
EMBLi
GenBanki
DDBJi
Links Updated
X00729 Genomic RNA. Translation: CAA25314.1.
RefSeqiNP_613285.1. NC_003550.1.

Genome annotation databases

GeneIDi956626.
KEGGivg:956626.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00729 Genomic RNA. Translation: CAA25314.1.
RefSeqiNP_613285.1. NC_003550.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NY7X-ray3.001834-1022[»]
2460-828[»]
2BFUX-ray4.00L460-828[»]
S834-1022[»]
5A32electron microscopy3.44A834-1022[»]
B460-828[»]
5A33electron microscopy3.04A834-1046[»]
B460-828[»]
5FMOX-ray2.30L460-833[»]
S834-1046[»]
ProteinModelPortaliP03599.
SMRiP03599.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP03599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956626.
KEGGivg:956626.

Miscellaneous databases

EvolutionaryTraceiP03599.
PMAP-CutDBP03599.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.