Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Leader protein: promotes host NUP62, NUP153, and NUP214 phosphorylation and induces cessation of active nucleocytoplasmic transport. Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells (By similarity).By similarity
Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. Cleaves host PABP1, this cleavage is important for viral replication.1 Publication
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function (By similarity).By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1671For protease 3C activitySequence analysis1
Active sitei1703For protease 3C activitySequence analysis1
Active sitei1784For protease 3C activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri10 – 22Sequence analysisAdd BLAST13
Nucleotide bindingi1311 – 1318ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B
Short name:
P3B
Alternative name(s):
H
VPg
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
E
Short name:
P3D-POL
OrganismiEncephalomyocarditis virus
Taxonomic identifieri12104 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008660 Componenti: Chromosome

Subcellular locationi

Protein 2B :
Protein 2C :
Protein 3A :
Protein 3B :
RNA-directed RNA polymerase 3D-POL :
Protein 2A :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1562CytoplasmicSequence analysisAdd BLAST1562
Intramembranei1563 – 1581Sequence analysisAdd BLAST19
Topological domaini1582 – 2290CytoplasmicSequence analysisAdd BLAST709

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000397801 – 67Leader proteinAdd BLAST67
ChainiPRO_000031096768 – 391Protein VP0Sequence analysisAdd BLAST324
ChainiPRO_000003978168 – 136Protein VP4Sequence analysisAdd BLAST69
ChainiPRO_0000039782137 – 391Protein VP2Sequence analysisAdd BLAST255
ChainiPRO_0000039783392 – 622Protein VP3Sequence analysisAdd BLAST231
ChainiPRO_0000039784623 – 899Protein VP1Sequence analysisAdd BLAST277
ChainiPRO_0000039785900 – 1042Protein 2ASequence analysisAdd BLAST143
ChainiPRO_00000397861043 – 1192Protein 2BSequence analysisAdd BLAST150
ChainiPRO_00000397871193 – 1517Protein 2CSequence analysisAdd BLAST325
ChainiPRO_00000397881518 – 1605Protein 3ASequence analysisAdd BLAST88
ChainiPRO_00000397891606 – 1625Protein 3BSequence analysisAdd BLAST20
ChainiPRO_00000397901626 – 1830Protease 3CSequence analysisAdd BLAST205
ChainiPRO_00000397911831 – 2290RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi68N-myristoyl glycine; by hostBy similarity1
Modified residuei1608O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei136 – 137CleavageSequence analysis2
Sitei391 – 392Cleavage; by protease 3CSequence analysis2
Sitei622 – 623Cleavage; by protease 3CSequence analysis2
Sitei899 – 900Cleavage; by protease 3CSequence analysis2
Sitei1042 – 1043Cleavage; by ribosomal skipSequence analysis2
Sitei1192 – 1193Cleavage; by protease 3CSequence analysis2
Sitei1517 – 1518Cleavage; by protease 3CSequence analysis2
Sitei1605 – 1606Cleavage; by protease 3CSequence analysis2
Sitei1625 – 1626Cleavage; by protease 3CSequence analysis2
Sitei1830 – 1831Cleavage; by protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Protease 3C interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication. Protein 2A interacts with host EIF4E (By similarity).By similarity

Protein-protein interaction databases

IntActiP03304. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliP03304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1279 – 1445SF3 helicasePROSITE-ProRule annotationAdd BLAST167
Domaini2059 – 2177RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 61AcidicAdd BLAST25

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 2 peptidase C3 domains.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri10 – 22Sequence analysisAdd BLAST13

Keywords - Domaini

Zinc-finger

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Isoform Genome polyprotein (identifier: P03304-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE
60 70 80 90 100
DDVFDPELDM EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI
110 120 130 140 150
DLSANAAGSD PPRLRSIFES LSGAVNAFSN MLPLLADQNT EEMENLSDRG
160 170 180 190 200
LKTLPAIRSQ TPSQQWAVLS VMVPFMMESI RHHVLTLLQK RFWRWKGTTP
210 220 230 240 250
SRLMIGHQHK SPLSTSAFPF LTSCPVKMVV SLVALRRHYL VKTGWRVQVQ
260 270 280 290 300
CNASQFHAGG LLVFMAPEYP TLDAFAMDNR WSKDNLPNGT RTQTNKKGPF
310 320 330 340 350
AMDHQNFWQW TLYPHQFLNL RTNTTVDLEV PYVNIAPTSS WTQHASWTLV
360 370 380 390 400
IAVVAPLTYS TGASTSLDIT ASIQPVRPVF NGLRHETLSR QSPIPVTIRE
410 420 430 440 450
HAGTWYSTLP DSTVPIYGKT PVAPSNYMVG EYKDFLEIAQ IPTFIGNKIP
460 470 480 490 500
NAVPYIEASN TAVKTQPLAT YQVTLSCSCL ANTFLAALSR NFAQYRGSLV
510 520 530 540 550
YTFVFTGTAM MKGKFLIAYT PPGAGKPTSR DQAMQATYAI WDLGLNSSYS
560 570 580 590 600
FTVPFISPTH FRMVGTDQVN ITNADGWVTV WQLTPLTYPP GCPTSAKILT
610 620 630 640 650
MVSAGKDFSL KMPISPAPWS PQGVENAEKG VTENTNATAD FVAQPVYLPE
660 670 680 690 700
NQTKVAFFYN RSSPIGAFTV KSGSLESGFA PFSNGTCPNS VILTPGPQFD
710 720 730 740 750
PAYDQLRPQR LTEIWGNGNE ETSKVFPLKS KQDYSFCLFS PFVYYKCDLE
760 770 780 790 800
VTLSPHTSGN HGLLVRWCPT GTPTKPTTQV LHEVSSLSEG RTPQVYSAGP
810 820 830 840 850
GISNQISFVV PYNSPLSVLS AVWYNGHKRF DNTGSLGIAP NSDFGTLFFA
860 870 880 890 900
GTKPDIKFTV YLRYKNKRVF CPRPTVFFPW PTSGDKIDMT PRAGVLMLES
910 920 930 940 950
PNALDISRTY PTLHVLIQFN HRGLEVRLFR HGHFWAETRA DVILRSKTKQ
960 970 980 990 1000
VSFLSNGNYP SMDSRAPWNP WKNTYQAVLR AEPCRVTMDI YYKRVRPFRL
1010 1020 1030 1040 1050
PLVQKEWPVR EENVFGLYRI FNAHYAGYFA DLLIHDIETN PGPFMFRPRK
1060 1070 1080 1090 1100
QVFQTQGAAV SSMAQTLLPN DLASKAMGSA FTALLDANED AQKAMKIIKT
1110 1120 1130 1140 1150
LSSLSDAWEN VKETLNNPEF WKQLLSRCVQ LIAGMTIAVM HPDPLTLLCL
1160 1170 1180 1190 1200
GTLTAAEITS QTSLCEEIAA KFKTIFITPP PRFPTISLFQ QQSPLKQVND
1210 1220 1230 1240 1250
IFSLAKNLDW AVKTVEKVVD WFGTWIVQEE KEQTLDQLLQ RFPEHAKRIS
1260 1270 1280 1290 1300
DLRNGMAAYV ECKESFDFFE KLYNQAVKEK RTGIAAVCEK FRQKHDHATA
1310 1320 1330 1340 1350
RCEPVVIVLR GDAGQGKSLS SQVIAQAVSK TIFGRQSVYS LPPDSDFFDG
1360 1370 1380 1390 1400
YENQFAAIMD DLGQNPDGSD FTTFCQMVST TNFLPNMASL ERKGTPFTSQ
1410 1420 1430 1440 1450
LVVATTNLPE FRPVTIAHYP AVERRITFDY SVSAGPVCSK TEAGYKVLDV
1460 1470 1480 1490 1500
ERAFRPTGEA PLPCFQNNCL FLEKAGLQFR DNRTKEIISL VDVIERAVAR
1510 1520 1530 1540 1550
IERKKKVLTT VQTLVAQGPV DEVSFHSVVQ QLKARQQATD EQLEELQEAF
1560 1570 1580 1590 1600
AKVQERNSVF SDWLKISAML CAATLALSQV VKMAKAVKQM VKPDLVRVQL
1610 1620 1630 1640 1650
DEQEQGPYNE TARVKPKTLQ LLDIQGPNPV MDFEKYVAKH VTAPIGFVYP
1660 1670 1680 1690 1700
TGVSTQTCLL VRGRTLVVNR HMAESDWTSI VVRGVTHARS TVKILAIAKA
1710 1720 1730 1740 1750
GKETDVSFIR LSSGPLFRDN TSKFVKAGDV LPTGAAPVTG IMNTDIPMMY
1760 1770 1780 1790 1800
TGTFLKAGVS VPVETGQTFN HCIHYKANTR KGWCGSALLA DLGGSKKILG
1810 1820 1830 1840 1850
IHSAGSMGIA AASIVSQEMI RAVVNAFEPQ GALERLPDGP RIHVPRKTAL
1860 1870 1880 1890 1900
RPTVARQVFQ PAYAPAVLSK FDPRTEADVD EVAFSKHTSN QESLPPVFRM
1910 1920 1930 1940 1950
VAKEYANRVF TLLGKDNGRL TVKQALEGLE GMDPMDRNTS PGLPYTALGM
1960 1970 1980 1990 2000
RRTDVVDWES ATLIPFAAER LRKMNEGDFS EVVYQTFLKD ELRPIEKVQA
2010 2020 2030 2040 2050
AKTRIVDVPP FEHCILGRQL LGKFASKFQT QPGLELGSAI GCDPDVHWTA
2060 2070 2080 2090 2100
FGVAMQGFER VYDVDYSNFD STHSVAMFRL LAEEFFTPEN GFDPLTREYL
2110 2120 2130 2140 2150
ESLAISTHAF EEKRFLITGG LPSGCAATSM LNTIMNNIII RAGLYLTYKN
2160 2170 2180 2190 2200
FEFDDVKVLS YGDDLLVATN YQLDFDKVRA SLAKTGYKIT PANTTSTFPL
2210 2220 2230 2240 2250
NSTLEDVVFL KRKFKKEGPL YRPVMNREAL EAMLSYYRPG TLSEKLTSIT
2260 2270 2280 2290
MLAVHSGKQE YDRLFAPFRE VGVVVPSFES VEYRWRSLFW
Note: Produced by conventional translation.
Length:2,290
Mass (Da):255,758
Last modified:July 21, 1986 - v1
Checksum:i26BC81BB7CF68CB5
GO
Isoform 2B* (identifier: P0DJX7-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DJX7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.
Length:128
Mass (Da):14,449
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1337S → P in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1397F → L in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1518G → A in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1537Q → E in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1557N → S in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1612A → T in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1755L → V in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1916D → N in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti1987 – 1988FL → IH in AAA43036 (PubMed:6091680).Curated2
Sequence conflicti2008V → I in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti2049T → H in AAA43036 (PubMed:6091680).Curated1
Sequence conflicti2194T → K in AAA43036 (PubMed:6091680).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00463 Genomic RNA. Translation: CAA25152.1.
M54935 Genomic RNA. Translation: AAA43036.1.
PIRiA03906. GNNYE.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00463 Genomic RNA. Translation: CAA25152.1.
M54935 Genomic RNA. Translation: AAA43036.1.
PIRiA03906. GNNYE.

3D structure databases

ProteinModelPortaliP03304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03304. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_EMCV
AccessioniPrimary (citable) accession number: P03304
Secondary accession number(s): Q66764
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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.