P03304 (POLG_EMCV) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 122. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 13 chains:
|Organism||Encephalomyocarditis virus [Complete proteome]|
|Taxonomic identifier||12104 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Cardiovirus|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
|Sequence length||2290 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. Ref.4
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. Ref.4
Protein VP0: VP0 precursor is a component of immature procapsids By similarity. Ref.4
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.4
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.4
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.4
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. Cleaves host PABP1, this cleavage is important for viral replication. Ref.4
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.4
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity. Ref.4
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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.
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. Ref.3
Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
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.
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.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Belongs to the picornaviruses polyprotein family.
Contains 2 peptidase C3 domains.
Contains 1 RdRp catalytic domain.
Contains 1 SF3 helicase domain.
|This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]|
|Isoform Genome polyprotein (identifier: P03304-1) |
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.
|Note: Produced by conventional translation.|
|Isoform 2B* (identifier: P0DJX7-1) |
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.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 67||67||Leader protein||PRO_0000039780|
|Chain||68 – 391||324||Protein VP0 Potential||PRO_0000310967|
|Chain||68 – 136||69||Protein VP4 Potential||PRO_0000039781|
|Chain||137 – 391||255||Protein VP2 Potential||PRO_0000039782|
|Chain||392 – 622||231||Protein VP3 Potential||PRO_0000039783|
|Chain||623 – 899||277||Protein VP1 Potential||PRO_0000039784|
|Chain||900 – 1042||143||Protein 2A Potential||PRO_0000039785|
|Chain||1043 – 1192||150||Protein 2B Potential||PRO_0000039786|
|Chain||1193 – 1517||325||Protein 2C Potential||PRO_0000039787|
|Chain||1518 – 1605||88||Protein 3A Potential||PRO_0000039788|
|Chain||1606 – 1625||20||Protein 3B Potential||PRO_0000039789|
|Chain||1626 – 1830||205||Protease 3C Potential||PRO_0000039790|
|Chain||1831 – 2290||460||RNA-directed RNA polymerase 3D-POL Potential||PRO_0000039791|
|Topological domain||1 – 1562||1562||Cytoplasmic Potential|
|Intramembrane||1563 – 1581||19||Potential|
|Topological domain||1582 – 2290||709||Cytoplasmic Potential|
|Domain||1279 – 1445||167||SF3 helicase|
|Domain||2059 – 2177||119||RdRp catalytic|
|Zinc finger||10 – 22||13||Potential|
|Nucleotide binding||1311 – 1318||8||ATP Potential|
|Region||37 – 61||25||Acidic|
|Active site||1671||1||For protease 3C activity Potential|
|Active site||1703||1||For protease 3C activity Potential|
|Active site||1784||1||For protease 3C activity Potential|
|Site||136 – 137||2||Cleavage Potential|
|Site||391 – 392||2||Cleavage; by protease 3C Potential|
|Site||622 – 623||2||Cleavage; by protease 3C Potential|
|Site||899 – 900||2||Cleavage; by protease 3C Potential|
|Site||1042 – 1043||2||Cleavage; by ribosomal skip Potential|
|Site||1192 – 1193||2||Cleavage; by protease 3C Potential|
|Site||1517 – 1518||2||Cleavage; by protease 3C Potential|
|Site||1605 – 1606||2||Cleavage; by protease 3C Potential|
|Site||1625 – 1626||2||Cleavage; by protease 3C Potential|
|Site||1830 – 1831||2||Cleavage; by protease 3C Potential|
Amino acid modifications
|Modified residue||1608||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|Lipidation||68||1||N-myristoyl glycine; by host By similarity|
|Sequence conflict||1337||1||S → P in AAA43036. Ref.2|
|Sequence conflict||1397||1||F → L in AAA43036. Ref.2|
|Sequence conflict||1518||1||G → A in AAA43036. Ref.2|
|Sequence conflict||1537||1||Q → E in AAA43036. Ref.2|
|Sequence conflict||1557||1||N → S in AAA43036. Ref.2|
|Sequence conflict||1612||1||A → T in AAA43036. Ref.2|
|Sequence conflict||1755||1||L → V in AAA43036. Ref.2|
|Sequence conflict||1916||1||D → N in AAA43036. Ref.2|
|Sequence conflict||1987 – 1988||2||FL → IH in AAA43036. Ref.2|
|Sequence conflict||2008||1||V → I in AAA43036. Ref.2|
|Sequence conflict||2049||1||T → H in AAA43036. Ref.2|
|Sequence conflict||2194||1||T → K in AAA43036. Ref.2|
|||"The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region."|
Palmenberg A.C., Kirby E.M., Janda M.R., Drake N.L., Duke G.M., Potratz K.F., Collett M.S.
Nucleic Acids Res. 12:2969-2985(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Nucleotide sequence of the 3'-terminus of encephalomyocarditis virus RNA."|
Petrov N.A., Chizhikov V.E., Blinov V.M., Karginov V.A., Mikryukov N.N., Gutorov V.V., Grishaev M.P., Beklemishev A.B., Vassilenko S.K.
Bioorg. Khim. 10:274-279(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1337-2290.
|||"TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus."|
Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.
J. Gen. Virol. 90:536-545(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN TRIM22.
|||"Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication."|
Kobayashi M., Arias C., Garabedian A., Palmenberg A.C., Mohr I.
J. Virol. 86:10686-10694(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEASE 3C.
|X00463 Genomic RNA. Translation: CAA25152.1.|
M54935 Genomic RNA. Translation: AAA43036.1.
|PIR||GNNYE. A03906. |
3D structure databases
|SMR||P03304. Positions 1-32, 76-896. |
Protein-protein interaction databases
|IntAct||P03304. 1 interaction.|
Protocols and materials databases
Family and domain databases
|Gene3D||22.214.171.124. 1 hit. |
|InterPro||IPR015031. Capsid_VP4_Picornavir. |
|Pfam||PF00548. 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.
|PRINTS||PR00918. CALICVIRUSNS. |
|SUPFAM||SSF50494. SSF50494. 1 hit. |
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: P03304|
Secondary accession number(s): Q66764
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|