P12296 · POLG_ENMGO
- ProteinGenome polyprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2293 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Leader protein
Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity).
Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
Capsid protein VP1
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
Capsid protein VP2
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
Capsid protein VP3
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
Capsid protein VP4
Lies on the inner surface of the capsid shell (PubMed:2156078, PubMed:3026048).
After binding to the host receptor, the capsid undergoes conformational changes (By similarity).
Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).
After genome has been released, the channel shrinks (By similarity).
After binding to the host receptor, the capsid undergoes conformational changes (By similarity).
Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).
After genome has been released, the channel shrinks (By similarity).
Capsid protein VP0
VP0 precursor is a component of immature procapsids.
Protein 2A
Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (PubMed:12921995).
Nuclear localization is required for this function (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
Inhibits the phosphorylation of the leader protein (By similarity).
Binds to the RNA stem-loop essential for the ribosomal frameshift event and trans-activates the production of protein 2B* (PubMed:28593994, PubMed:34887415).
Nuclear localization is required for this function (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
Inhibits the phosphorylation of the leader protein (By similarity).
Binds to the RNA stem-loop essential for the ribosomal frameshift event and trans-activates the production of protein 2B* (PubMed:28593994, PubMed:34887415).
Protein 2B
Affects membrane integrity and causes an increase in membrane permeability.
Protein 2C
Associates with and induces structural rearrangements of intracellular membranes (By similarity).
It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity).
It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity).
Protein 3A
Serves as membrane anchor via its hydrophobic domain.
VPg
Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.
Protease 3C
Cysteine protease that generates mature viral proteins from the precursor polyprotein (PubMed:8972564).
In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).
Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).
In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).
Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).
RNA-directed RNA polymerase
Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (Probable). Performs VPg uridylylation (PubMed:24600002).
Catalytic activity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Activity regulation
RNA-dependent RNA polymerase: Inhibited by GPC-N114.
pH Dependence
Optimum pH is 8.0 for protease 3C.
Temperature Dependence
Optimum temperature is 37 degrees Celsius for protease 3C.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 22 | RNA (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 46 | RNA (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 47 | RNA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 48 | RNA (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 49 | RNA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 50 | RNA (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 69 | RNA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 70 | RNA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 93 | RNA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 95 | RNA (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 97 | RNA (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 100 | RNA (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Site | 137-138 | Cleavage | ||||
Sequence: AD | ||||||
Site | 393-394 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 624-625 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 901-902 | Cleavage; by protease 3C | ||||
Sequence: ES | ||||||
Site | 1044-1045 | Cleavage; by ribosomal skip | ||||
Sequence: GP | ||||||
Site | 1195-1196 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Binding site | 1314-1321 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDAGQGKS | ||||||
Site | 1520-1521 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 1608-1609 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 1628-1629 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Active site | 1674 | For protease 3C activity | ||||
Sequence: H | ||||||
Active site | 1708 | For protease 3C activity | ||||
Sequence: D | ||||||
Active site | 1787 | For protease 3C activity | ||||
Sequence: C | ||||||
Site | 1833-1834 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Active site | 2068 | For RdRp activity | ||||
Sequence: D | ||||||
Active site | 2166 | For RdRp activity | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
- Cleaved into 13 chains
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Caphthovirinae > Cardiovirus > Cardiovirus A
- Virus hosts
Accessions
- Primary accessionP12296
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Capsid protein VP2
Capsid protein VP3
Capsid protein VP1
Protein 2A
Protein 2B
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
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 probably autophagosome-like vesicles.
Protein 2C
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
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 probably autophagosome-like vesicles.
Protein 3A
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
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 probably autophagosome-like vesicles.
VPg
Protease 3C
RNA-directed RNA polymerase
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
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 probably autophagosome-like vesicles.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5000141082 | 1-67 | Leader protein | |||
Sequence: MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ | ||||||
Chain | PRO_0000446090 | 1-2293 | Genome polyprotein | |||
Sequence: MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQSPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQANITNVDGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQGVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFAVKSGSLESGFAPFSNKACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGAHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGDLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLESPNPLDVSKTYPTLHILLQFNHRGLEARIFRHGQLWAETHAEVVLRSKTKQISFLSNGSYPSMDATTPLNPWKSTYQAVLRAEPHRVTMDVYHKRIRPFRLPLVQKEWRTCEENVFGLYHVFETHYAGYFSDLLIHDVETNPGPFTFKPRQRPVFQTQGAAVSSMAQTLLPNDLASKAMGSAFTALLDANEDAQKAMKIIKTLSSLSDAWENVKGTLNNPEFWKQLLSRCVQLIAGMTIAVMHPDPLTLLCLGVLTAAEITSQTSLCEEIAAKFKTIFTTPPPRFPVISLFQQQSPLKQVNDVFSLAKNLDWAVKTVEKVVDWFGTWVAQEEREQTLDQLLQRFPEHAKRISDLRNGMAAYVECKESFDFFEKLYNQAVKEKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQIIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNLLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGCKVLDVERAFRPTGDAPLPCFQNNCLFLEKAGLQFRDNRSKEILSLVDVIERAVTRIERKKKVLTAVQTLVAQGPVDEVSFYSVVQQLKARQEATDEQLEELQEAFARVQERSSVFSDWMKISAMLCAATLALTQVVKMAKAVKQMVRPDLVRVQLDEQEQGPYNETTRIKPKTLQLLDVQGPNPTMDFEKFVAKFVTAPIGFVYPTGVSTQTCLLVKGRTLAVNRHMAESDWTSIVVRGVSHTRSSVKIIAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKASDVLPHSSSPLIGIMNVDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSAILADLGGSKKILGFHSAGSMGVAAASIISQEMIDAVVQAFEPQGALERLPDGPRIHVPRKTALRPTVARQVFQPAFAPAVLSKFDPRTDADVDEVAFSKHTSNQETLPPVFRMVAREYANRVFALLGRDNGRLSVKQALDGLEGMDPMDKNTSPGLPYTTLGMRRTDVVDWETATLIPFAAERLEKMNNKDFSDIVYQTFLKDELRPIEKVQAAKTRIVDVPPFEHCILGRQLLGKFASKFQTQPGLELGSAIGCDPDVHWTAFGVAMQGFERVYDVDYSNFDSTHSVAVFRLLAEEFFSEENGFDPLVKDYLESLAISKHAYEEKRYLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLNFDRVRTSLAKTGYKITPANKTSTFPLESTLEDVVFLKRKFKKEGPLYRPVMNREALEAMLSYYRPGTLSEKLTSITMLAVHSGKQEYDRLFAPFREVGVIVPTFESVEYRWRSLFW | ||||||
Modified residue | 41 | Phosphotyrosine; by host SYK | ||||
Sequence: Y | ||||||
Modified residue | 47 | Phosphothreonine; by host CK2 | ||||
Sequence: T | ||||||
Lipidation | 68 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_5000141083 | 68-137 | Capsid protein VP4 | |||
Sequence: GNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLA | ||||||
Chain | PRO_0000310965 | 68-393 | Capsid protein VP0 | |||
Sequence: GNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQ | ||||||
Chain | PRO_5000141084 | 138-393 | Capsid protein VP2 | |||
Sequence: DQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQ | ||||||
Chain | PRO_5000141085 | 394-624 | Capsid protein VP3 | |||
Sequence: SPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQANITNVDGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQ | ||||||
Disulfide bond | 479↔481 | |||||
Sequence: CSC | ||||||
Chain | PRO_5000141086 | 625-901 | Capsid protein VP1 | |||
Sequence: GVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFAVKSGSLESGFAPFSNKACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGAHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGDLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLE | ||||||
Chain | PRO_5000141087 | 902-1044 | Protein 2A | |||
Sequence: SPNPLDVSKTYPTLHILLQFNHRGLEARIFRHGQLWAETHAEVVLRSKTKQISFLSNGSYPSMDATTPLNPWKSTYQAVLRAEPHRVTMDVYHKRIRPFRLPLVQKEWRTCEENVFGLYHVFETHYAGYFSDLLIHDVETNPG | ||||||
Chain | PRO_5000141088 | 1045-1195 | Protein 2B | |||
Sequence: PFTFKPRQRPVFQTQGAAVSSMAQTLLPNDLASKAMGSAFTALLDANEDAQKAMKIIKTLSSLSDAWENVKGTLNNPEFWKQLLSRCVQLIAGMTIAVMHPDPLTLLCLGVLTAAEITSQTSLCEEIAAKFKTIFTTPPPRFPVISLFQQQ | ||||||
Chain | PRO_5000141089 | 1196-1520 | Protein 2C | |||
Sequence: SPLKQVNDVFSLAKNLDWAVKTVEKVVDWFGTWVAQEEREQTLDQLLQRFPEHAKRISDLRNGMAAYVECKESFDFFEKLYNQAVKEKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQIIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNLLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGCKVLDVERAFRPTGDAPLPCFQNNCLFLEKAGLQFRDNRSKEILSLVDVIERAVTRIERKKKVLTAVQTLVAQ | ||||||
Chain | PRO_5000141090 | 1521-1608 | Protein 3A | |||
Sequence: GPVDEVSFYSVVQQLKARQEATDEQLEELQEAFARVQERSSVFSDWMKISAMLCAATLALTQVVKMAKAVKQMVRPDLVRVQLDEQEQ | ||||||
Chain | PRO_5000141091 | 1609-1628 | VPg | |||
Sequence: GPYNETTRIKPKTLQLLDVQ | ||||||
Modified residue | 1611 | O-(5'-phospho-RNA)-tyrosine | ||||
Sequence: Y | ||||||
Chain | PRO_5000141092 | 1629-1833 | Protease 3C | |||
Sequence: GPNPTMDFEKFVAKFVTAPIGFVYPTGVSTQTCLLVKGRTLAVNRHMAESDWTSIVVRGVSHTRSSVKIIAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKASDVLPHSSSPLIGIMNVDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSAILADLGGSKKILGFHSAGSMGVAAASIISQEMIDAVVQAFEPQ | ||||||
Chain | PRO_5000141093 | 1834-2293 | RNA-directed RNA polymerase | |||
Sequence: GALERLPDGPRIHVPRKTALRPTVARQVFQPAFAPAVLSKFDPRTDADVDEVAFSKHTSNQETLPPVFRMVAREYANRVFALLGRDNGRLSVKQALDGLEGMDPMDKNTSPGLPYTTLGMRRTDVVDWETATLIPFAAERLEKMNNKDFSDIVYQTFLKDELRPIEKVQAAKTRIVDVPPFEHCILGRQLLGKFASKFQTQPGLELGSAIGCDPDVHWTAFGVAMQGFERVYDVDYSNFDSTHSVAVFRLLAEEFFSEENGFDPLVKDYLESLAISKHAYEEKRYLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLNFDRVRTSLAKTGYKITPANKTSTFPLESTLEDVVFLKRKFKKEGPLYRPVMNREALEAMLSYYRPGTLSEKLTSITMLAVHSGKQEYDRLFAPFREVGVIVPTFESVEYRWRSLFW |
Post-translational modification
Leader protein
Phosphorylated.
Genome polyprotein
Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (PubMed:8972564).
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 (By similarity).
This process would release the P1-2A peptide from the translational complex (By similarity).
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 (By similarity).
This process would release the P1-2A peptide from the translational complex (By similarity).
Capsid protein VP0
During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle.
VPg
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.
Capsid protein VP4
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.
Keywords
- PTM
PTM databases
Interaction
Subunit
Protease 3C
Interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication (By similarity).
Protein 2A
Interacts with host EIF4E (By similarity).
Interacts with the leader protein (By similarity).
Interacts with the host small ribosomal subunit (PubMed:34887415).
Interacts with the leader protein (By similarity).
Interacts with the host small ribosomal subunit (PubMed:34887415).
Leader protein
Interacts with host RAN; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition (PubMed:25331866).
The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (Probable). Interacts with the protein 2A (By similarity).
The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (Probable). Interacts with the protein 2A (By similarity).
Protein 2C
Interacts with host IFIH1/MDA5; this interaction inhibits the induction of the IFN-beta signal pathway (By similarity).
Family & Domains
Features
Showing features for zinc finger, region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 10-22 | |||||
Sequence: CAHSMTFEECPKC | ||||||
Region | 37-61 | Acidic | ||||
Sequence: DEEWYPEELLTDGEDDVFDPDLDME | ||||||
Motif | 995-1003 | Nuclear localization signal | ||||
Sequence: KRIRPFRLP | ||||||
Region | 1030-1036 | Host EIF4E binding | ||||
Sequence: YFSDLLI | ||||||
Domain | 1282-1448 | SF3 helicase | ||||
Sequence: EKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQIIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNLLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGC | ||||||
Domain | 1631-1823 | Peptidase C3 | ||||
Sequence: NPTMDFEKFVAKFVTAPIGFVYPTGVSTQTCLLVKGRTLAVNRHMAESDWTSIVVRGVSHTRSSVKIIAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKASDVLPHSSSPLIGIMNVDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSAILADLGGSKKILGFHSAGSMGVAAASIISQEMI | ||||||
Domain | 2062-2180 | RdRp catalytic | ||||
Sequence: ERVYDVDYSNFDSTHSVAVFRLLAEEFFSEENGFDPLVKDYLESLAISKHAYEEKRYLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLNFDR |
Sequence similarities
Belongs to the picornaviruses polyprotein family.
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Ribosomal frameshifting.
P12296-1
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.
- NameGenome polyprotein
- NoteProduced by conventional translation.
- Length2,293
- Mass (Da)255,528
- Last updated2007-03-20 v3
- Checksum0394484E477B94E7
P0DJX8-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- Name2B*
Keywords
- Coding sequence diversity
- Technical term