UniProt functional annotation for P03303



	UniProt functional annotation for P03303

UniProt codes: P03303, Q89649.

Organism: Human rhinovirus 14 (HRV-14).

Taxonomy: Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Picornavirales; Picornaviridae; Enterovirus.

Function: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells (PubMed:10562537). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (Probable). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (PubMed:28696310). After genome has been released, the channel shrinks. {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:10562537, ECO:0000269|PubMed:28696310, ECO:0000305|PubMed:28696310}.

Function: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.

Function: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.

Function: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (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). {ECO:0000250|UniProtKB:P03300}.

Function: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}.

Function: [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP62 and NUP153 (Probable). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301, ECO:0000305|PubMed:12163599}.

Function: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.

Function: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.

Function: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.

Function: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (PubMed:17005635). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (PubMed:17005635). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (Probable). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512, ECO:0000305|PubMed:31381608}.

Function: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.

Function: [Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.

Function: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (PubMed:18572216). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (PubMed:33093214). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:18572216, ECO:0000269|PubMed:33093214}.

Function: [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.

Catalytic activity: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300};

Catalytic activity: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};

Catalytic activity: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};

Catalytic activity: [Protease 3C]: Reaction=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.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};

Cofactor: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313};

Activity regulation: [RNA-directed RNA polymerase]: Replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Capsid protein VP0]: Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Capsid protein VP1]: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity). Interacts with host ICAM1 (PubMed:10562537). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:10562537}.

Subunit: [Capsid protein VP2]: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Capsid protein VP3]: Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP4 in the mature capsid (By similarity). Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity). {ECO:0000250|UniProtKB:P03300}.

Subunit: [Capsid protein VP4]: Interacts with capsid protein VP1 and capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.

Subunit: [Protein 2C]: Homohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity). Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity). Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). {ECO:0000250|UniProtKB:P03300}.

Subunit: [Protein 3AB]: Interacts with protein 3CD. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Protein 3A]: Homodimer (By similarity). Interacts with host GBF1 (PubMed:17005635). Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (PubMed:31381608). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17005635, ECO:0000269|PubMed:31381608}.

Subunit: [Viral protein genome-linked]: Interacts with RNA-directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.

Subunit: [Protein 3CD]: Interacts with protein 3AB and with RNA- directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.

Subunit: [RNA-directed RNA polymerase]: Interacts with Viral protein genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.

Subcellular location: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.

Subcellular location: [Capsid protein VP4]: Virion.

Subcellular location: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.

Subcellular location: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.

Subcellular location: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.

Subcellular location: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Subcellular location: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Subcellular location: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Subcellular location: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Subcellular location: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.

Subcellular location: [Protease 3C]: Host cytoplasm.

Subcellular location: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Subcellular location: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.

Domain: [Protein 2C]: The N-terminus has membrane-binding (By similarity). The N-terminus also displays RNA-binding properties (By similarity). The N-terminus is involved in oligomerization (By similarity). The central part contains an ATPase domain and a C4-type zinc-finger (By similarity). The C-terminus is involved in RNA-binding (By similarity). The extreme C-terminus contains a region involved in oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.

Ptm: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.

Ptm: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.

Ptm: [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 it is followed by a conformational change infectious virion. {ECO:0000269|PubMed:8383233}.

Ptm: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.

Ptm: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.

Similarity: Belongs to the picornaviruses polyprotein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Human rhinovirus 14 (HRV-14).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Picornavirales; Picornaviridae; Enterovirus.



Function:		[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells (PubMed:10562537). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (Probable). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (PubMed:28696310). After genome has been released, the channel shrinks. {ECO:0000250\|UniProtKB:P03300, ECO:0000269\|PubMed:10562537, ECO:0000269\|PubMed:28696310, ECO:0000305\|PubMed:28696310}.



Function:		[Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250\|UniProtKB:P03300}.



Function:		[Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250\|UniProtKB:P03300}.



Function:		[Capsid protein VP4]: Lies on the inner surface of the capsid shell (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). {ECO:0000250\|UniProtKB:P03300}.



Function:		[Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP62 and NUP153 (Probable). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). {ECO:0000250\|UniProtKB:P03300, ECO:0000250\|UniProtKB:P03301, ECO:0000305\|PubMed:12163599}.



Function:		[Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (PubMed:17005635). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (PubMed:17005635). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (Probable). {ECO:0000250\|UniProtKB:P03300, ECO:0000269\|PubMed:17005635, ECO:0000305\|PubMed:30755512, ECO:0000305\|PubMed:31381608}.



Function:		[Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250\|UniProtKB:P03300}.



Function:		[Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (PubMed:18572216). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (PubMed:33093214). {ECO:0000250\|UniProtKB:P03300, ECO:0000269\|PubMed:18572216, ECO:0000269\|PubMed:33093214}.



Function:		[RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250\|UniProtKB:P03300}.


Catalytic activity:		[Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250\|UniProtKB:P03300};
Catalytic activity:		[Protease 2A]: Reaction=Selective cleavage of Tyr-\|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250\|UniProtKB:P03300};
Catalytic activity:		[RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00539};
Catalytic activity:		[Protease 3C]: Reaction=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.; EC=3.4.22.28; Evidence={ECO:0000255\|PROSITE-ProRule:PRU01222};
Cofactor:		[RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250\|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250\|UniProtKB:P03300, ECO:0000250\|UniProtKB:P03313};
Activity regulation:		[RNA-directed RNA polymerase]: Replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Capsid protein VP0]: Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Capsid protein VP1]: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity). Interacts with host ICAM1 (PubMed:10562537). {ECO:0000250\|UniProtKB:P03300, ECO:0000269\|PubMed:10562537}.
Subunit:		[Capsid protein VP2]: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Capsid protein VP3]: Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP4 in the mature capsid (By similarity). Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity). {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Capsid protein VP4]: Interacts with capsid protein VP1 and capsid protein VP3. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Protease 2A]: Homodimer. {ECO:0000250\|UniProtKB:P04936}.
Subunit:		[Protein 2C]: Homohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity). Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity). Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Protein 3AB]: Interacts with protein 3CD. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Protein 3A]: Homodimer (By similarity). Interacts with host GBF1 (PubMed:17005635). Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (PubMed:31381608). {ECO:0000250\|UniProtKB:P03300, ECO:0000269\|PubMed:17005635, ECO:0000269\|PubMed:31381608}.
Subunit:		[Viral protein genome-linked]: Interacts with RNA-directed RNA polymerase. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[Protein 3CD]: Interacts with protein 3AB and with RNA- directed RNA polymerase. {ECO:0000250\|UniProtKB:P03300}.
Subunit:		[RNA-directed RNA polymerase]: Interacts with Viral protein genome-linked and with protein 3CD. {ECO:0000250\|UniProtKB:P03300}.
Subcellular location:		[Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.
Subcellular location:		[Capsid protein VP4]: Virion.
Subcellular location:		[Capsid protein VP2]: Virion {ECO:0000250\|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
Subcellular location:		[Capsid protein VP3]: Virion {ECO:0000250\|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
Subcellular location:		[Capsid protein VP1]: Virion {ECO:0000250\|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
Subcellular location:		[Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Subcellular location:		[Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Subcellular location:		[Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Subcellular location:		[Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Subcellular location:		[Viral protein genome-linked]: Virion {ECO:0000250\|UniProtKB:P03300}. Host cytoplasm {ECO:0000250\|UniProtKB:Q66478}.
Subcellular location:		[Protease 3C]: Host cytoplasm.
Subcellular location:		[Protein 3CD]: Host nucleus {ECO:0000250\|UniProtKB:P03300}. Host cytoplasm {ECO:0000250\|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Subcellular location:		[RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
Domain:		[Protein 2C]: The N-terminus has membrane-binding (By similarity). The N-terminus also displays RNA-binding properties (By similarity). The N-terminus is involved in oligomerization (By similarity). The central part contains an ATPase domain and a C4-type zinc-finger (By similarity). The C-terminus is involved in RNA-binding (By similarity). The extreme C-terminus contains a region involved in oligomerization (By similarity). {ECO:0000250\|UniProtKB:P03300}.
Ptm:		[Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250\|UniProtKB:P03300}.
Ptm:		[Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250\|UniProtKB:P03300}.
Ptm:		[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 it is followed by a conformational change infectious virion. {ECO:0000269\|PubMed:8383233}.
Ptm:		[Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250\|UniProtKB:P03300}.
Ptm:		[Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250\|UniProtKB:P03300}.
Similarity:		Belongs to the picornaviruses polyprotein family. {ECO:0000305}.