| IED ID | IndEnz0002007852 |
| Enzyme Type ID | protease007852 |
| Protein Name |
Genome polyprotein Cleaved into: Capsid protein VP0 VP4-VP2 ; Capsid protein VP4 P1A Virion protein 4 ; Capsid protein VP2 P1B Virion protein 2 ; Capsid protein VP3 P1C Virion protein 3 ; Protein VP1-2A VPX ; Capsid protein VP1 P1D Virion protein 1 ; Assembly signal 2A pX ; Protein 2BC; Protein 2B P2B Fragment |
| Gene Name | |
| Organism | Simian hepatitis A virus genotype IV (isolate CY-145) (SHAV) (Simian hepatitis A virus (isolate Macaca/Philippines/CY-145/1988)) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Picornaviridae Hepatovirus Hepatovirus A Simian hepatitis A virus Simian hepatitis A virus genotype IV (isolate CY-145) (SHAV) (Simian hepatitis A virus (isolate Macaca/Philippines/CY-145/1988)) |
| Enzyme Sequence | MNMARQGLFQTVGSGLDHILSLADVEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQSEPLKTSVDKPGSKKTQGEKFFLIHSADWLSTHALFHEVAKLDVVSLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQGYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSEFNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQENWRSDPSEGGGIKITHFSTWTSIPTLAAQFAFNASASVGQQIKVIPVDPYFYQMTNSNPDQKYITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLQFCFVPGNELIEVTSITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNCYIKSSHQKGEYTAIEKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTSQTGDDSGGFSTTVSTEQNVPDPQVGITTPKDLKGKANKGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSVYKFMGRSHFLCTFTFNANNREYTFPITLSSTSNPPHGSPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKQSALTIDYKTALGAIRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDTTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFFFPRAPLNSSAMMTSENMLDRIAGGDLESSVDDPRTDEDRRFESHIEKKPYKELRLEVGKQRFKYAREELSNEILPPPRKLKGLFSQSKIS |
| Enzyme Length | 839 |
| Uniprot Accession Number | P31788 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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 naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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 naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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 naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of the immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2BC]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the DDX58/IFIH1 (RIG-I/MDA5) pathway. {ECO:0000250|UniProtKB:P08617}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (10); Compositional bias (3); Motif (2); Non-terminal residue (1); Region (4); Site (6) |
| Keywords | Capsid protein;Host endosome;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;T=pseudo3 icosahedral capsid protein;Transport;Viral attachment to host cell;Viral ion channel;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2B]: Host membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; 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 is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03303}.; PTM: [Protein VP1-2A]: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in nacked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Capsid protein VP4]: Unlike other picornaviruses, does not seem to be myristoylated. {ECO:0000250|UniProtKB:P08617}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 167..171; /note=(L)YPX(n)L motif; /evidence=ECO:0000250|UniProtKB:P08617; MOTIF 200..205; /note=(L)YPX(n)L motif; /evidence=ECO:0000250|UniProtKB:P08617 |
| Gene Encoded By | |
| Mass | 93,825 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |