UniProt functional annotation for P07570



	UniProt functional annotation for P07570

UniProt code: P07570.

Organism: Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).

Taxonomy: Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.

Function: [Matrix protein p10]: Matrix protein. {ECO:0000305}.

Function: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.

Function: [Capsid protein p27]: capsid protein. {ECO:0000305}.

Function: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE- ProRule:PRU00275, ECO:0000269|PubMed:9636364}.

Function: [Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE- ProRule:PRU00275, ECO:0000269|PubMed:9636364}.

Function: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000269|PubMed:22171253}.

Catalytic activity: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:17169987};

Subunit: [Protease 17 kDa]: Homodimer (By similarity). {ECO:0000250|UniProtKB:P10271}.

Subunit: [G-patch peptide]: Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). {ECO:0000269|PubMed:22171253}.

Subunit: [Nucleocapsid protein-dUTPase]: Homotrimer (PubMed:17169987). {ECO:0000269|PubMed:17169987}.

Subcellular location: [Matrix protein p10]: Virion {ECO:0000305}.

Subcellular location: [Capsid protein p27]: Virion {ECO:0000305}.

Subcellular location: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.

Subcellular location: [Protease 13 kDa]: Virion {ECO:0000269|PubMed:9636364}.

Subcellular location: [Protease 17 kDa]: Virion {ECO:0000269|PubMed:9636364}.

Domain: [Gag-Pro polyprotein]: Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Phosphorylated protein pp24 and phosphorylated protein pp18 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4. Both motifs contribute to viral release. The PSAP motif acts as an additional L domain and promotes the efficient release of the virions but requires an intact PPPY motif to perform its function. {ECO:0000269|PubMed:12915562}.

Domain: [Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is present at the C-terminus of the protease from which it is then detached by the protease itself. {ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:22171253}.

Ptm: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric. {ECO:0000269|PubMed:14568536, ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.

Ptm: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.

Ptm: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:9636364}.

Miscellaneous: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal frameshifting between gag-pro. {ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
Taxonomy:		Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.



Function:		[Matrix protein p10]: Matrix protein. {ECO:0000305}.



Function:		Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.



Function:		[Capsid protein p27]: capsid protein. {ECO:0000305}.



Function:		[Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255\|PROSITE- ProRule:PRU00275, ECO:0000269\|PubMed:9636364}.



Function:		[Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255\|PROSITE- ProRule:PRU00275, ECO:0000269\|PubMed:9636364}.



Function:		[G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000269\|PubMed:22171253}.


Catalytic activity:		Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269\|PubMed:17169987};
Subunit:		[Protease 17 kDa]: Homodimer (By similarity). {ECO:0000250\|UniProtKB:P10271}.
Subunit:		[G-patch peptide]: Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). {ECO:0000269\|PubMed:22171253}.
Subunit:		[Nucleocapsid protein-dUTPase]: Homotrimer (PubMed:17169987). {ECO:0000269\|PubMed:17169987}.
Subcellular location:		[Matrix protein p10]: Virion {ECO:0000305}.
Subcellular location:		[Capsid protein p27]: Virion {ECO:0000305}.
Subcellular location:		[Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.
Subcellular location:		[Protease 13 kDa]: Virion {ECO:0000269\|PubMed:9636364}.
Subcellular location:		[Protease 17 kDa]: Virion {ECO:0000269\|PubMed:9636364}.
Domain:		[Gag-Pro polyprotein]: Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Phosphorylated protein pp24 and phosphorylated protein pp18 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4. Both motifs contribute to viral release. The PSAP motif acts as an additional L domain and promotes the efficient release of the virions but requires an intact PPPY motif to perform its function. {ECO:0000269\|PubMed:12915562}.
Domain:		[Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is present at the C-terminus of the protease from which it is then detached by the protease itself. {ECO:0000269\|PubMed:16257973, ECO:0000269\|PubMed:22171253}.
Ptm:		[Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric. {ECO:0000269\|PubMed:14568536, ECO:0000269\|PubMed:16257973, ECO:0000269\|PubMed:9636364}.
Ptm:		[Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250\|UniProtKB:P10258}.
Ptm:		[Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269\|PubMed:9636364}.
Miscellaneous:		[Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal frameshifting between gag-pro. {ECO:0000305\|PubMed:2421920, ECO:0000305\|PubMed:24298557}.