UniProt functional annotation for P03322



	UniProt functional annotation for P03322

UniProt code: P03322.

Organism: Rous sarcoma virus (strain Prague C) (RSV-PrC).

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

Function: [Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains). {ECO:0000269|PubMed:26223638}.

Function: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:28588198}.

Function: [Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.

Function: [Spacer peptide]: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000269|PubMed:28588198}.

Function: [Protease p15]: Aspartyl protease that 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}.

Subunit: [Protease p15]: Active as a homodimer (PubMed:2166563, PubMed:2536902). {ECO:0000269|PubMed:2166563, ECO:0000269|PubMed:2536902}.

Subunit: [Capsid protein p27, alternate cleaved 1]: Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:14659756, ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062}.

Subunit: [Capsid protein p27, alternate cleaved 2]: Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:14659756, ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062}.

Subunit: [Gag polyprotein]: Homohexamer (PubMed:26223638). Interacts (via p2B domain) with host PACSIN2; this interaction probably allows PACSIN2 recruitment to viral assembly sites (By similarity). {ECO:0000250|UniProtKB:P0C776, ECO:0000269|PubMed:26223638}.

Subcellular location: [Matrix protein p19]: Virion {ECO:0000305}.

Subcellular location: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.

Subcellular location: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.

Subcellular location: [Nucleocapsid protein p12]: Virion {ECO:0000305}.

Subcellular location: [Gag polyprotein]: Host nucleus, host nucleolus {ECO:0000269|PubMed:23036987}. Host nucleus, host nucleoplasm {ECO:0000269|PubMed:23036987}. Note=Shuttles between nucleoplasm and nucleolus. {ECO:0000269|PubMed:23036987}.

Domain: [Gag 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. P2B contains two L domains: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases and a LYPX(n)L domain which is known to bind the Alix adaptator protein. {ECO:0000269|PubMed:20392845}.

Domain: [Gag polyprotein]: Contains a nuclear export signal in p10 and a nucleolar localization signal in nucleocapsid protein p12. {ECO:0000269|PubMed:23036987}.

Domain: Capsid protein p27: Proton-driven dimerization of the C- terminus facilitates capsid assembly. {ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062}.

Ptm: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:8636100, PubMed:8627817). The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1 (PubMed:28588198). {ECO:0000269|PubMed:28588198, ECO:0000269|PubMed:8627817, ECO:0000269|PubMed:8636100}.

Miscellaneous: [Isoform Gag polyprotein]: Produced by conventional translation. {ECO:0000269|PubMed:9813113}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rous sarcoma virus (strain Prague C) (RSV-PrC).
Taxonomy:		Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.



Function:		[Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains). {ECO:0000269\|PubMed:26223638}.



Function:		Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000269\|PubMed:10873863, ECO:0000269\|PubMed:28588198}.



Function:		[Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.



Function:		[Spacer peptide]: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000269\|PubMed:28588198}.



Function:		[Protease p15]: Aspartyl protease that 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}.


Subunit:		[Protease p15]: Active as a homodimer (PubMed:2166563, PubMed:2536902). {ECO:0000269\|PubMed:2166563, ECO:0000269\|PubMed:2536902}.
Subunit:		[Capsid protein p27, alternate cleaved 1]: Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). {ECO:0000269\|PubMed:10873863, ECO:0000269\|PubMed:14659756, ECO:0000269\|PubMed:19446529, ECO:0000269\|PubMed:20228062}.
Subunit:		[Capsid protein p27, alternate cleaved 2]: Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062). {ECO:0000269\|PubMed:10873863, ECO:0000269\|PubMed:14659756, ECO:0000269\|PubMed:19446529, ECO:0000269\|PubMed:20228062}.
Subunit:		[Gag polyprotein]: Homohexamer (PubMed:26223638). Interacts (via p2B domain) with host PACSIN2; this interaction probably allows PACSIN2 recruitment to viral assembly sites (By similarity). {ECO:0000250\|UniProtKB:P0C776, ECO:0000269\|PubMed:26223638}.
Subcellular location:		[Matrix protein p19]: Virion {ECO:0000305}.
Subcellular location:		[Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.
Subcellular location:		[Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.
Subcellular location:		[Nucleocapsid protein p12]: Virion {ECO:0000305}.
Subcellular location:		[Gag polyprotein]: Host nucleus, host nucleolus {ECO:0000269\|PubMed:23036987}. Host nucleus, host nucleoplasm {ECO:0000269\|PubMed:23036987}. Note=Shuttles between nucleoplasm and nucleolus. {ECO:0000269\|PubMed:23036987}.
Domain:		[Gag 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. P2B contains two L domains: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases and a LYPX(n)L domain which is known to bind the Alix adaptator protein. {ECO:0000269\|PubMed:20392845}.
Domain:		[Gag polyprotein]: Contains a nuclear export signal in p10 and a nucleolar localization signal in nucleocapsid protein p12. {ECO:0000269\|PubMed:23036987}.
Domain:		Capsid protein p27: Proton-driven dimerization of the C- terminus facilitates capsid assembly. {ECO:0000269\|PubMed:19446529, ECO:0000269\|PubMed:20228062}.
Ptm:		[Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:8636100, PubMed:8627817). The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1 (PubMed:28588198). {ECO:0000269\|PubMed:28588198, ECO:0000269\|PubMed:8627817, ECO:0000269\|PubMed:8636100}.
Miscellaneous:		[Isoform Gag polyprotein]: Produced by conventional translation. {ECO:0000269\|PubMed:9813113}.