UniProt functional annotation for P03336



	UniProt functional annotation for P03336

UniProt code: P03336.

Organism: AKV murine leukemia virus (AKR (endogenous) murine leukemia virus).

Taxonomy: Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus; Murine leukemia virus.

Function: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4- like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release. {ECO:0000250|UniProtKB:P03332}.

Function: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex. {ECO:0000250|UniProtKB:P03332}.

Function: [RNA-binding phosphoprotein p12]: Constituent of the pre- integration complex (PIC) which tethers the latter to mitotic chromosomes. {ECO:0000250|UniProtKB:P03332}.

Function: [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250|UniProtKB:P03332}.

Function: [Nucleocapsid protein p10-Gag]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization. {ECO:0000250|UniProtKB:P03332}.

Subunit: Capsid protein p30 is a homohexamer, that further associates as homomultimer (PubMed:17223564, PubMed:15386017). The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers(PubMed:17223564, PubMed:15386017). Capsid protein p30: Interacts with mouse UBE2I and mouse PIAS4 (By similarity). Gag polyprotein: Interacts (via PPXY motif) with host NEDD4 (By similarity). Gag polyprotein: Interacts (via PSAP motif) with host TSG101 (By similarity). Gag polyprotein: Interacts (via LYPX(n)L motif) with host PDCD6IP (By similarity). {ECO:0000250|UniProtKB:P03332, ECO:0000269|PubMed:15386017, ECO:0000269|PubMed:17223564}.

Subcellular location: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}.

Subcellular location: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03332}.

Subcellular location: [Capsid protein p30]: Virion {ECO:0000250|UniProtKB:P03332}.

Subcellular location: [Nucleocapsid protein p10-Gag]: Virion {ECO:0000250|UniProtKB:P03332}.

Subcellular location: [RNA-binding phosphoprotein p12]: Host cytoplasm {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on. {ECO:0000250|UniProtKB:P03332}.

Domain: [Gag polyprotein]: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. {ECO:0000250|UniProtKB:P03332}.

Ptm: [Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.

Ptm: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03332}.

Ptm: [Capsid protein p30]: Sumoylated; required for virus replication. {ECO:0000250|UniProtKB:P03332}.

Ptm: RNA-binding phosphoprotein p12 is phosphorylated on serine residues. {ECO:0000250|UniProtKB:P03332}.

Annotations taken from UniProtKB at the EBI.


Organism:		AKV murine leukemia virus (AKR (endogenous) murine leukemia virus).
Taxonomy:		Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus; Murine leukemia virus.



Function:		[Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4- like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release. {ECO:0000250\|UniProtKB:P03332}.



Function:		[Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex. {ECO:0000250\|UniProtKB:P03332}.



Function:		[RNA-binding phosphoprotein p12]: Constituent of the pre- integration complex (PIC) which tethers the latter to mitotic chromosomes. {ECO:0000250\|UniProtKB:P03332}.



Function:		[Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250\|UniProtKB:P03332}.



Function:		[Nucleocapsid protein p10-Gag]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization. {ECO:0000250\|UniProtKB:P03332}.


Subunit:		Capsid protein p30 is a homohexamer, that further associates as homomultimer (PubMed:17223564, PubMed:15386017). The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers(PubMed:17223564, PubMed:15386017). Capsid protein p30: Interacts with mouse UBE2I and mouse PIAS4 (By similarity). Gag polyprotein: Interacts (via PPXY motif) with host NEDD4 (By similarity). Gag polyprotein: Interacts (via PSAP motif) with host TSG101 (By similarity). Gag polyprotein: Interacts (via LYPX(n)L motif) with host PDCD6IP (By similarity). {ECO:0000250\|UniProtKB:P03332, ECO:0000269\|PubMed:15386017, ECO:0000269\|PubMed:17223564}.
Subcellular location:		[Gag polyprotein]: Virion {ECO:0000250\|UniProtKB:P03332}. Host cell membrane {ECO:0000250\|UniProtKB:P03332}; Lipid-anchor {ECO:0000250\|UniProtKB:P03332}. Host endosome, host multivesicular body {ECO:0000250\|UniProtKB:P26807}.
Subcellular location:		[Matrix protein p15]: Virion {ECO:0000250\|UniProtKB:P03332}.
Subcellular location:		[Capsid protein p30]: Virion {ECO:0000250\|UniProtKB:P03332}.
Subcellular location:		[Nucleocapsid protein p10-Gag]: Virion {ECO:0000250\|UniProtKB:P03332}.
Subcellular location:		[RNA-binding phosphoprotein p12]: Host cytoplasm {ECO:0000250\|UniProtKB:P03332}. Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on. {ECO:0000250\|UniProtKB:P03332}.
Domain:		[Gag polyprotein]: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. {ECO:0000250\|UniProtKB:P03332}.
Ptm:		[Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250\|UniProtKB:P03332}.
Ptm:		[Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250\|UniProtKB:P03332}.
Ptm:		[Capsid protein p30]: Sumoylated; required for virus replication. {ECO:0000250\|UniProtKB:P03332}.
Ptm:		RNA-binding phosphoprotein p12 is phosphorylated on serine residues. {ECO:0000250\|UniProtKB:P03332}.