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UniProt functional annotation for P11284 | ||
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| UniProt code: P11284. |
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| Organism: | |
Mouse mammary tumor virus (strain C3H) (MMTV). |
| Taxonomy: | |
Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus. |
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| Function: | |
[Matrix protein p10]: Matrix protein. {ECO:0000305}. |
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| Function: | |
[Nucleocapsid protein p14]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}. |
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| Function: | |
[Capsid protein p27]: Capsid protein. {ECO:0000305}. |
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| Subunit: | |
[Matrix protein p10]: Homodimer; when myristoylated. {ECO:0000250|UniProtKB:P10258}. |
| Subcellular location: | |
[Matrix protein p10]: Virion {ECO:0000250|UniProtKB:P10258}. |
| Subcellular location: | |
[Capsid protein p27]: Virion {ECO:0000250|UniProtKB:P10258}. |
| Subcellular location: | |
[Nucleocapsid protein p14]: Virion {ECO:0000250|UniProtKB:P10258}. |
| 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. Gag-p27 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101. {ECO:0000305}. |
| Ptm: | |
[Gag 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:0000269|PubMed:2542570}. |
| Ptm: | |
[Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:2542570}. |
| Miscellaneous: | |
[Isoform Gag polyprotein]: Produced by conventional translation. {ECO:0000269|PubMed:3035577}. |
Annotations taken from UniProtKB at the EBI.