P12418 · MU2_REOVD
- ProteinMicrotubule-associated protein mu-2
- GeneM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Minor inner capsid (core) component. Displays NTPase and RNA 5'-triphosphatase (RTPase) activities. ATP is the preferred substrate for hydrolysis. May function as a cofactor of polymerase lambda-3. Associates with microtubules and plays a role in the formation, structural organization and morphology of viral inclusions, where the assembly of cores and the replication of viral RNA occur. Together with mu-NS, recruits the other core proteins to these inclusions (By similarity).
Cofactor
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | host cytoskeleton | |
Cellular Component | viral capsid | |
Molecular Function | structural molecule activity | |
Biological Process | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host IRF9 activity | |
Biological Process | symbiont-mediated suppression of host type I interferon-mediated signaling pathway | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated protein mu-2
- Short namesMu2
Gene names
Organism names
- Strains
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Spinareoviridae > Orthoreovirus > Mammalian orthoreovirus
- Virus hosts
Accessions
- Primary accessionP12418
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in the inner capsid (12 copies).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 208 | Loss of filamentous subcellular location. | ||||
Sequence: P → S |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000222746 | 1-736 | Microtubule-associated protein mu-2 | |||
Sequence: MAYIAVPAVVDSRSSEAIGLLESFGVDAGADANDVSYQDHDYVLDQLQYMLDGYEAGDVIDALVHKNWLHHSVYCLLPPKSQLLEYWKSNPSAIPDNVDRRLRKRLMLKKDLRKDDEYNQLARAFKISDVYAPLISSTTSPMTMIQNLNRGEIVYTTTDRVIGARILLYAPRKYYASTLSFTMTKCIIPFGKEVGRVPHSRFNVGTFPSIATPKCFVMSGVDIESIPNEFIKLFYQRVKSVHANILNDISPQIVSDMINRKRLRVHTPSDRRAAQLMHLPYHVKRGASHVDVYKVDVVDMLFEVVDVADGLRNVSRKLTMHTVPVCILEMLGIEIADYCIRQEDGMLTDWFLLLTMLSDGLTDRRTHCQYLMNPSSVPPDVILNISITGFINRHTIDVMPDIYDFVKPIGAVLPKGSFKSTIMRVLDSISILGIQIMPRAHVVDSDEVGEQMEPTFEQAVMEIYKGIAGVDSLDDLIKWVLNSDLIPHDDRLGQLFQAFLPLAKDLLAPMARKFYDNSMSEGRLLTFAHADSELLNANYFGHLLRLKIPYITEVNLMIRKNREGGELFQLVLSYLYKMYATSAQPKWFGSLLRLLICPWLHMEKLIGEADPASTSAEIGWHIPREQLMQDGWCGCEDGFIPYVSIRAPRLVIEELMEKNWGQYHAQVIVTDQLVVGEPRRVSAKAVIKGNHLPVKLVSRFACFTLTAKYEMRLSCGHSTGRGAAYSARLAFRSDLA |
Interaction
Subunit
Interacts with protein mu-NS; in viral inclusions. Interacts with polymerase lambda-3; this interaction stimulates the ATPase activity of mu-2 (By similarity).
Protein-protein interaction databases
Family & Domains
Sequence
- Sequence statusComplete
- Length736
- Mass (Da)83,276
- Last updated1989-10-01 v1
- Checksum2CF0D88BA16EF564
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 150 | in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 208 | in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916 | ||||
Sequence: P → S | ||||||
Sequence conflict | 342 | in Ref. 4; ABP48916 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 372 | in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916 | ||||
Sequence: M → I |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M27261 EMBL· GenBank· DDBJ | AAA47256.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
AF461683 EMBL· GenBank· DDBJ | AAL99937.1 EMBL· GenBank· DDBJ | mRNA | ||
AF461684 EMBL· GenBank· DDBJ | AAL99938.1 EMBL· GenBank· DDBJ | mRNA | ||
AY551083 EMBL· GenBank· DDBJ | AAS55892.1 EMBL· GenBank· DDBJ | mRNA | ||
EF494438 EMBL· GenBank· DDBJ | ABP48916.1 EMBL· GenBank· DDBJ | Genomic RNA |