P12418 · MU2_REOVD

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

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componenthost cytoskeleton
Cellular Componentviral capsid
Molecular Functionstructural molecule activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of host IRF9 activity
Biological Processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Microtubule-associated protein mu-2
  • Short names
    Mu2

Gene names

    • Name
      M1

Organism names

Accessions

  • Primary accession
    P12418
  • Secondary accessions
    • A4ZY23
    • Q71M35
    • Q8QT10

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis208Loss of filamentous subcellular location.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002227461-736Microtubule-associated protein mu-2

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

Structure

3D structure databases

Family & Domains

Sequence similarities

Belongs to the orthoreovirus mu-2 protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    736
  • Mass (Da)
    83,276
  • Last updated
    1989-10-01 v1
  • Checksum
    2CF0D88BA16EF564
MAYIAVPAVVDSRSSEAIGLLESFGVDAGADANDVSYQDHDYVLDQLQYMLDGYEAGDVIDALVHKNWLHHSVYCLLPPKSQLLEYWKSNPSAIPDNVDRRLRKRLMLKKDLRKDDEYNQLARAFKISDVYAPLISSTTSPMTMIQNLNRGEIVYTTTDRVIGARILLYAPRKYYASTLSFTMTKCIIPFGKEVGRVPHSRFNVGTFPSIATPKCFVMSGVDIESIPNEFIKLFYQRVKSVHANILNDISPQIVSDMINRKRLRVHTPSDRRAAQLMHLPYHVKRGASHVDVYKVDVVDMLFEVVDVADGLRNVSRKLTMHTVPVCILEMLGIEIADYCIRQEDGMLTDWFLLLTMLSDGLTDRRTHCQYLMNPSSVPPDVILNISITGFINRHTIDVMPDIYDFVKPIGAVLPKGSFKSTIMRVLDSISILGIQIMPRAHVVDSDEVGEQMEPTFEQAVMEIYKGIAGVDSLDDLIKWVLNSDLIPHDDRLGQLFQAFLPLAKDLLAPMARKFYDNSMSEGRLLTFAHADSELLNANYFGHLLRLKIPYITEVNLMIRKNREGGELFQLVLSYLYKMYATSAQPKWFGSLLRLLICPWLHMEKLIGEADPASTSAEIGWHIPREQLMQDGWCGCEDGFIPYVSIRAPRLVIEELMEKNWGQYHAQVIVTDQLVVGEPRRVSAKAVIKGNHLPVKLVSRFACFTLTAKYEMRLSCGHSTGRGAAYSARLAFRSDLA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict150in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916
Sequence conflict208in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916
Sequence conflict342in Ref. 4; ABP48916
Sequence conflict372in Ref. 2; AAL99937, 3; AAS55892 and 4; ABP48916

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Similar Proteins

Disclaimer

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