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Protein

Microtubule-associated protein mu-2

Gene

M1

Organism
Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. suppression by virus of host IRF9 activity Source: UniProtKB-KW
  2. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF9 by virus, Viral immunoevasion

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein mu-2
Short name:
Mu2
Gene namesi
Name:M1
OrganismiReovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Taxonomic identifieri10884 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000007253 Componenti: Genome

Subcellular locationi

Virion Curated. Host cytoplasmhost cytoskeleton By similarity
Note: Found in the inner capsid (12 copies). Associates with microtubules (By similarity).By similarity

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cytoskeleton Source: UniProtKB-SubCell
  3. viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoskeleton, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi415 – 4151K → A: Loss of ATPase activity; when associated with A-419. No effect on microtubules association. 1 Publication
Mutagenesisi419 – 4191K → A: Loss of ATPase activity; when associated with A-415. No effect on microtubules association. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Microtubule-associated protein mu-2PRO_0000222747Add
BLAST

Interactioni

Subunit structurei

Interacts with protein mu-NS; in viral inclusions. Interacts with polymerase lambda-3; this interaction stimulates the ATPase activity of mu-2.2 Publications

Protein-protein interaction databases

IntActiQ00335. 15 interactions.

Family & Domainsi

Sequence similaritiesi

Belongs to the orthoreovirus mu-2 protein family.Curated

Family and domain databases

InterProiIPR012494. Reovirus_Mu2.
[Graphical view]
PfamiPF07781. Reovirus_Mu2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYIAVPAVV DSRSSEAIGL LESFGVDAGA DANDVSYQDH DYVLDQLQYM
60 70 80 90 100
LDGYEAGDVI DALVHKNWLH HSVYCLLPPK SQLLEYWKSN PSVIPDNVDR
110 120 130 140 150
RLRKRLMLKK DLRKDDEYNQ LARAFKISDV YAPLISSTTS PMTMIQNLNQ
160 170 180 190 200
GEIVYTTTDR VIGARILLYA PRKYYASTLS FTMTKCIIPF GKEVGRVPHS
210 220 230 240 250
RFNVGTFPSI ATPKCFVMSG VDIESIPNEF IKLFYQRVKS VHANILNDIS
260 270 280 290 300
PQIVSDMINR KRLRVHTPSD RRAAQLMHLP YHVKRGASHV DVYKVDVVDV
310 320 330 340 350
LLEVVDVADG LRNVSRKLTM HTVPVCILEM LGIEIADYCI RQEDGMFTDW
360 370 380 390 400
FLLLTMLSDG LTDRRTHCQY LINPSSVPPD VILNISITGF INRHTIDVMP
410 420 430 440 450
DIYDFVKPIG AVLPKGSFKS TIMRVLDSIS ILGVQIMPRA HVVDSDEVGE
460 470 480 490 500
QMEPTFEHAV MEIYKGIAGV DSLDDLIKWV LNSDLIPHDD RLGQLFQAFL
510 520 530 540 550
PLAKDLLAPM ARKFYDNSMS EGRLLTFAHA DSELLNANYF GHLLRLKIPY
560 570 580 590 600
ITEVNLMIRK NREGGELFQL VLSYLYKMYA TSAQPKWFGS LLRLLICPWL
610 620 630 640 650
HMEKLIGEAD PASTSAEIGW HIPREQLMQD GWCGCEDGFI PYVSIRAPRL
660 670 680 690 700
VMEELMEKNW GQYHAQVIVT DQLVVGEPRR VSAKAVIKGN HLPVKLVSRF
710 720 730
ACFTLTAKYE MRLSCGHSTG RGAAYNARLA FRSDLA
Length:736
Mass (Da):83,266
Last modified:November 30, 1992 - v1
Checksum:i41508441FA4FA784
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021L → F in AAL99936 (PubMed:11932414).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59945 Genomic RNA. Translation: CAA42570.1.
AF461682 mRNA. Translation: AAL99936.1.
PIRiS23654.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59945 Genomic RNA. Translation: CAA42570.1.
AF461682 mRNA. Translation: AAL99936.1.
PIRiS23654.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ00335. 15 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR012494. Reovirus_Mu2.
[Graphical view]
PfamiPF07781. Reovirus_Mu2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence comparison of the M1 genome segment of reovirus type 1 Lang and type 3 Dearing."
    Zou S., Brown E.G.
    Virus Res. 22:159-164(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Reovirus core protein mu2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules."
    Parker J.S.L., Broering T.J., Kim J., Higgins D.E., Nibert M.L.
    J. Virol. 76:4483-4496(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Reovirus sigma NS protein localizes to inclusions through an association requiring the mu NS amino terminus."
    Miller C.L., Broering T.J., Parker J.S.L., Arnold M.M., Nibert M.L.
    J. Virol. 77:4566-4576(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN MU-NS.
  4. "Nucleoside and RNA triphosphatase activities of orthoreovirus transcriptase cofactor mu2."
    Kim J., Parker J.S.L., Murray K.E., Nibert M.L.
    J. Biol. Chem. 279:4394-4403(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLYMERASE LAMBDA-3, CHARACTERIZATION OF NTPASE ACTIVITY, RTPASE ACTIVITY, MUTAGENESIS OF LYS-415 AND LSY-419.
  5. "Reovirus nonstructural protein mu NS recruits viral core surface proteins and entering core particles to factory-like inclusions."
    Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L., Parker J.S.L.
    J. Virol. 78:1882-1892(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMU2_REOVL
AccessioniPrimary (citable) accession number: Q00335
Secondary accession number(s): Q8QT11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 1992
Last sequence update: November 30, 1992
Last modified: January 6, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.