ID   MU2_REOVJ               Reviewed;         736 AA.
AC   Q91PK4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Microtubule-associated protein mu-2;
DE            Short=Mu2;
GN   Name=M1;
OS   Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Spinareoviridae; Orthoreovirus; Mammalian orthoreovirus.
OX   NCBI_TaxID=10885;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Yin P., Keirstead N.D., Coombs K.M.;
RT   "Sequence analysis of the reovirus Type 2 Jones M1 gene.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Minor inner capsid (core) component. Displays NTPase and RNA
CC       5'-triphosphatase (RTPase) activities. ATP is the preferred substrate
CC       for hydrolysis. May function as a cofactor of polymerase lambda-3.
CC       Associates with microtubules and plays a role in the formation,
CC       structural organization and morphology of viral inclusions, where the
CC       assembly of cores and the replication of viral RNA occur. Together with
CC       mu-NS, recruits the other core proteins to these inclusions (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with protein mu-NS; in viral inclusions. Interacts
CC       with polymerase lambda-3; this interaction stimulates the ATPase
CC       activity of mu-2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm, host
CC       cytoskeleton {ECO:0000250}. Note=Found in the inner capsid (12 copies).
CC       Associates with microtubules (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the orthoreovirus mu-2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF124519; AAK54467.1; -; Genomic_RNA.
DR   SMR; Q91PK4; -.
DR   Proteomes; UP000006370; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0039560; P:disruption by virus of host JAK-STAT cascade via inhibition of host IRF9 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR012494; Reovirus_Mu2.
DR   Pfam; PF07781; Reovirus_Mu2; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; Host cytoskeleton; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host IRF9 by virus; Interferon antiviral system evasion;
KW   Viral immunoevasion; Virion.
FT   CHAIN           1..736
FT                   /note="Microtubule-associated protein mu-2"
FT                   /id="PRO_0000345001"
SQ   SEQUENCE   736 AA;  84004 MW;  C200281480E2FAA7 CRC64;
     MAYVAVPAVV DSRSSEAIGL LESFGVTATK EESDVQYQDH DYVLDQLQYM LDGYEAGDVI
     DALVYRNWLH ESVYCLLPPK SQLLEYWKSN PAVIPESVDR RLRKRLMMKK DLRKDDEYNQ
     LVRAFKLSDV YTPLVSSSTS PMTMIQSINQ NQIVYSTTDR VIGARISLYA PRKYYSATLS
     FTLNRCIIPY GKNVAPIGHA RFNIGTFPSL ASPKCFVLSS VDIESIPNEF IKLFYQRVRS
     VHANILNDIS PQLLSDMLQR KRLRVSSPNE RKIAQIMHLP YHVKRGATHV DVYRVDVVDV
     LFEVVDIKDG LRSVSRKLTL QTVPVSVIEL IGLETADYCI RKENGMFTDW FLLLTMLSDG
     LIDRRTHSQY LINPSSIPPD VIINIYVSGF TNRRVIDVMP EMYDFVKPIG AVLPKGSFKS
     TIMRVLDEME VLGVRIMPRC HVVDSDEVGE RMQPTFEHAV MEIYKGIAGV DSLEELINWV
     LGPDLIPHDE RLGKLYQSFL PLAKDLLAPV ARHFYEESLS EGRLLTFAHA DSELLNANYF
     GHLLRLKIPF ITEVNLMIRK NREGGELFQL VLSYLYKMYA TSAQPMWFGS LLRLMICPWL
     HMEKLIGDAD AAITSAEVGW HIPKEHLMQD GWCGCEDGFI TYVVIRAPKL VLEELREKNW
     GQYHAQVIVT DRLEVGEPRR VHARVVIKGN HMPSKLISRY ACFSLTMRYM MHLTCGHSIG
     RSSAYGARLV FRSSLA
//