ID   MU2_REOVD               Reviewed;         736 AA.
AC   P12418; A4ZY23; Q71M35; Q8QT10;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Microtubule-associated protein mu-2;
DE            Short=Mu2;
GN   Name=M1;
OS   Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX   NCBI_TaxID=10886;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2523177; DOI=10.1016/0042-6822(89)90154-2;
RA   Wiener J.R., Bartlett J.A., Joklik W.K.;
RT   "The sequences of reovirus serotype 3 genome segments M1 and M3 encoding
RT   the minor protein mu 2 and the major nonstructural protein mu NS,
RT   respectively.";
RL   Virology 169:293-304(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   PRO-208.
RC   STRAIN=Isolate T3/Human/Ohio/1955;
RX   PubMed=11932414; DOI=10.1128/jvi.76.9.4483-4496.2002;
RA   Parker J.S.L., Broering T.J., Kim J., Higgins D.E., Nibert M.L.;
RT   "Reovirus core protein mu2 determines the filamentous morphology of viral
RT   inclusion bodies by interacting with and stabilizing microtubules.";
RL   J. Virol. 76:4483-4496(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate T3/Human/Washington;
RX   PubMed=15507160; DOI=10.1186/1743-422x-1-6;
RA   Yin P., Keirstead N.D., Broering T.J., Arnold M.M., Parker J.S.L.,
RA   Nibert M.L., Coombs K.M.;
RT   "Comparisons of the M1 genome segments and encoded mu2 proteins of
RT   different reovirus isolates.";
RL   Virol. J. 1:6-6(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Infectious clone;
RX   PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA   Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA   Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA   Wilson G.J., Chappell J.D., Dermody T.S.;
RT   "A plasmid-based reverse genetics system for animal double-stranded RNA
RT   viruses.";
RL   Cell Host Microbe 1:147-157(2007).
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:0000269|PubMed:11932414}. Note=Found in the inner
CC       capsid (12 copies).
CC   -!- SIMILARITY: Belongs to the orthoreovirus mu-2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; M27261; AAA47256.1; -; Genomic_RNA.
DR   EMBL; AF461683; AAL99937.1; -; mRNA.
DR   EMBL; AF461684; AAL99938.1; -; mRNA.
DR   EMBL; AY551083; AAS55892.1; -; mRNA.
DR   EMBL; EF494438; ABP48916.1; -; Genomic_RNA.
DR   PIR; A30179; M4XR3D.
DR   SMR; P12418; -.
DR   IntAct; P12418; 9.
DR   PRIDE; P12418; -.
DR   Proteomes; UP000006373; Genome.
DR   Proteomes; UP000165799; 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:suppression 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   1: Evidence at protein level;
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; Reference proteome; Viral immunoevasion;
KW   Virion.
FT   CHAIN           1..736
FT                   /note="Microtubule-associated protein mu-2"
FT                   /id="PRO_0000222746"
FT   MUTAGEN         208
FT                   /note="P->S: Loss of filamentous subcellular location."
FT                   /evidence="ECO:0000269|PubMed:11932414"
FT   CONFLICT        150
FT                   /note="R -> Q (in Ref. 2; AAL99937, 3; AAS55892 and 4;
FT                   ABP48916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="P -> S (in Ref. 2; AAL99937, 3; AAS55892 and 4;
FT                   ABP48916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="Q -> R (in Ref. 4; ABP48916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="M -> I (in Ref. 2; AAL99937, 3; AAS55892 and 4;
FT                   ABP48916)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   736 AA;  83276 MW;  2CF0D88BA16EF564 CRC64;
     MAYIAVPAVV DSRSSEAIGL LESFGVDAGA DANDVSYQDH DYVLDQLQYM LDGYEAGDVI
     DALVHKNWLH HSVYCLLPPK SQLLEYWKSN PSAIPDNVDR RLRKRLMLKK DLRKDDEYNQ
     LARAFKISDV YAPLISSTTS PMTMIQNLNR GEIVYTTTDR VIGARILLYA PRKYYASTLS
     FTMTKCIIPF GKEVGRVPHS RFNVGTFPSI ATPKCFVMSG VDIESIPNEF IKLFYQRVKS
     VHANILNDIS PQIVSDMINR KRLRVHTPSD RRAAQLMHLP YHVKRGASHV DVYKVDVVDM
     LFEVVDVADG LRNVSRKLTM HTVPVCILEM LGIEIADYCI RQEDGMLTDW FLLLTMLSDG
     LTDRRTHCQY LMNPSSVPPD VILNISITGF INRHTIDVMP DIYDFVKPIG AVLPKGSFKS
     TIMRVLDSIS ILGIQIMPRA HVVDSDEVGE QMEPTFEQAV MEIYKGIAGV DSLDDLIKWV
     LNSDLIPHDD RLGQLFQAFL PLAKDLLAPM ARKFYDNSMS EGRLLTFAHA DSELLNANYF
     GHLLRLKIPY ITEVNLMIRK NREGGELFQL VLSYLYKMYA TSAQPKWFGS LLRLLICPWL
     HMEKLIGEAD PASTSAEIGW HIPREQLMQD GWCGCEDGFI PYVSIRAPRL VIEELMEKNW
     GQYHAQVIVT DQLVVGEPRR VSAKAVIKGN HLPVKLVSRF ACFTLTAKYE MRLSCGHSTG
     RGAAYSARLA FRSDLA