ID   MU2_REOVL               Reviewed;         736 AA.
AC   Q00335; Q8QT11;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Microtubule-associated protein mu-2;
DE            Short=Mu2;
GN   Name=M1;
OS   Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Spinareoviridae; Orthoreovirus; Mammalian orthoreovirus.
OX   NCBI_TaxID=10884;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1566600; DOI=10.1016/0168-1702(92)90042-8;
RA   Zou S., Brown E.G.;
RT   "Nucleotide sequence comparison of the M1 genome segment of reovirus type 1
RT   Lang and type 3 Dearing.";
RL   Virus Res. 22:159-164(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   INTERACTION WITH PROTEIN MU-NS.
RX   PubMed=12663763; DOI=10.1128/jvi.77.8.4566-4576.2003;
RA   Miller C.L., Broering T.J., Parker J.S.L., Arnold M.M., Nibert M.L.;
RT   "Reovirus sigma NS protein localizes to inclusions through an association
RT   requiring the mu NS amino terminus.";
RL   J. Virol. 77:4566-4576(2003).
RN   [4]
RP   INTERACTION WITH POLYMERASE LAMBDA-3, CHARACTERIZATION OF NTPASE ACTIVITY,
RP   RTPASE ACTIVITY, AND MUTAGENESIS OF LYS-415 AND LYS-419.
RX   PubMed=14613938; DOI=10.1074/jbc.m308637200;
RA   Kim J., Parker J.S.L., Murray K.E., Nibert M.L.;
RT   "Nucleoside and RNA triphosphatase activities of orthoreovirus
RT   transcriptase cofactor mu2.";
RL   J. Biol. Chem. 279:4394-4403(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=14747553; DOI=10.1128/jvi.78.4.1882-1892.2004;
RA   Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L.,
RA   Parker J.S.L.;
RT   "Reovirus nonstructural protein mu NS recruits viral core surface proteins
RT   and entering core particles to factory-like inclusions.";
RL   J. Virol. 78:1882-1892(2004).
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.
CC       {ECO:0000269|PubMed:14747553}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
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. {ECO:0000269|PubMed:12663763,
CC       ECO:0000269|PubMed:14613938}.
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; X59945; CAA42570.1; -; Genomic_RNA.
DR   EMBL; AF461682; AAL99936.1; -; mRNA.
DR   PIR; S23654; S23654.
DR   SMR; Q00335; -.
DR   IntAct; Q00335; 15.
DR   Proteomes; UP000007253; 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   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; Interferon antiviral system evasion;
KW   Reference proteome; Viral immunoevasion; Virion.
FT   CHAIN           1..736
FT                   /note="Microtubule-associated protein mu-2"
FT                   /id="PRO_0000222747"
FT   MUTAGEN         415
FT                   /note="K->A: Loss of ATPase activity; when associated with
FT                   A-419. No effect on microtubules association."
FT                   /evidence="ECO:0000269|PubMed:14613938"
FT   MUTAGEN         419
FT                   /note="K->A: Loss of ATPase activity; when associated with
FT                   A-415. No effect on microtubules association."
FT                   /evidence="ECO:0000269|PubMed:14613938"
FT   CONFLICT        302
FT                   /note="L -> F (in Ref. 2; AAL99936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   736 AA;  83266 MW;  41508441FA4FA784 CRC64;
     MAYIAVPAVV DSRSSEAIGL LESFGVDAGA DANDVSYQDH DYVLDQLQYM LDGYEAGDVI
     DALVHKNWLH HSVYCLLPPK SQLLEYWKSN PSVIPDNVDR RLRKRLMLKK DLRKDDEYNQ
     LARAFKISDV YAPLISSTTS PMTMIQNLNQ GEIVYTTTDR VIGARILLYA PRKYYASTLS
     FTMTKCIIPF GKEVGRVPHS RFNVGTFPSI ATPKCFVMSG VDIESIPNEF IKLFYQRVKS
     VHANILNDIS PQIVSDMINR KRLRVHTPSD RRAAQLMHLP YHVKRGASHV DVYKVDVVDV
     LLEVVDVADG LRNVSRKLTM HTVPVCILEM LGIEIADYCI RQEDGMFTDW FLLLTMLSDG
     LTDRRTHCQY LINPSSVPPD VILNISITGF INRHTIDVMP DIYDFVKPIG AVLPKGSFKS
     TIMRVLDSIS ILGVQIMPRA HVVDSDEVGE QMEPTFEHAV MEIYKGIAGV DSLDDLIKWV
     LNSDLIPHDD RLGQLFQAFL PLAKDLLAPM ARKFYDNSMS EGRLLTFAHA DSELLNANYF
     GHLLRLKIPY ITEVNLMIRK NREGGELFQL VLSYLYKMYA TSAQPKWFGS LLRLLICPWL
     HMEKLIGEAD PASTSAEIGW HIPREQLMQD GWCGCEDGFI PYVSIRAPRL VMEELMEKNW
     GQYHAQVIVT DQLVVGEPRR VSAKAVIKGN HLPVKLVSRF ACFTLTAKYE MRLSCGHSTG
     RGAAYNARLA FRSDLA
//