MU2_REOVL
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 03-AUG-2022, entry version 72.
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; Reoviridae; Spinareovirinae; 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: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_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
