SIGM3_REOVL
ID SIGM3_REOVL Reviewed; 365 AA.
AC P07939;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Outer capsid protein sigma-3;
DE Short=Sigma3;
GN Name=S4;
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=3518713; DOI=10.1016/0006-291x(86)90893-4;
RA Atwater J.A., Manemitsu S.M., Samuel C.E.;
RT "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning
RT and nucleotide sequence of the reovirus serotype 1 Lang strain s4 mRNA
RT which encodes the major capsid surface polypeptide sigma 3.";
RL Biochem. Biophys. Res. Commun. 136:183-192(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1736524; DOI=10.1016/0042-6822(92)90308-c;
RA Seliger L.S., Giantini M., Shatkin A.J.;
RT "Translational effects and sequence comparisons of the three serotypes of
RT the reovirus S4 gene.";
RL Virology 187:202-210(1992).
RN [3]
RP FUNCTION.
RX PubMed=11007773; DOI=10.1074/jbc.m004562200;
RA Farsetta D.L., Chandran K., Nibert M.L.;
RT "Transcriptional activities of reovirus RNA polymerase in recoated cores.
RT Initiation and elongation are regulated by separate mechanisms.";
RL J. Biol. Chem. 275:39693-39701(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MU-1.
RX PubMed=11832217; DOI=10.1016/s0092-8674(02)00612-8;
RA Liemann S., Chandran K., Baker T.S., Nibert M.L., Harrison S.C.;
RT "Structure of the reovirus membrane-penetration protein, Mu1, in a complex
RT with is protector protein, Sigma3.";
RL Cell 108:283-295(2002).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
RX PubMed=16216585; DOI=10.1016/j.str.2005.07.012;
RA Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L.,
RA Baker T.S.;
RT "Features of reovirus outer capsid protein mu1 revealed by electron
RT cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom
RT resolution.";
RL Structure 13:1545-1557(2005).
CC -!- FUNCTION: Stimulates translation by blocking the activation of the
CC dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host
CC interferon response. Sigma3 prevents the activation of EIF2AK2 by
CC competing with the kinase for dsRNA-binding (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: The viral outer shell polypeptides, of which sigma-3 is one,
CC impose structural constraints that prevent elongation of nascent
CC transcripts by the RNA-dependent RNA polymerase lambda-3.
CC {ECO:0000269|PubMed:11007773}.
CC -!- SUBUNIT: Heterohexamer of three sigma-3 and three Mu-1 proteins. The
CC RNA-binding form is probably a homodimer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Found in the outer
CC capsid. Each subunit is positioned with the small lobe anchoring it to
CC the protein mu1 on the surface of the virion, and the large lobe, the
CC site of initial cleavages during entry-related proteolytic disassembly,
CC protruding outwards (By similarity). {ECO:0000250}.
CC -!- PTM: Cleaved during virus the endosomal proteolytic disassembly of the
CC outer capsid. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the orthoreovirus sigma-3 protein family.
CC {ECO:0000305}.
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DR EMBL; M13139; AAA47272.1; -; Genomic_RNA.
DR EMBL; X61586; CAA43783.1; -; Genomic_RNA.
DR PIR; A24245; MNXRS4.
DR PDB; 1JMU; X-ray; 2.80 A; G/H/I=1-365.
DR PDB; 2CSE; EM; 7.00 A; D/E/F/G/H/I/M/N/O/S=1-365.
DR PDB; 6XF8; EM; 6.50 A; G/H/I=1-365.
DR PDB; 6ZTY; EM; -; U/V/W=1-365.
DR PDB; 6ZTZ; EM; -; X/Y/Z=1-365.
DR PDBsum; 1JMU; -.
DR PDBsum; 2CSE; -.
DR PDBsum; 6XF8; -.
DR PDBsum; 6ZTY; -.
DR PDBsum; 6ZTZ; -.
DR SMR; P07939; -.
DR IntAct; P07939; 10.
DR EvolutionaryTrace; P07939; -.
DR Proteomes; UP000007253; Genome.
DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR InterPro; IPR000153; Reo_capsid_sigma3.
DR InterPro; IPR023634; Reovirus_capsid_sigma-3_dom_sf.
DR Pfam; PF00979; Reovirus_cap; 1.
DR SUPFAM; SSF64465; SSF64465; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; 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 PKR by virus; Interferon antiviral system evasion;
KW Metal-binding; Outer capsid protein; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Translation regulation;
KW Viral immunoevasion; Virion; Zinc; Zinc-finger.
FT CHAIN 1..365
FT /note="Outer capsid protein sigma-3"
FT /id="PRO_0000222754"
FT ZN_FING 51..73
FT /note="CCHC-type"
FT /evidence="ECO:0000250"
FT CONFLICT 325
FT /note="D -> N (in Ref. 2; CAA43783)"
FT /evidence="ECO:0000305"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6ZTY"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 319..334
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:1JMU"
SQ SEQUENCE 365 AA; 41156 MW; 859808F2BF92B141 CRC64;
MEVCLPNGHQ IVDLINNAFE GRVSIYSAQE GWDKTISAQP DMMVCGGAVV CMHCLGVVGS
LQRKLKHLPH HRCNQQIRHQ DYVDVQFADR VTAHWKRGML SFVAQMHAMM NDVSPEDLDR
VRTEGGSLVE LNWLQVDPNS MFRSIHSSWT DPLQVVDDLD TKLDQYWTAL NLMIDSSDLV
PNFMMRDPSH AFNGVRLEGD ARQTQFSRTF DSRSSLEWGV MVYDYSELEH DPSKGRAYRK
ELVTPARDFG HFGLSHYSRA TTPILGKMPA VFSGMLTGNC KMYPFIKGTA KLKTVRKLVD
SVNHAWGVEK IRYALGPGGM TGWYDRTMQQ APIVLTPAAL TMFSDTTKFG DLDYPVMIGD
PMILG
