SIGM2_REOVL
ID SIGM2_REOVL Reviewed; 418 AA.
AC P11314;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Inner capsid protein sigma-2;
DE Short=Sigma2;
GN Name=S2;
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=1920614; DOI=10.1128/jvi.65.11.5721-5731.1991;
RA Dermody T.S., Schiff L.A., Nibert M.L., Coombs K.M., Fields B.N.;
RT "The S2 gene nucleotide sequences of prototype strains of the three
RT reovirus serotypes: characterization of reovirus core protein sigma 2.";
RL J. Virol. 65:5721-5731(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3663211; DOI=10.1016/s0006-291x(87)80190-0;
RA George C.X., Crowe A., Munemitsu S.M., Atwater J.A., Samuel C.E.;
RT "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning
RT and nucleotide sequence of the reovirus serotype 1 Lang strain s2 mRNA
RT which encodes the virion core polypeptide sigma 2.";
RL Biochem. Biophys. Res. Commun. 147:1153-1161(1987).
RN [3]
RP INTERACTION WITH PROTEIN MU-NS.
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).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
RC STRAIN=Reassortant F18;
RX PubMed=10801118; DOI=10.1038/35010041;
RA Reinisch K.M., Nibert M.L., Harrison S.C.;
RT "Structure of the reovirus core at 3.6 A resolution.";
RL Nature 404:960-967(2000).
CC -!- FUNCTION: Inner capsid (core) component.
CC -!- SUBUNIT: Interacts with protein mu-NS; in viral inclusions.
CC {ECO:0000269|PubMed:14747553}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Found in the inner
CC capsid (150 copies).
CC -!- SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47278.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ej6";
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DR EMBL; L19774; AAA47239.1; -; Genomic_RNA.
DR EMBL; M17598; AAA47278.1; ALT_FRAME; mRNA.
DR PIR; A41306; FOXRL2.
DR PDB; 1EJ6; X-ray; 3.60 A; D/E=1-418.
DR PDB; 2CSE; EM; 7.00 A; X/Y/Z=1-418.
DR PDB; 6XF8; EM; 6.50 A; E=2-418.
DR PDB; 6ZTZ; EM; -; D/P=2-418.
DR PDBsum; 1EJ6; -.
DR PDBsum; 2CSE; -.
DR PDBsum; 6XF8; -.
DR PDBsum; 6ZTZ; -.
DR SMR; P11314; -.
DR BindingDB; P11314; -.
DR PRIDE; P11314; -.
DR EvolutionaryTrace; P11314; -.
DR Proteomes; UP000007253; Genome.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR InterPro; IPR004317; Sigma_1_2_reovir.
DR Pfam; PF03084; Sigma_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Inner capsid protein; Reference proteome;
KW Virion.
FT CHAIN 1..418
FT /note="Inner capsid protein sigma-2"
FT /id="PRO_0000222751"
FT CONFLICT 89
FT /note="I -> V (in Ref. 2; AAA47278)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="H -> Y (in Ref. 2; AAA47278)"
FT /evidence="ECO:0000305"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 351..385
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:6ZTZ"
SQ SEQUENCE 418 AA; 47110 MW; 4B30CF9217BA1DDB CRC64;
MARAAFLFKT VGFGGLQNVP INDELSSHLL RAGNSPWQLT QFLDWISLGR GLATSALVPT
AGSRYYQMSC LLSGTLQIPF RPNHRWGDIR FLRLVWSAPT LDGLVVAPPQ VLAQPALQAQ
ADRVYDCDDY PFLARDPRFK HRVYQQLSAV TLLNLTGFGP ISYVRVDEDM WSGDVNQLLM
NYFGHTFAEI AYTLCQASAN RPWEHDGTYA RMTQIILSLF WLSYVGVIHQ QNTYRTFYFQ
CNRRGDAAEV WILSCSLNHS AQIRPGNRSL FVMPTSPDWN MDVNLILSST LTGCLCSGSQ
LPLIDNNSVP AVSRNIHGWT GRAGNQLHGF QVRRMVTEFC DRLRRDGVMT QAQQNQIEAL
ADQTQQFKRD KLEAWAREDD QYNQANPNST MFRTKPFTNA QWGRGNTGAT SAAIAALI
