ID   SIGM1_REOVJ             Reviewed;         462 AA.
AC   P04507; Q85663;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 3.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Outer capsid protein sigma-1;
DE            Short=Sigma1;
DE   AltName: Full=Cell attachment protein;
DE   AltName: Full=Hemagglutinin;
GN   Name=S1;
OS   Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX   NCBI_TaxID=10885;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3855545; DOI=10.1073/pnas.82.1.24;
RA   Cashdollar L.W., Chmelo R.A., Wiener J.R., Joklik W.K.;
RT   "Sequences of the S1 genes of the three serotypes of reovirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:24-28(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2305549; DOI=10.1016/0042-6822(90)90093-7;
RA   Duncan R., Horne D., Cashdollar L.W., Joklik W.K., Lee P.W.K.;
RT   "Identification of conserved domains in the cell attachment proteins of the
RT   three serotypes of reovirus.";
RL   Virology 174:399-409(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2335823; DOI=10.1128/jvi.64.6.2976-2989.1990;
RA   Nibert M.L., Dermody T.S., Fields B.N.;
RT   "Structure of the reovirus cell-attachment protein: a model for the domain
RT   organization of sigma 1.";
RL   J. Virol. 64:2976-2989(1990).
CC   -!- FUNCTION: Fiber-like molecule that attaches the virion to the host cell
CC       membrane by binding to the primary receptor F11R/JAM-A and to sialic
CC       acid containing proteins (coreceptor). The interaction of sigma-1 with
CC       F11R is required for NF-kB activation and apoptosis. Binding to both
CC       sialic acid and F11R is required to induce maximal levels of apoptosis
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts (via the head region) with human F11R
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Found in the outer
CC       capsid (36 copies). {ECO:0000250}.
CC   -!- PTM: Undergoes dramatic conformational rearrangements during viral
CC       disassembly in the endocytic pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA66879.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M10261; AAA66879.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; M32861; AAA47268.1; -; Genomic_RNA.
DR   EMBL; M35964; AAA47251.1; -; Genomic_RNA.
DR   PIR; A04123; HMXRH2.
DR   PIR; C34829; C34829.
DR   SMR; P04507; -.
DR   Proteomes; UP000006370; Genome.
DR   GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR008982; Adenovirus_pIV-like_att.
DR   InterPro; IPR002592; Vir_attach_sigma1_reovir.
DR   Pfam; PF01664; Reo_sigma1; 1.
DR   SUPFAM; SSF49835; SSF49835; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Coiled coil; Glycoprotein; Hemagglutinin;
KW   Host-virus interaction; Outer capsid protein;
KW   Viral attachment to host cell; Virion; Virus entry into host cell.
FT   CHAIN           1..462
FT                   /note="Outer capsid protein sigma-1"
FT                   /id="PRO_0000040666"
FT   REGION          1..317
FT                   /note="Tail"
FT   REGION          318..462
FT                   /note="Head"
FT   COILED          18..49
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        147
FT                   /note="V -> L (in Ref. 2; AAA47268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="L -> V (in Ref. 3; AAA47251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="H -> Y (in Ref. 3; AAA47251)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  50466 MW;  87383752835EEA8F CRC64;
     MSDLVQLIRR EILLLTGNGE SANSKHEIEE IKKQIKDISA DVNRISNIVD SIQGQLGGLS
     VRVSAIESGV SENGNRIDRL ERDVSGISAS VSGIDSRLSE LGDRVNVAEQ RIGQLDTVTD
     NLLERASRLE TEVSAITNDL GSLNTRVTTE LNDVRQTIAA IDTRLTTLET DAVTSVGQGL
     QKTGNSIKVI VGTGMWFDRN NVLQLFLSNQ QKGLGFIDNG MVVKIDTQYF SFDSNGNITL
     NNNISGLPAR TGSLEASRID VVAPPLVIQS TGSTRLLRLM YEAVDFVVTN NVLTLRNRSV
     TPTFKFPLEL NSADNSVSIH RNYRIRLGQW SGQLEYHTPS LRWNAPVTVN LMRVDDWLIL
     SFTRFSTSGI LASGKFVLNF VTGLSPGWAT GSTEPSTTTN PLSTTFAAIQ FINGSSRVDA
     FRILGVAEWN AGELEITNHG GTYTAHTNVD WAPMTIMYPC LG