SIGM1_REOVD
ID SIGM1_REOVD Reviewed; 455 AA.
AC P03528; A4ZY26; Q85668;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 02-JUN-2021, entry version 125.
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 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10886;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6095208; DOI=10.1093/nar/12.22.8699;
RA Nagata L., Masri S.A., Mah D.C.W., Lee P.W.K.;
RT "Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene
RT which encodes the viral cell attachment protein sigma 1.";
RL Nucleic Acids Res. 12:8699-8710(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=4000269; DOI=10.1038/315421a0;
RA Bassel-Duby R., Jayasuriya A.K., Chatterjee D., Sonenberg N.,
RA Maizel J.V. Jr., Fields B.N.;
RT "Sequence of reovirus haemagglutinin predicts a coiled-coil structure.";
RL Nature 315:421-423(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone;
RX PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA Wilson G.J., Chappell J.D., Dermody T.S.;
RT "A plasmid-based reverse genetics system for animal double-stranded RNA
RT viruses.";
RL Cell Host Microbe 1:147-157(2007).
RN [6]
RP INTERACTION WITH HUMAN F11R.
RX PubMed=11239401; DOI=10.1016/s0092-8674(01)00231-8;
RA Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y.,
RA Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S.;
RT "Junction adhesion molecule is a receptor for reovirus.";
RL Cell 104:441-451(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 246-455.
RX PubMed=11782420; DOI=10.1093/emboj/21.1.1;
RA Chappell J.D., Prota A.E., Dermody T.S., Stehle T.;
RT "Crystal structure of reovirus attachment protein sigma1 reveals
RT evolutionary relationship to adenovirus fiber.";
RL EMBO J. 21:1-11(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 292-455.
RX PubMed=17303562; DOI=10.1074/jbc.m610805200;
RA Schelling P., Guglielmi K.M., Kirchner E., Paetzold B., Dermody T.S.,
RA Stehle T.;
RT "The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised
RT for conformational change.";
RL J. Biol. Chem. 282:11582-11589(2007).
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 -!- SUBUNIT: Homotrimer. Interacts (via the head region) with human F11R.
CC {ECO:0000269|PubMed:11239401}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Found in the outer capsid (36
CC copies).
CC -!- PTM: Undergoes dramatic conformational rearrangements during viral
CC disassembly in the endocytic pathway.
CC -!- SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M10262; AAA47275.1; -; Genomic_DNA.
DR EMBL; X01161; CAA25605.1; -; Genomic_RNA.
DR EMBL; M32862; AAA47274.1; -; mRNA.
DR EMBL; EF494441; ABP48919.1; -; Genomic_RNA.
DR PIR; S25234; S25234.
DR PDB; 1KKE; X-ray; 2.60 A; A/B/C=246-455.
DR PDB; 2OJ5; X-ray; 1.75 A; A/B/C/D/E/F=293-455.
DR PDB; 2OJ6; X-ray; 1.85 A; A/B/C/D/E/F=293-455.
DR PDB; 3EOY; X-ray; 3.40 A; A/B/C/D/E/F=293-455.
DR PDB; 3S6X; X-ray; 2.25 A; A/B/C=170-455.
DR PDB; 3S6Y; X-ray; 2.79 A; A/B/C=170-455.
DR PDB; 3S6Z; X-ray; 2.28 A; A/B/C=170-455.
DR PDB; 6GAP; X-ray; 2.15 A; A/B/C=25-262.
DR PDBsum; 1KKE; -.
DR PDBsum; 2OJ5; -.
DR PDBsum; 2OJ6; -.
DR PDBsum; 3EOY; -.
DR PDBsum; 3S6X; -.
DR PDBsum; 3S6Y; -.
DR PDBsum; 3S6Z; -.
DR PDBsum; 6GAP; -.
DR SMR; P03528; -.
DR BindingDB; P03528; -.
DR ABCD; P03528; 1 sequenced antibody.
DR EvolutionaryTrace; P03528; -.
DR Proteomes; UP000006373; 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; IPR009013; Attachment_protein_shaft_sf.
DR InterPro; IPR002592; Vir_attach_sigma1_reovir.
DR Pfam; PF01664; Reo_sigma1; 1.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Glycoprotein; Hemagglutinin;
KW Host-virus interaction; Outer capsid protein; Reference proteome;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..455
FT /note="Outer capsid protein sigma-1"
FT /id="PRO_0000040665"
FT REGION 1..307
FT /note="Tail"
FT REGION 308..455
FT /note="Head"
FT COILED 116..148
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 22
FT /note="A -> V (in Ref. 5; ABP48919)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="EL -> DV (in Ref. 3; CAA25605 and 4; AAA47274)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> T (in Ref. 2; AAA47275)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="A -> T (in Ref. 5; ABP48919)"
FT /evidence="ECO:0000305"
FT HELIX 28..168
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6GAP"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:6GAP"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:6GAP"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:6GAP"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3S6X"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:3S6X"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3S6X"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3S6X"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3S6X"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3S6X"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2OJ5"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 316..328
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 331..344
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:1KKE"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:2OJ5"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 394..408
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 410..422
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:2OJ5"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:2OJ5"
SQ SEQUENCE 455 AA; 49095 MW; F376721B9F936A34 CRC64;
MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT QGLDDANKRI
IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS SVTQLGARVG QLETGLAELR
VDHDNLVARV DTAERNIGSL TTELSTLTLR VTSIQADFES RISTLERTAV TSAGAPLSIR
NNRMTMGLND GLTLSGNNLA IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD
SINSRIGATE QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI
ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI CLPAFDGFSI
ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA IGLSSGGAPQ YMSKNLWVEQ
WQDGVLRLRV EGGGSITHSN SKWPAMTVSY PRSFT
