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 08-NOV-2023, entry version 130. 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; Spinareoviridae; Orthoreovirus; Mammalian 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 GlyCosmos; P03528; 3 sites, No reported glycans. 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 Gene3D; 1.20.5.340; -; 1. DR Gene3D; 6.10.250.3380; -; 1. DR Gene3D; 6.20.10.20; -; 1. DR Gene3D; 2.60.90.20; Virus attachment protein , globular domain; 1. 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; SSF51225; Fibre shaft of virus attachment proteins; 1. DR SUPFAM; SSF57997; Tropomyosin; 1. DR SUPFAM; SSF49835; Virus attachment protein globular domain; 1. PE 1: Evidence at protein level; KW 3D-structure; 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..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 //