ID SIGM1_REOVL Reviewed; 470 AA. AC P04506; A4ZY30; P07937; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 08-NOV-2023, entry version 116. 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 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Spinareoviridae; Orthoreovirus; Mammalian orthoreovirus. OX NCBI_TaxID=10884; 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=2430568; DOI=10.1016/0006-291x(86)90761-8; RA 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 bicistronic RT s1 mRNA which encodes the minor capsid polypeptide sigma 1a and the RT nonstructural polypeptide sigma 1bNS."; RL Biochem. Biophys. Res. Commun. 140:508-514(1986). RN [3] 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 [4] 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). 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 NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21. RX PubMed=6158163; DOI=10.1016/0042-6822(80)90154-3; RA Li J.K.-K., Keene J.D., Scheible P.P., Joklik W.K.; RT "Nature of the 3'-terminal sequences of the plus and minus strands of the RT S1 gene of reovirus serotypes 1, 2 and 3."; RL Virology 105:41-51(1980). 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=AAA47276.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAA66877.1; Type=Frameshift; Evidence={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; M10260; AAA66877.1; ALT_FRAME; Genomic_RNA. DR EMBL; M14779; AAA47276.1; ALT_FRAME; Genomic_RNA. DR EMBL; M32860; AAA47267.1; -; Genomic_RNA. DR EMBL; M35963; AAA47242.1; -; Genomic_RNA. DR EMBL; EF494445; ABP48923.1; -; Genomic_RNA. DR EMBL; AH002406; AAA47240.1; -; Genomic_RNA. DR PIR; A04122; HMXRH1. DR PIR; A34829; HMXRL1. DR PDB; 4GU3; X-ray; 3.60 A; A/B/C=261-470. DR PDB; 4GU4; X-ray; 3.50 A; A/B/C=261-470. DR PDB; 4ODB; X-ray; 3.20 A; A/B/C=308-470. DR PDB; 4XC5; X-ray; 2.20 A; A/B/C=308-470. DR PDB; 5MHS; X-ray; 3.70 A; A/B/C=308-470. DR PDB; 6GAJ; X-ray; 1.35 A; A/B/C=29-159. DR PDB; 6GAK; X-ray; 1.43 A; A/B/C=29-159. DR PDB; 6GAO; X-ray; 2.10 A; A/B/C=29-264. DR PDBsum; 4GU3; -. DR PDBsum; 4GU4; -. DR PDBsum; 4ODB; -. DR PDBsum; 4XC5; -. DR PDBsum; 5MHS; -. DR PDBsum; 6GAJ; -. DR PDBsum; 6GAK; -. DR PDBsum; 6GAO; -. DR SMR; P04506; -. DR GlyCosmos; P04506; 4 sites, No reported glycans. DR ABCD; P04506; 1 sequenced antibody. DR Proteomes; UP000007253; Genome. DR GO; GO:0019028; C:viral capsid; IDA:CACAO. 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; 1.20.1270.70; Designed single chain three-helix bundle; 1. DR Gene3D; 2.60.90.20; Virus attachment protein , globular domain; 1. DR InterPro; IPR008982; Adenovirus_pIV-like_att. DR InterPro; IPR002592; Vir_attach_sigma1_reovir. DR Pfam; PF01664; Reo_sigma1; 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; Reference proteome; KW Viral attachment to host cell; Virion; Virus entry into host cell. FT CHAIN 1..470 FT /note="Outer capsid protein sigma-1" FT /id="PRO_0000040667" FT REGION 1..324 FT /note="Tail" FT REGION 325..470 FT /note="Head" FT COILED 26..46 FT /evidence="ECO:0000255" FT CARBOHYD 21 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 353 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CONFLICT 91 FT /note="V -> G (in Ref. 1; AAA66877 and 2; AAA47276)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="S -> F (in Ref. 1; AAA66877)" FT /evidence="ECO:0000305" FT CONFLICT 384 FT /note="V -> L (in Ref. 2; AAA47276)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="L -> W (in Ref. 4; AAA47242)" FT /evidence="ECO:0000305" FT HELIX 30..156 FT /evidence="ECO:0007829|PDB:6GAJ" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:6GAO" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:6GAO" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:6GAO" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:4GU4" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:4GU4" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:4GU4" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:4GU4" FT STRAND 299..304 FT /evidence="ECO:0007829|PDB:4GU4" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:4XC5" FT TURN 319..322 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:4XC5" FT HELIX 328..331 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 333..345 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 348..361 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 364..369 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 379..386 FT /evidence="ECO:0007829|PDB:4XC5" FT TURN 387..390 FT /evidence="ECO:0007829|PDB:4ODB" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 409..420 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 423..437 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 440..449 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 454..458 FT /evidence="ECO:0007829|PDB:4XC5" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:4XC5" SQ SEQUENCE 470 AA; 51404 MW; F4D18989AD54491C CRC64; MDASLITEIR KIVLQLSVSS NGSQSKEIEE IKKQVQVNVD DIRAANIKLD GLGRQIADIS NSISTIESRL GEMDNRLVGI SSQVTQLSNS VSQNTQSISS LGDRINAVEP RVDSLDTVTS NLTGRTSTLE ADVGSLRTEL AALTTRVTTE VTRLDGLINS GQNSIGELST RLSNVETSMV TTAGRGLQKN GNTLNVIVGN GMWFNSSNQL QLDLSGQSKG VGFVGTGMVV KIDTNYFAYN SNGEITLVSQ INELPSRVST LESAKIDSVL PPLTVREASG VRTLSFGYDT SDFTIINSVL SLRSRLTLPT YRYPLELDTA NNRVQVADRF GMRTGTWTGQ LQYQHPQLSW RANVTLNLMK VDDWLVLSFS QMTTNSIMAD GKFVINFVSG LSSGWQTGDT EPSSTIDPLS TTFAAVQFLN NGQRIDAFRI MGVSEWTDGE LEIKNYGGTY TGHTQVYWAP WTIMYPCNVR //