P04506 (SIGM1_REOVL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 82.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Outer capsid protein sigma-1 Short name=Sigma1 Alternative name(s): Cell attachment protein Hemagglutinin | ||
| Gene names |
| ||
| Organism | Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1) [Reference proteome] | ||
| Taxonomic identifier | 10884 [NCBI] | ||
| Taxonomic lineage | Viruses › dsRNA viruses › Reoviridae › Spinareovirinae › Orthoreovirus › ![]() | ||
| Virus host | Mammalia [TaxID: 40674] |
Protein attributes
| Sequence length | 470 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis By similarity. |
| Subunit structure | Homotrimer. Interacts (via the head region) with human F11R By similarity. |
| Subcellular location | Virion By similarity. Note: Found in the outer capsid (36 copies) By similarity. |
| Post-translational modification | Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway By similarity. |
| Sequence similarities | Belongs to the orthoreovirus sigma-1 protein family. |
| Sequence caution | The sequence AAA47276.1 differs from that shown. Reason: Frameshift at position 410. The sequence AAA66877.1 differs from that shown. Reason: Frameshift at positions 410 and 434. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Viral attachment to host cell Virus entry into host cell |
| Cellular component | Virion |
| Domain | Coiled coil |
| Molecular function | Capsid protein Hemagglutinin |
| PTM | Glycoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell adhesion Inferred from electronic annotation. Source: InterPro viral attachment to host cellInferred from electronic annotation. Source: UniProtKB-KW viral entry into host cellInferred from electronic annotation. Source: UniProtKB-KW viral infectious cycleInferred from electronic annotation. Source: InterPro |
| Cellular_component | viral capsid Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 470 | 470 | Outer capsid protein sigma-1 | PRO_0000040667 | ||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1 – 324 | 324 | Tail | |||||||||||||||||||||||||||||||||||||||||||
| Region | 325 – 470 | 146 | Head | |||||||||||||||||||||||||||||||||||||||||||
| Coiled coil | 26 – 46 | 21 | Potential | |||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 21 | 1 | N-linked (GlcNAc...); by host Potential | |||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 121 | 1 | N-linked (GlcNAc...); by host Potential | |||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 205 | 1 | N-linked (GlcNAc...); by host Potential | |||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 353 | 1 | N-linked (GlcNAc...); by host Potential | |||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 91 | 1 | V → G in AAA66877. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 91 | 1 | V → G in AAA47276. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 169 | 1 | S → F in AAA66877. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 384 | 1 | V → L in AAA47276. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 409 | 1 | L → W in AAA47242. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 274 – 278 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 281 – 285 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 290 – 292 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 293 – 296 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 299 – 304 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 315 – 318 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 319 – 322 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 323 – 326 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 328 – 331 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 333 – 345 | 13 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 348 – 361 | 14 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 364 – 369 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 372 – 375 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 379 – 386 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 397 – 400 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 409 – 419 | 11 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 421 – 437 | 17 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 440 – 447 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 454 – 458 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 461 – 466 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Sequences of the S1 genes of the three serotypes of reovirus." Cashdollar L.W., Chmelo R.A., Wiener J.R., Joklik W.K. Proc. Natl. Acad. Sci. U.S.A. 82:24-28(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning and nucleotide sequence of the reovirus serotype 1 Lang strain bicistronic s1 mRNA which encodes the minor capsid polypeptide sigma 1a and the nonstructural polypeptide sigma 1bNS." Munemitsu S.M., Atwater J.A., Samuel C.E. Biochem. Biophys. Res. Commun. 140:508-514(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [3] | "Identification of conserved domains in the cell attachment proteins of the three serotypes of reovirus." Duncan R., Horne D., Cashdollar L.W., Joklik W.K., Lee P.W.K. Virology 174:399-409(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [4] | "Structure of the reovirus cell-attachment protein: a model for the domain organization of sigma 1." Nibert M.L., Dermody T.S., Fields B.N. J. Virol. 64:2976-2989(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [5] | "A plasmid-based reverse genetics system for animal double-stranded RNA viruses." Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., Wilson G.J., Chappell J.D., Dermody T.S. Cell Host Microbe 1:147-157(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Infectious clone. |
| [6] | "Nature of the 3'-terminal sequences of the plus and minus strands of the S1 gene of reovirus serotypes 1, 2 and 3." Li J.K.-K., Keene J.D., Scheible P.P., Joklik W.K. Virology 105:41-51(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M10260 Genomic RNA. Translation: AAA66877.1. Frameshift. M14779 Genomic RNA. Translation: AAA47276.1. Frameshift. M32860 Genomic RNA. Translation: AAA47267.1. M35963 Genomic RNA. Translation: AAA47242.1. EF494445 Genomic RNA. Translation: ABP48923.1. AH002406 Genomic RNA. Translation: AAA47240.1. | ||||||||||||||||||
| PIR | HMXRH1. A04122. HMXRL1. A34829. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P04506. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 2.10.25.20. 1 hit. 2.60.90.20. 1 hit. | ||||||||||||||||||
| InterPro | IPR008982. Adenovirus_pIV-rel_att. IPR009013. Attachment_protein_shaft_dom. IPR027314. Sigma1_globular_dom. IPR002592. Vir_attach_sigma1_reovir. [Graphical view] | ||||||||||||||||||
| Pfam | PF01664. Reo_sigma1. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF49835. Viral_att. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | SIGM1_REOVL | ||||||||
| Accession | Primary (citable) accession number: P04506 Secondary accession number(s): A4ZY30, P07937 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
