Reviewed, UniProtKB/Swiss-Prot P03528 (SIGM1_REOVD)

Names and origin

Protein names

Recommended name:
    Outer capsid protein sigma-1
      Short name=Sigma1
Alternative name(s):
    Hemagglutinin
    Cell attachment protein

Gene names

Name:

S1

Organism

Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [Complete proteome]

Taxonomic identifier

10886 [NCBI]

Taxonomic lineage

Viruses › dsRNA viruses › Reoviridae › Spinareovirinae › Orthoreovirus

Virus host

Mammalia [TaxID: 40674]

Protein attributes

Sequence length	455 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.
Subunit structure	Homotrimer. Interacts (via the head region) with human F11R. Ref.6
Subcellular location	Virion. Note: Found in the outer capsid (36 copies).
Post-translational modification	Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.
Sequence similarities	Belongs to the orthoreovirus sigma-1 protein family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Capsid protein Virion
Domain	Coiled coil
Molecular function	Hemagglutinin
PTM	Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: InterPro cell recognition Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW viral infectious cycle Inferred 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 – 455

455

Outer capsid protein sigma-1

PRO_0000040665

Regions

Region

1 – 307

307

Tail

Region

308 – 455

148

Head

Coiled coil

116 – 148

33

Potential

Amino acid modifications

Glycosylation

231

1

N-linked (GlcNAc...); by host Potential

Glycosylation

264

1

N-linked (GlcNAc...); by host Potential

Glycosylation

282

1

N-linked (GlcNAc...); by host Potential

Experimental info

Sequence conflict

22

1

A → V in ABP48919. Ref.5

Sequence conflict

118 – 119

2

EL → DV in CAA25605. Ref.3

Sequence conflict

118 – 119

2

EL → DV in AAA47274. Ref.4

Sequence conflict

163

1

S → T in AAA47275. Ref.2

Sequence conflict

408

1

A → T in ABP48919. Ref.5

Secondary structure

1

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455

Helix Strand Turn

Details...

Beta strand

261 – 264

4

Turn

265 – 267

3

Beta strand

270 – 272

3

Turn

276 – 278

3

Beta strand

279 – 281

3

Beta strand

287 – 289

3

Beta strand

300 – 303

4

Beta strand

306 – 309

4

Helix

311 – 314

4

Beta strand

316 – 328

13

Beta strand

331 – 344

14

Beta strand

347 – 352

6

Beta strand

355 – 358

4

Beta strand

362 – 369

8

Beta strand

372 – 374

3

Helix

380 – 383

4

Turn

386 – 389

4

Beta strand

394 – 408

15

Beta strand

410 – 422

13

Beta strand

425 – 431

7

Beta strand

439 – 443

5

Beta strand

446 – 452

7

Sequences

	Sequence		Length	Mass (Da)
	P03528-1 [UniParc]. Last modified July 22, 2008. Version 3. Checksum: F376721B9F936A34	FASTA	455	49,095
	10 20 30 40 50 60 MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT QGLDDANKRI 70 80 90 100 110 120 IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS SVTQLGARVG QLETGLAELR 130 140 150 160 170 180 VDHDNLVARV DTAERNIGSL TTELSTLTLR VTSIQADFES RISTLERTAV TSAGAPLSIR 190 200 210 220 230 240 NNRMTMGLND GLTLSGNNLA IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD 250 260 270 280 290 300 SINSRIGATE QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI 310 320 330 340 350 360 ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI CLPAFDGFSI 370 380 390 400 410 420 ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA IGLSSGGAPQ YMSKNLWVEQ 430 440 450 WQDGVLRLRV EGGGSITHSN SKWPAMTVSY PRSFT

References

[1]	"Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral cell attachment protein sigma 1." Nagata L., Masri S.A., Mah D.C.W., Lee P.W.K. Nucleic Acids Res. 12:8699-8710(1984) [PubMed: 6095208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"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: 3855545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of reovirus haemagglutinin predicts a coiled-coil structure." Bassel-Duby R., Jayasuriya A.K., Chatterjee D., Sonenberg N., Maizel J.V. Jr., Fields B.N. Nature 315:421-423(1985) [PubMed: 4000269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]	"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: 2305549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 18005692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Infectious clone.
[6]	"Junction adhesion molecule is a receptor for reovirus." Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y., Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S. Cell 104:441-451(2001) [PubMed: 11239401] [Abstract] Cited for: INTERACTION WITH HUMAN F11R.
[7]	"Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber." Chappell J.D., Prota A.E., Dermody T.S., Stehle T. EMBO J. 21:1-11(2002) [PubMed: 11782420] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 246-455.
[8]	"The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change." Schelling P., Guglielmi K.M., Kirchner E., Paetzold B., Dermody T.S., Stehle T. J. Biol. Chem. 282:11582-11589(2007) [PubMed: 17303562] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 292-455.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.

PIR

S25234.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KKE	X-ray	2.60	A/B/C	246-455	[»]
2OJ5	X-ray	1.75	A/B/C/D/E/F	293-455	[»]
2OJ6	X-ray	1.85	A/B/C/D/E/F	293-455	[»]
3EOY	X-ray	3.40	A/B/C/D/E/F	293-455	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR002592. Vir_attach_sigma1_reovir.
IPR008982. Viral_att.
IPR009013. Viral_attachment_fibre_shaft.
[Graphical view]

Pfam

PF01664. Reo_sigma1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SIGM1_REOVD

Accession

Primary (citable) accession number: P03528
Secondary accession number(s): A4ZY26, Q85668

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 22, 2008
Last modified:	December 15, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)