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Protein

Outer capsid protein sigma-1

Gene

S1

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein sigma-1
Short name:
Sigma1
Alternative name(s):
Cell attachment protein
Hemagglutinin
Gene namesi
Name:S1
OrganismiReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Taxonomic identifieri10886 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
Proteomesi
  • UP000006373 Componenti: Genome

Subcellular locationi

  • Virion

  • Note: Found in the outer capsid (36 copies).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000406651 – 455Outer capsid protein sigma-1Add BLAST455

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi231N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi264N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi282N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP03528.

Interactioni

Subunit structurei

Homotrimer. Interacts (via the head region) with human F11R.1 Publication

Chemistry databases

BindingDBiP03528.

Structurei

Secondary structure

1455
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi177 – 180Combined sources4
Beta strandi183 – 186Combined sources4
Beta strandi192 – 195Combined sources4
Beta strandi198 – 201Combined sources4
Beta strandi207 – 212Combined sources6
Beta strandi215 – 218Combined sources4
Turni222 – 224Combined sources3
Beta strandi225 – 228Combined sources4
Beta strandi231 – 234Combined sources4
Helixi236 – 239Combined sources4
Helixi240 – 250Combined sources11
Beta strandi261 – 264Combined sources4
Turni265 – 268Combined sources4
Beta strandi269 – 272Combined sources4
Turni276 – 278Combined sources3
Beta strandi279 – 281Combined sources3
Beta strandi287 – 289Combined sources3
Beta strandi300 – 303Combined sources4
Beta strandi306 – 309Combined sources4
Helixi311 – 314Combined sources4
Beta strandi316 – 328Combined sources13
Beta strandi331 – 344Combined sources14
Beta strandi347 – 352Combined sources6
Beta strandi355 – 358Combined sources4
Beta strandi362 – 369Combined sources8
Beta strandi372 – 374Combined sources3
Helixi380 – 383Combined sources4
Turni386 – 389Combined sources4
Beta strandi394 – 408Combined sources15
Beta strandi410 – 422Combined sources13
Beta strandi425 – 431Combined sources7
Beta strandi439 – 443Combined sources5
Beta strandi446 – 452Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKEX-ray2.60A/B/C246-455[»]
2OJ5X-ray1.75A/B/C/D/E/F293-455[»]
2OJ6X-ray1.85A/B/C/D/E/F293-455[»]
3EOYX-ray3.40A/B/C/D/E/F293-455[»]
3S6XX-ray2.25A/B/C170-455[»]
3S6YX-ray2.79A/B/C170-455[»]
3S6ZX-ray2.28A/B/C170-455[»]
ProteinModelPortaliP03528.
SMRiP03528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03528.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 307TailAdd BLAST307
Regioni308 – 455HeadAdd BLAST148

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili116 – 148Sequence analysisAdd BLAST33

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProiIPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamiPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMiSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.

Sequencei

Sequence statusi: Complete.

P03528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT
60 70 80 90 100
QGLDDANKRI IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS
110 120 130 140 150
SVTQLGARVG QLETGLAELR VDHDNLVARV DTAERNIGSL TTELSTLTLR
160 170 180 190 200
VTSIQADFES RISTLERTAV TSAGAPLSIR NNRMTMGLND GLTLSGNNLA
210 220 230 240 250
IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD SINSRIGATE
260 270 280 290 300
QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI
310 320 330 340 350
ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI
360 370 380 390 400
CLPAFDGFSI ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA
410 420 430 440 450
IGLSSGGAPQ YMSKNLWVEQ WQDGVLRLRV EGGGSITHSN SKWPAMTVSY

PRSFT
Length:455
Mass (Da):49,095
Last modified:July 22, 2008 - v3
Checksum:iF376721B9F936A34
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22A → V in ABP48919 (PubMed:18005692).Curated1
Sequence conflicti118 – 119EL → DV in CAA25605 (PubMed:4000269).Curated2
Sequence conflicti118 – 119EL → DV in AAA47274 (PubMed:2305549).Curated2
Sequence conflicti163S → T in AAA47275 (PubMed:3855545).Curated1
Sequence conflicti408A → T in ABP48919 (PubMed:18005692).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.
PIRiS25234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.
PIRiS25234.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKEX-ray2.60A/B/C246-455[»]
2OJ5X-ray1.75A/B/C/D/E/F293-455[»]
2OJ6X-ray1.85A/B/C/D/E/F293-455[»]
3EOYX-ray3.40A/B/C/D/E/F293-455[»]
3S6XX-ray2.25A/B/C170-455[»]
3S6YX-ray2.79A/B/C170-455[»]
3S6ZX-ray2.28A/B/C170-455[»]
ProteinModelPortaliP03528.
SMRiP03528.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP03528.

Proteomic databases

PRIDEiP03528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03528.

Family and domain databases

Gene3Di2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProiIPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamiPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMiSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSIGM1_REOVD
AccessioniPrimary (citable) accession number: P03528
Secondary accession number(s): A4ZY26, Q85668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.