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UniProtKB - P03528 (SIGM1_REOVD)
Protein
Outer capsid protein sigma-1
Gene
S1
Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
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
- cell adhesion Source: InterPro
- viral entry into host cell Source: UniProtKB-KW
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Molecular function | Hemagglutinin |
Biological process | Host-virus interaction, Viral attachment to host cell, Virus entry into host cell |
Names & Taxonomyi
Protein namesi | Recommended name: Outer capsid protein sigma-1Short name: Sigma1 Alternative name(s): Cell attachment protein Hemagglutinin |
Gene namesi | Name:S1 |
Organismi | Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) |
Taxonomic identifieri | 10886 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Duplornaviricota › Resentoviricetes › Reovirales › Reoviridae › Spinareovirinae › Orthoreovirus › |
Virus hosti | Mammalia [TaxID: 40674] |
Proteomesi |
|
Subcellular locationi
- Virion Note: Found in the outer capsid (36 copies).
Keywords - Cellular componenti
Capsid protein, Outer capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000040665 | 1 – 455 | Outer capsid protein sigma-1Add BLAST | 455 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 231 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 264 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 282 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 |
Post-translational modificationi
Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.
Keywords - PTMi
GlycoproteinInteractioni
Subunit structurei
Homotrimer.
Interacts (via the head region) with human F11R.
1 PublicationChemistry databases
BindingDBi | P03528 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P03528 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03528 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 307 | TailAdd BLAST | 307 | |
Regioni | 308 – 455 | HeadAdd BLAST | 148 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 116 – 148 | Sequence analysisAdd BLAST | 33 |
Sequence similaritiesi
Belongs to the orthoreovirus sigma-1 protein family.Curated
Keywords - Domaini
Coiled coilFamily and domain databases
InterProi | View protein in InterPro IPR008982, Adenovirus_pIV-like_att IPR009013, Attachment_protein_shaft_sf IPR002592, Vir_attach_sigma1_reovir |
Pfami | View protein in Pfam PF01664, Reo_sigma1, 1 hit |
SUPFAMi | SSF49835, SSF49835, 1 hit SSF51225, SSF51225, 1 hit |
i Sequence
Sequence statusi: Complete.
P03528-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 22 | A → V in ABP48919 (PubMed:18005692).Curated | 1 | |
Sequence conflicti | 118 – 119 | EL → DV in CAA25605 (PubMed:4000269).Curated | 2 | |
Sequence conflicti | 118 – 119 | EL → DV in AAA47274 (PubMed:2305549).Curated | 2 | |
Sequence conflicti | 163 | S → T in AAA47275 (PubMed:3855545).Curated | 1 | |
Sequence conflicti | 408 | A → T in ABP48919 (PubMed:18005692).Curated | 1 |
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 |
PIRi | S25234 |
Similar proteinsi
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 |
PIRi | S25234 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
3S6X | X-ray | 2.25 | A/B/C | 170-455 | [»] | |
3S6Y | X-ray | 2.79 | A/B/C | 170-455 | [»] | |
3S6Z | X-ray | 2.28 | A/B/C | 170-455 | [»] | |
6GAP | X-ray | 2.15 | A/B/C | 25-262 | [»] | |
SMRi | P03528 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
BindingDBi | P03528 |
Protocols and materials databases
ABCDi | P03528, 1 sequenced antibody |
Miscellaneous databases
EvolutionaryTracei | P03528 |
Family and domain databases
InterProi | View protein in InterPro IPR008982, Adenovirus_pIV-like_att IPR009013, Attachment_protein_shaft_sf IPR002592, Vir_attach_sigma1_reovir |
Pfami | View protein in Pfam PF01664, Reo_sigma1, 1 hit |
SUPFAMi | SSF49835, SSF49835, 1 hit SSF51225, SSF51225, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SIGM1_REOVD | |
Accessioni | P03528Primary (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: | June 2, 2021 | |
This is version 125 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families