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P04507

- SIGM1_REOVJ

UniProt

P04507 - SIGM1_REOVJ

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Protein

Outer capsid protein sigma-1

Gene

S1

Organism
Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 (By similarity).By similarity

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. viral entry into host cell Source: UniProtKB-KW
  3. virion attachment to host cell Source: UniProtKB-KW
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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
Taxonomic identifieri10885 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000006370: Genome

Subcellular locationi

Virion By similarity
Note: Found in the outer capsid (36 copies).By similarity

GO - Cellular componenti

  1. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Outer capsid protein sigma-1PRO_0000040666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi237 – 2371N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi243 – 2431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...); by hostSequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotrimer. Interacts (via the head region) with human F11R (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP04507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 317317TailAdd
BLAST
Regioni318 – 462145HeadAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili18 – 4932Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.60.90.20. 1 hit.
InterProiIPR008982. Adenovirus_pIV-rel_att.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamiPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMiSSF49835. SSF49835. 1 hit.

Sequencei

Sequence statusi: Complete.

P04507-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDLVQLIRR EILLLTGNGE SANSKHEIEE IKKQIKDISA DVNRISNIVD
60 70 80 90 100
SIQGQLGGLS VRVSAIESGV SENGNRIDRL ERDVSGISAS VSGIDSRLSE
110 120 130 140 150
LGDRVNVAEQ RIGQLDTVTD NLLERASRLE TEVSAITNDL GSLNTRVTTE
160 170 180 190 200
LNDVRQTIAA IDTRLTTLET DAVTSVGQGL QKTGNSIKVI VGTGMWFDRN
210 220 230 240 250
NVLQLFLSNQ QKGLGFIDNG MVVKIDTQYF SFDSNGNITL NNNISGLPAR
260 270 280 290 300
TGSLEASRID VVAPPLVIQS TGSTRLLRLM YEAVDFVVTN NVLTLRNRSV
310 320 330 340 350
TPTFKFPLEL NSADNSVSIH RNYRIRLGQW SGQLEYHTPS LRWNAPVTVN
360 370 380 390 400
LMRVDDWLIL SFTRFSTSGI LASGKFVLNF VTGLSPGWAT GSTEPSTTTN
410 420 430 440 450
PLSTTFAAIQ FINGSSRVDA FRILGVAEWN AGELEITNHG GTYTAHTNVD
460
WAPMTIMYPC LG
Length:462
Mass (Da):50,466
Last modified:July 22, 2008 - v3
Checksum:i87383752835EEA8F
GO

Sequence cautioni

The sequence AAA66879.1 differs from that shown. Reason: Frameshift at positions 370 and 415.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471V → L in AAA47268. (PubMed:2305549)Curated
Sequence conflicti207 – 2071L → V in AAA47251. (PubMed:2335823)Curated
Sequence conflicti439 – 4391H → Y in AAA47251. (PubMed:2335823)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10261 Genomic RNA. Translation: AAA66879.1. Frameshift.
M32861 Genomic RNA. Translation: AAA47268.1.
M35964 Genomic RNA. Translation: AAA47251.1.
PIRiA04123. HMXRH2.
C34829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10261 Genomic RNA. Translation: AAA66879.1 . Frameshift.
M32861 Genomic RNA. Translation: AAA47268.1 .
M35964 Genomic RNA. Translation: AAA47251.1 .
PIRi A04123. HMXRH2.
C34829.

3D structure databases

ProteinModelPortali P04507.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.90.20. 1 hit.
InterProi IPR008982. Adenovirus_pIV-rel_att.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view ]
Pfami PF01664. Reo_sigma1. 1 hit.
[Graphical view ]
SUPFAMi SSF49835. SSF49835. 1 hit.
ProtoNeti Search...

Publicationsi

  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. "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].
  3. "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].

Entry informationi

Entry nameiSIGM1_REOVJ
AccessioniPrimary (citable) accession number: P04507
Secondary accession number(s): Q85663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 22, 2008
Last modified: October 1, 2014
This is version 85 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3