P04506 · SIGM1_REOVL

Function

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentviral capsid
Cellular Componentviral outer capsid
Biological Processcell adhesion
Biological Processsymbiont entry into host cell
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Outer capsid protein sigma-1
  • Short names
    Sigma1
  • Alternative names
    • Cell attachment protein
    • Hemagglutinin

Gene names

    • Name
      S1

Organism names

Accessions

  • Primary accession
    P04506
  • Secondary accessions
    • A4ZY30
    • P07937

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000406671-470Outer capsid protein sigma-1
Glycosylation21N-linked (GlcNAc...) asparagine; by host
Glycosylation121N-linked (GlcNAc...) asparagine; by host
Glycosylation205N-linked (GlcNAc...) asparagine; by host
Glycosylation353N-linked (GlcNAc...) asparagine; by host

Post-translational modification

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

Keywords

PTM databases

Interaction

Subunit

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

Structure

Family & Domains

Features

Showing features for region, coiled coil.

TypeIDPosition(s)Description
Region1-324Tail
Coiled coil26-46
Region325-470Head

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    470
  • Mass (Da)
    51,404
  • Last updated
    1990-11-01 v2
  • Checksum
    F4D18989AD54491C
MDASLITEIRKIVLQLSVSSNGSQSKEIEEIKKQVQVNVDDIRAANIKLDGLGRQIADISNSISTIESRLGEMDNRLVGISSQVTQLSNSVSQNTQSISSLGDRINAVEPRVDSLDTVTSNLTGRTSTLEADVGSLRTELAALTTRVTTEVTRLDGLINSGQNSIGELSTRLSNVETSMVTTAGRGLQKNGNTLNVIVGNGMWFNSSNQLQLDLSGQSKGVGFVGTGMVVKIDTNYFAYNSNGEITLVSQINELPSRVSTLESAKIDSVLPPLTVREASGVRTLSFGYDTSDFTIINSVLSLRSRLTLPTYRYPLELDTANNRVQVADRFGMRTGTWTGQLQYQHPQLSWRANVTLNLMKVDDWLVLSFSQMTTNSIMADGKFVINFVSGLSSGWQTGDTEPSSTIDPLSTTFAAVQFLNNGQRIDAFRIMGVSEWTDGELEIKNYGGTYTGHTQVYWAPWTIMYPCNVR

Sequence caution

The sequence AAA47276.1 differs from that shown. Reason: Frameshift
The sequence AAA66877.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict91in Ref. 1; AAA66877 and 2; AAA47276
Sequence conflict169in Ref. 1; AAA66877
Sequence conflict384in Ref. 2; AAA47276
Sequence conflict409in Ref. 4; AAA47242

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M10260
EMBL· GenBank· DDBJ
AAA66877.1
EMBL· GenBank· DDBJ
Genomic RNA Frameshift
M14779
EMBL· GenBank· DDBJ
AAA47276.1
EMBL· GenBank· DDBJ
Genomic RNA Frameshift
M32860
EMBL· GenBank· DDBJ
AAA47267.1
EMBL· GenBank· DDBJ
Genomic RNA
M35963
EMBL· GenBank· DDBJ
AAA47242.1
EMBL· GenBank· DDBJ
Genomic RNA
EF494445
EMBL· GenBank· DDBJ
ABP48923.1
EMBL· GenBank· DDBJ
Genomic RNA
AH002406
EMBL· GenBank· DDBJ
AAA47240.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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