Q5RCW8 · RSAD2_PONAB

Function

function

Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses. Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Activity regulation

IRAK1 and TRAF6 synergistically activate RSAD2 increasing its activity with CTP as substrate about 10-fold.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site83[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site87[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site90[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentGolgi apparatus
Cellular Componentlipid droplet
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial outer membrane
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionlyase activity
Molecular Functionmetal ion binding
Biological ProcessCD4-positive, alpha-beta T cell activation
Biological ProcessCD4-positive, alpha-beta T cell differentiation
Biological Processdefense response to virus
Biological Processinnate immune response
Biological Processnegative regulation of protein secretion
Biological Processpositive regulation of T-helper 2 cell cytokine production
Biological Processpositive regulation of toll-like receptor 7 signaling pathway
Biological Processpositive regulation of toll-like receptor 9 signaling pathway
Biological Processresponse to virus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
  • EC number
  • Short names
    SAND
  • Alternative names
    • Radical S-adenosyl methionine domain-containing protein 2
    • Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible (Viperin)

Gene names

    • Name
      RSAD2

Organism names

Accessions

  • Primary accession
    Q5RCW8

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

Type
IDPosition(s)Description
ChainPRO_00003095851-361S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
Modified residue197N6-acetyllysine
Cross-link206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Acetylated by HAT1. HAT1-mediated acetylation of Lys-197 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation.
'Lys-6'-linked polyubiquitination at Lys-206 leads to RSAD2 protein degradation.

Keywords

Expression

Induction

By interferon type I, type II and LPS.

Interaction

Subunit

Homodimer. Interacts with IRAK1 and TRAF6. Interacts with FPPS. Interacts with HADHB. Interacts (via C-terminus) with VAPA/VAP33 (via C-terminus).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain69-289Radical SAM core

Domain

The N-terminal region (1-42) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet.

Sequence similarities

Belongs to the radical SAM superfamily. RSAD2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    361
  • Mass (Da)
    42,172
  • Last updated
    2004-12-21 v1
  • Checksum
    BC6893B1319A16FA
MWVLTPAAFAEKLLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRTKQQLVLREPDETKEEEEDPPLPATPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVKFCKVELRLPSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRTWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPIRWKVFQCLLIEGENCGEDALREAERFVIDDEEFERSLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKEPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYIWSKADLKLDW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR858150
EMBL· GenBank· DDBJ
CAH90389.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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