protein

Recombinant Human Double-stranded RNA-specific adenosine deaminase

MBS717263

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Double-stranded RNA-specific adenosine deaminase

Double-stranded RNA-specific adenosine deaminase

136 kDa double-stranded RNA-binding protein; p136; Interferon-inducible protein 4; IFI-4; K88DSRBP

double-stranded RNA-specific adenosine deaminase isoform d; Double-stranded RNA-specific adenosine deaminase; double-stranded RNA-specific adenosine deaminase; adenosine deaminase, RNA-specific; 136 kDa double-stranded RNA-binding protein; p136; Interferon-inducible protein 4; IFI-4; K88DSRBP

ADAR

ADAR; ADAR; DSH; AGS6; G1P1; IFI4; P136; ADAR1; DRADA; DSRAD; IFI-4; K88DSRBP; ADAR1; DSRAD; G1P1; IFI4; DRADA; p136; IFI-4

DSRAD_HUMAN

E Coli

1-176

931

MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSF
LLKQIEFLKGQLPEAPVIGKQTPSLPPSLPGLRPRFPVL
LASSTRGRQVDIRGVPRGVHLGSQGLQRGFQHPSPRGRS
LPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKAT
TAHDLSGKLGTPKKEINRVL

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Transcription

Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication

Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing.Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K.Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994) Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells evidence for two forms of the deaminase.Patterson J.B., Samuel C.E.Mol. Cell. Biol. 15:5376-5388(1995) Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase.Liu Y., George C.X., Patterson J.B., Samuel C.E.J. Biol. Chem. 272:4419-4428(1997) The gene coding for the interferon-inducible human dsRNA adenosine deaminase is transcribed into several messengers specifying different proteins.Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G., Caput D. The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

70167113

NP_001020278.1

NM_001025107.2

P55265

47kD

C6 Deamination Of Adenosine Pathway (1269708); Cytokine Signaling In Immune System Pathway (1269310); Cytosolic DNA-sensing Pathway (125137); Cytosolic DNA-sensing Pathway (124833); Formation Of Editosomes By ADAR Proteins Pathway (1269707); Gene Expression Pathway (1269649); Immune System Pathway (1269170); Influenza A Pathway (217173); Influenza A Pathway (217150); Interferon Signaling Pathway (1269311)

This gene encodes the enzyme responsible for RNA editing by site-specific deamination of adenosines. This enzyme destabilizes double-stranded RNA through conversion of adenosine to inosine. Mutations in this gene have been associated with dyschromatosis symmetrica hereditaria. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2010]

ADAR: Converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. Has been found to modify more frequently adenosines in AU-rich regions, probably due to the relative ease of melting A/U base pairs as compared to G/C pairs. Functions to modify viral RNA genomes and may be responsible for hypermutation of certain negative-stranded viruses. Edits the messenger RNAs for glutamate receptor (GLUR) subunits by site- selective adenosine deamination. Produces low-level editing at the GLUR-B Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Binds to short interfering RNAs (siRNA) without editing them and suppresses siRNA-mediated RNA interference. Binds to ILF3/NF90 and up-regulates ILF3-mediated gene expression. Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed. Homodimer. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. 5 isoforms of the human protein are produced by alternative promoter. Protein type: Nucleolus; RNA-binding; Hydrolase; RNA processing; EC 3.5.4.37. Chromosomal Location of Human Ortholog: 1q21.3. Cellular Component: cytoplasm; membrane; nucleolus; nucleoplasm; nucleus. Molecular Function: DNA binding; double-stranded RNA adenosine deaminase activity; metal ion binding; protein binding. Biological Process: adenosine to inosine editing; base conversion or substitution editing; cytokine and chemokine mediated signaling pathway; defense response to virus; erythrocyte differentiation; gene expression; hemopoietic progenitor cell differentiation; in utero embryonic development; innate immune response; miRNA-mediated gene silencing, miRNA loading onto RISC; mRNA modification; mRNA processing; negative regulation of apoptosis; negative regulation of viral genome replication; osteoblast differentiation; positive regulation of viral genome replication; pre-microRNA processing; protein export from nucleus; protein import into nucleus; response to virus; somatic diversification of immune receptors via somatic mutation. Disease: Aicardi-goutieres Syndrome 6; Dyschromatosis Symmetrica Hereditaria

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180