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P51400 (RED1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Double-stranded RNA-specific editase 1
EC=3.5.-.-
Alternative name(s):
RNA-editing deaminase 1
RNA-editing enzyme 1
dsRNA adenosine deaminase
Gene names
Name:Adarb1
Synonyms:Red1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Editing of the messenger RNAs for glutamate receptor (GluR) subunits by site-selective adenosine deamination. Edits both the GluR-B Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently.

Cofactor

Binds 1 inositol hexakisphosphate (IP6) per subunit By similarity.

Tissue specificity

Brain and peripheral tissues.

Sequence similarities

Contains 1 A to I editase domain.

Contains 2 DRBM (double-stranded RNA-binding) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Double-stranded RNA-specific editase 1
PRO_0000171781

Regions

Domain78 – 14467DRBM 1
Domain231 – 29868DRBM 2
Domain370 – 707338A to I editase

Sites

Active site3961Proton donor By similarity
Metal binding3941Zinc By similarity
Metal binding4511Zinc By similarity
Metal binding5261Zinc By similarity
Binding site4001Inositol hexakisphosphate By similarity
Binding site4011Inositol hexakisphosphate By similarity
Binding site5291Inositol hexakisphosphate By similarity
Binding site5321Inositol hexakisphosphate By similarity
Binding site6391Inositol hexakisphosphate By similarity
Binding site6721Inositol hexakisphosphate By similarity
Binding site6821Inositol hexakisphosphate By similarity
Binding site7001Inositol hexakisphosphate By similarity

Secondary structure

1 ...................... 711
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51400 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5A25C4B202530C54

FASTA71177,925
        10         20         30         40         50         60 
MDIEDEENMS SSSIDVKENR NLDNMPPKDS STPGPGEGIP LSNGGGGSTS RKRPLEEGSN 

        70         80         90        100        110        120 
GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYMLLSQ TGPVHAPLFV MSVEVNGQVF 

       130        140        150        160        170        180 
EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF 

       190        200        210        220        230        240 
ETPDKSEPPF YVGSNGDDSF SSSGDVSLSA SPVPASLTQP PLPIPPPFPP PSGKNPVMIL 

       250        260        270        280        290        300 
NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALATVFNLH 

       310        320        330        340        350        360 
LDQTPSRQPV LSEGLQLHLP QVLADAVSRL VLGKFSDLTD NFSSPHARRK VLSGVVMTTG 

       370        380        390        400        410        420 
TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYAQ LELYLNNKED 

       430        440        450        460        470        480 
QKKSIFQKSE RGGFRLKDTV QFHLYISTSP CGDARIFSPH EPVLEGMAPD SHQLTEPADR 

       490        500        510        520        530        540 
HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG 

       550        560        570        580        590        600 
ALLSIFVEPI YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR 

       610        620        630        640        650        660 
QPGKAPNFSV NWTVGDTAIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH GKVPPHLLRT 

       670        680        690        700        710 
KITKPTTYHE SKLAAKEYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSFT P

« Hide

References

[1]"A mammalian RNA editing enzyme."
Melcher T., Maas S., Herb A., Sprengel R., Seeburg P.H., Higuchi M.
Nature 379:460-464(1996) [PubMed: 8559253] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43534 mRNA. Translation: AAA96755.1.
IPIIPI00202145.
PIRS68443.
RefSeqNP_001104525.1. NM_001111055.1.
NP_001104526.1. NM_001111056.1.
NP_001104527.1. NM_001111057.1.
NP_037026.2. NM_012894.2.
UniGeneRn.172406.
Rn.89675.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B7TNMR-A74-146[»]
2B7VNMR-A231-301[»]
2L3CNMR-A74-147[»]
2L3JNMR-A74-301[»]
ProteinModelPortalP51400.
SMRP51400. Positions 74-146, 231-301, 306-710.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25367.
KEGGrno:25367.
UCSCNM_012894. rat.

Organism-specific databases

CTD104.
RGD2033. Adarb1.

Phylogenomic databases

eggNOGroNOG12900.
GeneTreeENSGT00550000074412.
HOVERGENHBG003836.
InParanoidP51400.
OrthoDBEOG4MGS70.
PhylomeDBP51400.

Gene expression databases

ArrayExpressP51400.
GenevestigatorP51400.
GermOnlineENSRNOG00000001227. Rattus norvegicus.

Family and domain databases

InterProIPR002466. A_deamin.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
[Graphical view]
Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.
KOK13194.
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio606369.

Entry information

Entry nameRED1_RAT
AccessionPrimary (citable) accession number: P51400
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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