Skip Header

Contribute Send feedback
Read comments (?) or add your own

P54923 (ADPRH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Protein ADP-ribosylarginine] hydrolase

Short name=ADP-ribosylarginine hydrolase
EC=3.2.2.19
Alternative name(s):
ADP-ribose-L-arginine cleaving enzyme
Gene names
Name:Adprh
Synonyms:Arh1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reverse reaction of mono-ADP-ribosylation.

Catalytic activity

Protein-N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + protein-L-arginine.

N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine.

Enzyme regulation

Synergistically stimulated by magnesium and dithiothreitol (DTT) in vitro.

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

Keywords
   LigandMagnesium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein de-ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Molecular functionADP-ribosylarginine hydrolase activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362[Protein ADP-ribosylarginine] hydrolase
PRO_0000157284

Sequences

Sequence LengthMass (Da)Tools
P54923 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E06BCAEF69BA7C4E

FASTA36240,068
        10         20         30         40         50         60 
MGGGLIERYV AAMVLSAAGD TLGYFNGKWE FIRDGETIHQ QLAQMGDLEA IDVARWRVSD 

        70         80         90        100        110        120 
DTVMHLATAE ALMEAGQSPD LPRLYSLLAK HYRDCMGDMD GRAPGGACMQ NAMLLQPNRA 

       130        140        150        160        170        180 
DGYRIPFNSH EGGCGAAMRA MCIGLRFPHP SQLDLLIQVS IESGRMTHHH PTGYLGSLAS 

       190        200        210        220        230        240 
ALFTAYAVNG KSPWQWGKGL MEVLPEAKKY ITQSGYFVKE NLQHWSYFEK EWEKYLELRG 

       250        260        270        280        290        300 
ILDGNSAPVF PQPFGVKERD QFYIDVSYSG WGGSSGHDAP MIAYDALLAA GDSWKELAHR 

       310        320        330        340        350        360 
AFFHGGDSDS TAAIAGCWWG VMYGFKGVNP ANYEKLEYRQ RLEEAGRALY SLGSKEDPVL 


DP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase."
Takada T., Iida K., Moss J.
J. Biol. Chem. 268:17837-17843(1993) [PubMed: 8349667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization and promoter analysis of the mouse ADP-ribosylarginine hydrolase gene."
Aoki K., Kato J., Shoemaker M.T., Moss J.
Gene 351:83-95(2005) [PubMed: 15893437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13290 mRNA. Translation: AAA37259.1.
AF244347 mRNA. Translation: AAF86223.1.
BC003437 mRNA. Translation: AAH03437.1.
IPIIPI00111149.
PIRA47411.
RefSeqNP_031440.1. NM_007414.3.
UniGeneMm.20047.

3D structure databases

ProteinModelPortalP54923.
SMRP54923. Positions 6-360.
ModBaseSearch...

Protein-protein interaction databases

STRINGP54923.

PTM databases

PhosphoSiteP54923.

2D gel databases

REPRODUCTION-2DPAGEP54923.

Proteomic databases

PRIDEP54923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002923; ENSMUSP00000002923; ENSMUSG00000002844.
GeneID11544.
KEGGmmu:11544.

Organism-specific databases

CTD141.
MGIMGI:1098234. Adprh.

Phylogenomic databases

eggNOGroNOG09199.
HOGENOMHBG715225.
HOVERGENHBG050462.
InParanoidP54923.
OMAHWSYFQD.
OrthoDBEOG4QJRNH.
PhylomeDBP54923.

Gene expression databases

ArrayExpressP54923.
BgeeP54923.
CleanExMM_ADPRH.
GenevestigatorP54923.
GermOnlineENSMUSG00000002844. Mus musculus.

Family and domain databases

InterProIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
KOK01245.
PfamPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMSSF101478. Ribosyl_crysJ1. 1 hit.
ProtoNetSearch...

Other

NextBio279014.
SOURCESearch...

Entry information

Entry nameADPRH_MOUSE
AccessionPrimary (citable) accession number: P54923
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families