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Reviewed, UniProtKB/Swiss-Prot Q02589 (ADPRH_RAT)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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

Its activity is synergistically stimulated by magnesium and dithiothreitol (DTT) in vitro.

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

Keywords
   LigandMagnesium
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processprotein amino acid de-ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Molecular functionADP-ribosylarginine hydrolase activity Ref.1

Inferred from mutant phenotype. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362[Protein ADP-ribosylarginine] hydrolase
PRO_0000157285

Experimental info

Sequence conflict2521K → Q in AAA40691. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q02589-1 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: 6C941A940AEAE10E

FASTA36239,961
        10         20         30         40         50         60 
MGGGLIERYV AAMVLSAAGD TLGYFNGKWE FLRDGEKIHR QLAQMGDLEA IDVAQWRVSD 

        70         80         90        100        110        120 
DTIMHLATAE ALMEAGSSPD LPQLYSLLAK HYRDCMGDMD GRAPGGACMQ NAMQLDPDRA 

       130        140        150        160        170        180 
DGWRIPFNSH EGGCGAAMRA MCIGLRFPHP SQLDTLIQVS IESGRMTHHH PTGYLGSLAS 

       190        200        210        220        230        240 
ALFTAYAVNG KSPRQWGKGL MEVLPEAKAY VTQSGYFVKE NLQHWSYFEK EWEKYLELRG 

       250        260        270        280        290        300 
ILDGKSAPVF PKPFGVKERD QFYIEVSYSG WGGSSGHDAP MIAYDALLAA GDSWKELAHR 

       310        320        330        340        350        360 
AFFHGGDSDS TATIAGCWWG VMHGFKGVNP SNYEKLEYRQ RLEEAGRALY SLGSKEDTIL 


GP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and immunological characterization of ADP-ribosylarginine hydrolases."
Moss J., Stanley S.J., Nightingale M.S., Murtagh J.J. Jr., Monaco L., Mishima K., Chen H.C., Williamson K.C., Tsai S.C.
J. Biol. Chem. 267:10481-10488(1992) [PubMed: 1375222] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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].
Tissue: Testis.
[3]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 147-165, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

M86341 mRNA. Translation: AAA40691.1.
BC082065 mRNA. Translation: AAH82065.1.
IPIIPI00208197.
PIRA38135.
RefSeqNP_899154.2.
UniGeneRn.13315

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSRNOT00000038439; ENSRNOP00000034815; ENSRNOG00000027260; Rattus norvegicus. [Genome view]
GeneID25371.
KEGGrno:25371.
NMPDRfig|10116.3.peg.7179.
UCSCNM_183325. rat.

Organism-specific databases

CTD25371.
RGD2052. Adprh.

Phylogenomic databases

HOVERGENQ02589.
OMAIPFNSHE.

Enzyme and pathway databases

BRENDA3.2.2.19. 248.

Gene expression databases

ArrayExpressQ02589.
GenevestigatorQ02589.
GermOnlineENSRNOG00000027260. Rattus norvegicus.

Family and domain databases

InterProIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PANTHERPTHR22957:SF7. ADP-ribosylarg_hydro. 1 hit.
PfamPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFPIRSF016939. ADP_ribslarg_hdr. 1 hit.
ProtoNetSearch...

Other Resources

NextBio606385.

Entry information

Entry nameADPRH_RAT
AccessionPrimary (citable) accession number: Q02589
Secondary accession number(s): Q66H27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 29, 2007
Last modified: November 3, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents