[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8349667 [NCBI, ExPASy, EBI, Israel, Japan] Takada T., Iida K., Moss J.; "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase."; J. Biol. Chem. 268:17837-17843(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/j.gene.2005.02.016; PubMed=15893437 [NCBI, ExPASy, EBI, Israel, Japan] Aoki K., Kato J., Shoemaker M.T., Moss J.; "Genomic organization and promoter analysis of the mouse ADP-ribosylarginine hydrolase gene."; Gene 351:83-95(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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.
CATALYTIC ACTIVITY: N(omega)-(ADP-D-ribosyl)-L-arginine + H₂O = ADP-ribose + L-arginine.
ENZYME REGULATION: Synergistically stimulated by magnesium and dithiothreitol (DTT) in vitro.
SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L13290; AAA37259.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF244347; AAF86223.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003437; AAH03437.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00111149; -.

A47411; A47411.

NP_031440.1; -.

3D structure databases

ModBase

P54923.

PTM databases

PhosphoSite

P54923; -.

Enzyme and pathway databases

BRENDA

3.2.2.19; 244.

2D gel databases

REPRODUCTION-2DPAGE

P54923; -.

Organism-specific databases

MGI

MGI:1098234; Adprh.

Gene expression databases

P54923; -.

P54923; -.

MM_ADPRH; -.

ENSMUSG00000002844; Mus musculus.

Ontologies

GO:0003875;	Molecular function: ADP-ribosylarginine hydrolase activity (inferred from mutant phenotype from UniProtKB).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051725;	Biological process: protein amino acid de-ADP-ribosylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR012108; ADP-ribosylarg_hydro.
IPR005502; Ribosyl_crysJ1.
Graphical view of domain structure.

PANTHER

PTHR22957:SF7; ADP-ribosylarg_hydro; 1.

Pfam

PF03747; ADP_ribosyl_GH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF016939; ADP_ribslarg_hdr; 1.

Proteomic databases

PRIDE

P54923; -.

Genome annotation databases

Ensembl

ENSMUSG00000002844; Mus musculus. [Contig view]

GeneID

11544; -.

KEGG

mmu:11544; -.

Phylogenomic databases

HOGENOM

P54923; -.

HOVERGEN

P54923; -.

OMA

P54923; IPFNSHE.

Other

279014; -.

Adprh; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Hydrolase; Magnesium.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 362`	`362`		`[Protein ADP-ribosylarginine] hydrolase.`	`PRO_0000157284`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 40068 Da [This is the MW of the unprocessed precursor]

CRC64: E06BCAEF69BA7C4E [This is a checksum on the sequence]

        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

P54923 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools