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InterPro: IPR012108 ADP-ribosylarginine hydrolase

Protein matches Help

UniProtKB

Matches:

33 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR012108 ADP-ribosylarg_hydro

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF016939	ADP_ribslarg_hdr	27
PANTHER	PTHR22957:SF7	ADP-ribosylarg_hydro	33
Signatures in BioMart

InterPro Relationships Help

Parent

IPR005502 ADP-ribosylation/Crystallin J1

GO Term annotation Help

Process

GO:0051725 protein amino acid de-ADP-ribosylation

Function

GO:0000287 magnesium ion binding
GO:0003875 ADP-ribosylarginine hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

This enzyme catalyzes the reverse reaction of mono-ADP-ribosylation by removing ADP-ribose from arginine residues in ADP-ribosylated proteins. NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyse opposing arms of the putative ADP-ribosylation cycle.

ADP-ribosylarginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarity in their deduced amino acid sequence. The conserved vicinal aspartates 60 and 61 in rat ADP-ribosylarginine hydrolase are critical for catalytic activity, but not for high affinity binding of the substrate analogue, ADP-ribose [1].

ADP-ribosylarginine hydrolases in different organisms also differ in their dithiothreitol (DTT) requirements. Cysteine 108 in rat hydrolase plays a critical role in DTT dependence and may be important in immunoreactivity [2].

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012108

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P54922 [Protein ADP-ribosylarginine] hydrolase

P54923 [Protein ADP-ribosylarginine] hydrolase

Q02589 [Protein ADP-ribosylarginine] hydrolase

Q54H71 [Protein ADP-ribosylarginine] hydrolase

Q5UQP4 Putative ADP-ribosyl glycohydrolase L444

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005502	ADP-ribosylation/Crystallin J1
IPR012108	ADP-ribosylarginine hydrolase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Konczalik P, Moss J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 16736-40 1999 [PubMed: 10358013] http://dx.doi.org/10.1074/jbc.274.24.16736
2.	Takada T, Iida K, Moss J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 17837-43 1993 [PubMed: 8349667] http://intl.jbc.org/cgi/content/abstract/268/24/17837

InterPro 24.0