Primary Information |
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| BoMiProt ID | Bomi3443 |
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| Protein Name | [Protein ADP-ribosylarginine] hydrolase/ADP-ribose-L-arginine cleaving enzyme |
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| Organism | Bos taurus |
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| Uniprot ID | Q32KR8 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001033643.1 |
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| Aminoacid Length | 353 |
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| Molecular Weight | 39152 |
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| FASTA Sequence |
Download |
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| Gene Name | ADPRH |
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| Gene ID | 525738 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | liver |
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| Protein Function | Participates in ADP-ribosylation cycle during the release of ADP-ribose and regenerate an unmodified protein.It acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. |
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| Biochemical Properties | Binds 2 magnesium ions per subunit.H2O + Nω-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] ADP-ribosylarginine hydrolases differ in their dithiothreitol (DTT) requirements: the rat and mouse enzymes require DTT for maximal activity, while the calf, guinea pig, and human hydrolases are DTT-independent. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| na |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1.Takada T, Iida K, Moss J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J Biol Chem. 1993 Aug 25;268(24):17837-43. PMID: 8349667. |
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