UniProtKB - Q3SYV9 (ADPRS_BOVIN)
Protein
ADP-ribose glycohydrolase ARH3
Gene
ADPRS
Organism
Bos taurus (Bovine)
Status
Functioni
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.By similarity
Catalytic activityi
- EC:3.2.1.143By similarity
Cofactori
Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity
Activity regulationi
The protein undergoes a dramatic conformational switch from closed to open states upon substrate-binding, which enables specific substrate recognition for the 1''-O-linkage. The glutamate flap (Glu-42) blocks substrate entrance to Mg2+ in the unliganded closed state. In presence of substrate, Glu-42 is ejected from the active site: this closed-to-open transition significantly widens the substrate-binding channel and precisely positions the scissile 1''-O-linkage for cleavage while securing tightly 2'- and 3'-hydroxyls of ADP-ribose.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 42 | Magnesium 2By similarity | 1 | |
Sitei | 42 | Glutamate flapBy similarity | 1 | |
Metal bindingi | 77 | Magnesium 1By similarity | 1 | |
Metal bindingi | 78 | Magnesium 1By similarity | 1 | |
Binding sitei | 78 | SubstrateBy similarity | 1 | |
Metal bindingi | 79 | Magnesium 1By similarity | 1 | |
Binding sitei | 183 | SubstrateBy similarity | 1 | |
Binding sitei | 236 | SubstrateBy similarity | 1 | |
Binding sitei | 272 | SubstrateBy similarity | 1 | |
Metal bindingi | 315 | Magnesium 2By similarity | 1 | |
Metal bindingi | 317 | Magnesium 1By similarity | 1 | |
Metal bindingi | 317 | Magnesium 2By similarity | 1 | |
Metal bindingi | 318 | Magnesium 2By similarity | 1 |
GO - Molecular functioni
- ADP-ribosylserine hydrolase activity Source: UniProtKB
- hydrolase activity, hydrolyzing O-glycosyl compounds Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- O-acetyl-ADP-ribose deacetylase activity Source: UniProtKB
- poly(ADP-ribose) glycohydrolase activity Source: UniProtKB
GO - Biological processi
- DNA repair Source: UniProtKB
- peptidyl-serine ADP-deribosylation Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | DNA damage, DNA repair |
Ligand | Magnesium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: ADP-ribose glycohydrolase ARH3CuratedAlternative name(s): |
Gene namesi | Name:ADPRS Synonyms:ADPRHL2By similarity, ARH3By similarity |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Mitochondrion
- Mitochondrion matrix By similarity
Nucleus
- Nucleus By similarity
Other locations
- Cytoplasm By similarity
- Chromosome By similarity
Note: Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites.By similarity
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: GO_Central
Nucleus
- nucleus Source: UniProtKB
Other locations
- site of DNA damage Source: UniProtKB
Keywords - Cellular componenti
Chromosome, Cytoplasm, Mitochondrion, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000277612 | 1 – 365 | ADP-ribose glycohydrolase ARH3Add BLAST | 365 |
Proteomic databases
PaxDbi | Q3SYV9 |
PRIDEi | Q3SYV9 |
Interactioni
Subunit structurei
Monomer.
By similarityProtein-protein interaction databases
STRINGi | 9913.ENSBTAP00000028950 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 147 – 153 | Substrate bindingBy similarity | 7 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2 – 6 | Poly-Ala | 5 |
Sequence similaritiesi
Belongs to the ADP-ribosylglycohydrolase family.Curated
Phylogenomic databases
eggNOGi | ENOG502QUER, Eukaryota |
InParanoidi | Q3SYV9 |
OrthoDBi | 988788at2759 |
Family and domain databases
Gene3Di | 1.10.4080.10, 1 hit |
InterProi | View protein in InterPro IPR005502, Ribosyl_crysJ1 IPR036705, Ribosyl_crysJ1_sf |
Pfami | View protein in Pfam PF03747, ADP_ribosyl_GH, 1 hit |
SUPFAMi | SSF101478, SSF101478, 1 hit |
i Sequence
Sequence statusi: Complete.
Q3SYV9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAAAAAMTAA GCGGAGAARS LSRFRGCLAG ALLGDCVGAV YEARDTVDLT
60 70 80 90 100
SVLRQVQDLE PDPGSPGSAR TEALCYTDDT AMARALVQSL LAKEAFDEVD
110 120 130 140 150
MAHRFAQEYK KDPDRGYGAG VITVFRKHLS PRCRDVFEPA RAQFNGKGSY
160 170 180 190 200
GNGGAMRVAG ISLAYSSVQD VQKFARLSAQ LTHASSLGYN GAILQALAVH
210 220 230 240 250
LALQGESSSE HFLEQLLGHM EELESDAQSV LDARELGMEE RPYSSRLKKI
260 270 280 290 300
GELLEQDSVT REEVVSELGN GIAAFESVPT AIYCFLRCME PDPEIPSTFN
310 320 330 340 350
SLQRTLVYSI SLGGDTDTIA TMAGAIAGAY YGMEQVPESW QQSCEGYEET
360
DVLAQSLHRV FQKSL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC103360 mRNA Translation: AAI03361.1 |
RefSeqi | NP_001030417.1, NM_001035340.2 |
Genome annotation databases
GeneIDi | 521650 |
KEGGi | bta:521650 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC103360 mRNA Translation: AAI03361.1 |
RefSeqi | NP_001030417.1, NM_001035340.2 |
3D structure databases
SMRi | Q3SYV9 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000028950 |
Proteomic databases
PaxDbi | Q3SYV9 |
PRIDEi | Q3SYV9 |
Genome annotation databases
GeneIDi | 521650 |
KEGGi | bta:521650 |
Organism-specific databases
CTDi | 54936 |
Phylogenomic databases
eggNOGi | ENOG502QUER, Eukaryota |
InParanoidi | Q3SYV9 |
OrthoDBi | 988788at2759 |
Family and domain databases
Gene3Di | 1.10.4080.10, 1 hit |
InterProi | View protein in InterPro IPR005502, Ribosyl_crysJ1 IPR036705, Ribosyl_crysJ1_sf |
Pfami | View protein in Pfam PF03747, ADP_ribosyl_GH, 1 hit |
SUPFAMi | SSF101478, SSF101478, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ADPRS_BOVIN | |
Accessioni | Q3SYV9Primary (citable) accession number: Q3SYV9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 6, 2007 |
Last sequence update: | October 11, 2005 | |
Last modified: | February 10, 2021 | |
This is version 83 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - SIMILARITY comments
Index of protein domains and families