Adprs
entrez
100206
canonical
uniprot
Q8CG72
canonical
ensembl
ENSMUSG00000042558
resolver
ensp
ENSMUSP00000099677
resolver
genesymbol
Adprs
resolver
genesymbol_syn
Adprhl2
resolver
genesymbol_syn
Arh3
resolver
uniprot
A3KFY3
resolver
uniprot
Q80UW9
resolver
uniprot
Q8R575
resolver
uniprot
Q921U6
resolver
uniprot_entry
ADPRS_MOUSE
resolver
uniprot_sec
A3KFY3
resolver
uniprot_sec
Q80UW9
resolver
uniprot_sec
Q8R575
resolver
uniprot_sec
Q921U6
resolver
activity_regulation
ACTIVITY REGULATION: 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-47) blocks substrate entrance to Mg(2+) in the unliganded closed state. In presence of substrate, Glu-47 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. {ECO:0000250|UniProtKB:Q9NX46}.
uniprot
proteins
amino_acid_sequence
MAVAAAAAATAMSAAGGGGASAARSISRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKKLLNPKCRDVYEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLEQLLGHMEELEGDAQSVLDAKELGMEERPYSSRLKKVGELLDQDVVSREEVVSELGNGIAAFESVPTAIYCFLRCMEPHPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGFEETDVLAQSLHRVFQESS
uniprot
proteins
ec_number
3.2.1.143
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
function
FUNCTION: ADP-ribosylhydrolase 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 and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (By similarity). 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 (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). 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 (PubMed:24191052, PubMed:30830864). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). 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). {ECO:0000250|UniProtKB:Q9NX46, ECO:0000269|PubMed:24191052, ECO:0000269|PubMed:30830864}.
uniprot
proteins
mass_dalton
39414
uniprot
proteins
protein_family
ADP-ribosylglycohydrolase family
uniprot
proteins
pubmed
12070318
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16278211
uniprot
proteins
pubmed
18323597
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24191052
uniprot
proteins
pubmed
30830864
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16278211, ECO:0000269|PubMed:24191052}. Cytoplasm {ECO:0000269|PubMed:16278211}. Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix {ECO:0000269|PubMed:24191052}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}.
uniprot
proteins