OARD1_BOVIN
ID OARD1_BOVIN Reviewed; 152 AA.
AC Q1LZ74;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ADP-ribose glycohydrolase OARD1 {ECO:0000305};
DE AltName: Full=O-acetyl-ADP-ribose deacetylase 1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q9Y530};
DE AltName: Full=Terminal ADP-ribose protein glycohydrolase 1 {ECO:0000250|UniProtKB:Q9Y530};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase OARD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:Q9Y530};
GN Name=OARD1 {ECO:0000250|UniProtKB:Q9Y530};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts
CC on different substrates, such as proteins ADP-ribosylated on glutamate
CC and O-acetyl-ADP-D-ribose. Specifically acts as a glutamate mono-ADP-
CC ribosylhydrolase by mediating the removal of mono-ADP-ribose attached
CC to glutamate residues on proteins. Does not act on poly-ADP-ribosylated
CC proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate
CC residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG
CC to become a substrate for OARD1. Deacetylates O-acetyl-ADP ribose, a
CC signaling molecule generated by the deacetylation of acetylated lysine
CC residues in histones and other proteins. Catalyzes the deacylation of
CC O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose,
CC yielding ADP-ribose plus acetate, propionate and butyrate,
CC respectively. {ECO:0000250|UniProtKB:Q9Y530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767;
CC Evidence={ECO:0000250|UniProtKB:Q9Y530};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:Q9Y530};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC Evidence={ECO:0000250|UniProtKB:Q9Y530};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by the product
CC ADP-ribose. {ECO:0000250|UniProtKB:Q9Y530}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y530}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9Y530}. Chromosome
CC {ECO:0000250|UniProtKB:Q9Y530}. Note=Localizes both in the nucleoplasm
CC and in the nucleolus. Relocalizes to the nucleoplasm in response to DNA
CC damage. Recruited to DNA lesion regions following DNA damage.
CC {ECO:0000250|UniProtKB:Q9Y530}.
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DR EMBL; BC116164; AAI16165.1; -; mRNA.
DR RefSeq; NP_001070581.1; NM_001077113.1.
DR RefSeq; XP_005223565.1; XM_005223508.1.
DR RefSeq; XP_005223566.1; XM_005223509.1.
DR RefSeq; XP_005223567.1; XM_005223510.2.
DR RefSeq; XP_005223568.1; XM_005223511.2.
DR AlphaFoldDB; Q1LZ74; -.
DR SMR; Q1LZ74; -.
DR STRING; 9913.ENSBTAP00000007840; -.
DR PaxDb; Q1LZ74; -.
DR PRIDE; Q1LZ74; -.
DR Ensembl; ENSBTAT00000007840; ENSBTAP00000007840; ENSBTAG00000005975.
DR GeneID; 768056; -.
DR KEGG; bta:768056; -.
DR CTD; 221443; -.
DR VEuPathDB; HostDB:ENSBTAG00000005975; -.
DR VGNC; VGNC:32390; OARD1.
DR eggNOG; ENOG502RXG1; Eukaryota.
DR GeneTree; ENSGT00390000006988; -.
DR HOGENOM; CLU_054419_4_1_1; -.
DR InParanoid; Q1LZ74; -.
DR OMA; ERIKCVK; -.
DR OrthoDB; 1416296at2759; -.
DR TreeFam; TF324128; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000005975; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q1LZ74; baseline.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; ISS:UniProtKB.
DR GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; ISS:UniProtKB.
DR GO; GO:0001883; F:purine nucleoside binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; ISS:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0042278; P:purine nucleoside metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT CHAIN 2..152
FT /note="ADP-ribose glycohydrolase OARD1"
FT /id="PRO_0000265095"
FT DOMAIN 2..152
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT BINDING 119..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y530"
SQ SEQUENCE 152 AA; 17035 MW; B6C3EE393F96D191 CRC64;
MAGSPNEDSE GSRITYVKGD LFACPQTDSL VHCISEDCRM GAGIAVLFKK KFGGVQELLN
QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLRKSL EAMKSHCLKN GVTDLSMPRI
GCGLDRLQWE NVSAIIEEVF EATDIRITVY TL
