ID OARD1_MOUSE Reviewed; 152 AA.
AC Q8R5F3; Q3U5M3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 121.
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:0000312|MGI:MGI:2146818};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK153512; BAE32055.1; -; mRNA.
DR EMBL; AC166164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23617.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23618.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23619.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23621.1; -; Genomic_DNA.
DR EMBL; BC022574; AAH22574.1; -; mRNA.
DR EMBL; BC157987; AAI57988.1; -; mRNA.
DR CCDS; CCDS37647.1; -.
DR RefSeq; NP_001276419.1; NM_001289490.1.
DR RefSeq; NP_001276420.1; NM_001289491.1.
DR RefSeq; NP_997102.2; NM_207219.4.
DR RefSeq; XP_006523518.1; XM_006523455.1.
DR RefSeq; XP_006523519.1; XM_006523456.1.
DR RefSeq; XP_006523521.1; XM_006523458.1.
DR RefSeq; XP_006523522.1; XM_006523459.3.
DR RefSeq; XP_006523523.1; XM_006523460.3.
DR AlphaFoldDB; Q8R5F3; -.
DR SMR; Q8R5F3; -.
DR BioGRID; 223130; 1.
DR STRING; 10090.ENSMUSP00000130802; -.
DR PhosphoSitePlus; Q8R5F3; -.
DR EPD; Q8R5F3; -.
DR MaxQB; Q8R5F3; -.
DR PaxDb; 10090-ENSMUSP00000130802; -.
DR ProteomicsDB; 291931; -.
DR Pumba; Q8R5F3; -.
DR Antibodypedia; 29984; 51 antibodies from 13 providers.
DR DNASU; 106821; -.
DR Ensembl; ENSMUST00000046651.7; ENSMUSP00000039280.7; ENSMUSG00000040771.15.
DR Ensembl; ENSMUST00000167180.8; ENSMUSP00000130802.2; ENSMUSG00000040771.15.
DR GeneID; 106821; -.
DR KEGG; mmu:106821; -.
DR UCSC; uc008cxu.2; mouse.
DR AGR; MGI:2146818; -.
DR CTD; 221443; -.
DR MGI; MGI:2146818; Oard1.
DR VEuPathDB; HostDB:ENSMUSG00000040771; -.
DR eggNOG; ENOG502RXG1; Eukaryota.
DR GeneTree; ENSGT00390000006988; -.
DR HOGENOM; CLU_054419_4_1_1; -.
DR InParanoid; Q8R5F3; -.
DR OMA; CHCLKNG; -.
DR OrthoDB; 1347733at2759; -.
DR PhylomeDB; Q8R5F3; -.
DR TreeFam; TF324128; -.
DR BioGRID-ORCS; 106821; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Oard1; mouse.
DR PRO; PR:Q8R5F3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R5F3; Protein.
DR Bgee; ENSMUSG00000040771; Expressed in epiblast (generic) and 63 other cell types or tissues.
DR ExpressionAtlas; Q8R5F3; baseline and differential.
DR Genevisible; Q8R5F3; MM.
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:DNA damage response; 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 CDD; cd02901; Macro_Poa1p-like; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR PANTHER; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Hydrolase; Nucleus; 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_0000089530"
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 CONFLICT 3
FT /note="T -> S (in Ref. 4; AAH22574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17107 MW; 1ADEFB913BC26605 CRC64;
MATRLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK RFGGVQELLS
QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL EAMKSHCLKN GVTDLSMPRI
GCGLDRLQWE NVSAILEEVF ESTDIKITVY TL
//
