OARD1_HUMAN
ID OARD1_HUMAN Reviewed; 152 AA.
AC Q9Y530; A6NEK4; A8K4H4; Q96F23;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ADP-ribose glycohydrolase OARD1 {ECO:0000305};
DE AltName: Full=O-acetyl-ADP-ribose deacetylase 1;
DE EC=3.5.1.- {ECO:0000305|PubMed:21849506};
DE AltName: Full=Terminal ADP-ribose protein glycohydrolase 1 {ECO:0000303|PubMed:23481255};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase OARD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255};
GN Name=OARD1 {ECO:0000312|HGNC:HGNC:21257};
GN Synonyms=C6orf130 {ECO:0000312|HGNC:HGNC:21257},
GN TARG1 {ECO:0000303|PubMed:23481255};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP FUNCTION.
RX PubMed=23474714; DOI=10.1038/nsmb.2521;
RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R.,
RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B.,
RA Hottiger M.O.;
RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
RL Nat. Struct. Mol. Biol. 20:502-507(2013).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=29712969; DOI=10.1038/s41598-018-25137-w;
RA Buetepage M., Preisinger C., von Kriegsheim A., Scheufen A., Lausberg E.,
RA Li J., Kappes F., Feederle R., Ernst S., Eckei L., Krieg S.,
RA Mueller-Newen G., Rossetti G., Feijs K.L.H., Verheugd P., Luescher B.;
RT "Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-
RT induced poly-ADP-ribosylation and by nucleolar transcription.";
RL Sci. Rep. 8:6748-6748(2018).
RN [12]
RP CATALYTIC ACTIVITY.
RX PubMed=31599159; DOI=10.1021/acschembio.9b00429;
RA Stevens L.A., Kato J., Kasamatsu A., Oda H., Lee D.Y., Moss J.;
RT "The ARH and Macrodomain Families of alpha-ADP-ribose-acceptor Hydrolases
RT Catalyze alpha-NAD+ Hydrolysis.";
RL ACS Chem. Biol. 14:2576-2584(2019).
RN [13]
RP STRUCTURE BY NMR OF 11-152.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the A1PP domain from human protein C6orf130.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [14]
RP STRUCTURE BY NMR.
RG Center for eukaryotic structural genomics (CESG);
RT "Solution structure of human C6orf130, a putative Macro domain.";
RL Submitted (APR-2008) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR IN COMPLEX WITH ADENOSINE-5-DIPHOSPHORIBOSE, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-32; CYS-33; SER-35;
RP THR-83; GLY-123 AND ASP-125, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=21849506; DOI=10.1074/jbc.m111.276238;
RA Peterson F.C., Chen D., Lytle B.L., Rossi M.N., Ahel I., Denu J.M.,
RA Volkman B.F.;
RT "Orphan macrodomain (human C6ORF130) is an o-acyl-ADP-ribose deacylase:
RT solution structure and catalytic properties.";
RL J. Biol. Chem. 286:35955-35965(2011).
RN [16] {ECO:0007744|PDB:4J5Q, ECO:0007744|PDB:4J5R, ECO:0007744|PDB:4J5S}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 11-152 IN COMPLEX WITH ADP-RIBOSE
RP ANALOGUE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, TISSUE SPECIFICITY,
RP INVOLVEMENT IN SEVERE NEURODEGENERATION, VARIANT 76-ARG--LEU-152 DEL, AND
RP MUTAGENESIS OF LYS-84 AND ASP-125.
RX PubMed=23481255; DOI=10.1038/emboj.2013.51;
RA Sharifi R., Morra R., Appel C.D., Tallis M., Chioza B., Jankevicius G.,
RA Simpson M.A., Matic I., Ozkan E., Golia B., Schellenberg M.J., Weston R.,
RA Williams J.G., Rossi M.N., Galehdari H., Krahn J., Wan A., Trembath R.C.,
RA Crosby A.H., Ahel D., Hay R., Ladurner A.G., Timinszky G., Williams R.S.,
RA Ahel I.;
RT "Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in
RT neurodegenerative disease.";
RL EMBO J. 32:1225-1237(2013).
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 (PubMed:23481255, PubMed:23474714,
CC PubMed:21849506). Specifically acts as a glutamate mono-ADP-
CC ribosylhydrolase by mediating the removal of mono-ADP-ribose attached
CC to glutamate residues on proteins (PubMed:23481255, PubMed:23474714).
CC Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose
CC chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed
CC into mono-ADP-ribosylated glutamate by PARG to become a substrate for
CC OARD1 (PubMed:23481255). Deacetylates O-acetyl-ADP ribose, a signaling
CC molecule generated by the deacetylation of acetylated lysine residues
CC in histones and other proteins (PubMed:21849506). Catalyzes the
CC deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-
CC butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and
CC butyrate, respectively (PubMed:21849506). {ECO:0000269|PubMed:21849506,
CC ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255}.
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:0000305|PubMed:21849506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061;
CC Evidence={ECO:0000305|PubMed:21849506};
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:0000269|PubMed:23474714,
CC ECO:0000269|PubMed:23481255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249;
CC Evidence={ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255};
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:0000269|PubMed:31599159};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by the product
CC ADP-ribose. {ECO:0000269|PubMed:21849506}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=182 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21849506};
CC -!- INTERACTION:
CC Q9Y530; P09874: PARP1; NbExp=5; IntAct=EBI-8502288, EBI-355676;
CC Q9Y530; Q53GL7: PARP10; NbExp=3; IntAct=EBI-8502288, EBI-2857573;
CC Q9Y530; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-8502288, EBI-79165;
CC Q9Y530; O95271: TNKS; NbExp=3; IntAct=EBI-8502288, EBI-1105254;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:29712969}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:29712969}. Chromosome
CC {ECO:0000269|PubMed:23481255}. Note=Localizes both in the nucleoplasm
CC and in the nucleolus (PubMed:29712969). Relocalizes to the nucleoplasm
CC in response to DNA damage (PubMed:29712969). Recruited to DNA lesion
CC regions following DNA damage (PubMed:23481255).
CC {ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:29712969}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:23481255}.
CC -!- DISEASE: Note=Defects in OARD1 are found in patients with severe
CC neurodegeneration (PubMed:23481255). Defects were found in an extended
CC consanguineous family with several affected cases in two generations
CC (PubMed:23481255). {ECO:0000269|PubMed:23481255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK290939; BAF83628.1; -; mRNA.
DR EMBL; AK313361; BAG36161.1; -; mRNA.
DR EMBL; AL031778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04011.1; -; Genomic_DNA.
DR EMBL; BC011709; AAH11709.1; -; mRNA.
DR CCDS; CCDS34445.1; -.
DR RefSeq; NP_001316613.1; NM_001329684.1.
DR RefSeq; NP_001316614.1; NM_001329685.1.
DR RefSeq; NP_001316615.1; NM_001329686.1.
DR RefSeq; NP_001316617.1; NM_001329688.1.
DR RefSeq; NP_659500.1; NM_145063.3.
DR PDB; 2EEE; NMR; -; A=11-152.
DR PDB; 2L8R; NMR; -; A=3-152.
DR PDB; 2LGR; NMR; -; A=2-152.
DR PDB; 4J5Q; X-ray; 1.35 A; A=7-152.
DR PDB; 4J5R; X-ray; 1.25 A; A/B=11-152.
DR PDB; 4J5S; X-ray; 1.55 A; A/B/C/D=11-152.
DR PDBsum; 2EEE; -.
DR PDBsum; 2L8R; -.
DR PDBsum; 2LGR; -.
DR PDBsum; 4J5Q; -.
DR PDBsum; 4J5R; -.
DR PDBsum; 4J5S; -.
DR AlphaFoldDB; Q9Y530; -.
DR BMRB; Q9Y530; -.
DR SMR; Q9Y530; -.
DR BioGRID; 128727; 18.
DR IntAct; Q9Y530; 5.
DR MINT; Q9Y530; -.
DR STRING; 9606.ENSP00000420484; -.
DR ChEMBL; CHEMBL4295991; -.
DR iPTMnet; Q9Y530; -.
DR PhosphoSitePlus; Q9Y530; -.
DR BioMuta; OARD1; -.
DR DMDM; 38258957; -.
DR EPD; Q9Y530; -.
DR jPOST; Q9Y530; -.
DR MassIVE; Q9Y530; -.
DR MaxQB; Q9Y530; -.
DR PaxDb; Q9Y530; -.
DR PeptideAtlas; Q9Y530; -.
DR PRIDE; Q9Y530; -.
DR ProteomicsDB; 86280; -.
DR Antibodypedia; 29984; 48 antibodies from 13 providers.
DR DNASU; 221443; -.
DR Ensembl; ENST00000424266.7; ENSP00000416829.2; ENSG00000124596.17.
DR Ensembl; ENST00000463088.5; ENSP00000420193.1; ENSG00000124596.17.
DR Ensembl; ENST00000468811.5; ENSP00000420601.1; ENSG00000124596.17.
DR Ensembl; ENST00000479950.5; ENSP00000420484.1; ENSG00000124596.17.
DR GeneID; 221443; -.
DR KEGG; hsa:221443; -.
DR MANE-Select; ENST00000424266.7; ENSP00000416829.2; NM_001329686.2; NP_001316615.1.
DR UCSC; uc003opm.4; human.
DR CTD; 221443; -.
DR DisGeNET; 221443; -.
DR GeneCards; OARD1; -.
DR HGNC; HGNC:21257; OARD1.
DR HPA; ENSG00000124596; Low tissue specificity.
DR MIM; 614393; gene.
DR neXtProt; NX_Q9Y530; -.
DR OpenTargets; ENSG00000124596; -.
DR PharmGKB; PA134879529; -.
DR VEuPathDB; HostDB:ENSG00000124596; -.
DR eggNOG; ENOG502RXG1; Eukaryota.
DR GeneTree; ENSGT00390000006988; -.
DR InParanoid; Q9Y530; -.
DR OMA; ERIKCVK; -.
DR OrthoDB; 1416296at2759; -.
DR PhylomeDB; Q9Y530; -.
DR TreeFam; TF324128; -.
DR PathwayCommons; Q9Y530; -.
DR SignaLink; Q9Y530; -.
DR BioGRID-ORCS; 221443; 16 hits in 1077 CRISPR screens.
DR EvolutionaryTrace; Q9Y530; -.
DR GenomeRNAi; 221443; -.
DR Pharos; Q9Y530; Tdark.
DR PRO; PR:Q9Y530; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y530; protein.
DR Bgee; ENSG00000124596; Expressed in sperm and 193 other tissues.
DR ExpressionAtlas; Q9Y530; baseline and differential.
DR Genevisible; Q9Y530; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; IDA:UniProtKB.
DR GO; GO:0001883; F:purine nucleoside binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IDA:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Disease variant; Hydrolase; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..152
FT /note="ADP-ribose glycohydrolase OARD1"
FT /id="PRO_0000089529"
FT DOMAIN 2..152
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23481255"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:21849506,
FT ECO:0000269|PubMed:23481255"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21849506"
FT BINDING 119..125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21849506,
FT ECO:0000269|PubMed:23481255"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21849506,
FT ECO:0000269|PubMed:23481255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 76..152
FT /note="Missing (probable disease-associated variant found
FT in a family with severe neurodegeneration)"
FT /evidence="ECO:0000269|PubMed:23481255"
FT /id="VAR_081206"
FT MUTAGEN 32
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:21849506"
FT MUTAGEN 33
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:21849506"
FT MUTAGEN 35
FT /note="S->A: Reduced catalytic activity. No effect on
FT affinity towards substrate."
FT /evidence="ECO:0000269|PubMed:21849506"
FT MUTAGEN 83
FT /note="T->A: Reduced catalytic activity. No effect on
FT affinity towards substrate."
FT /evidence="ECO:0000269|PubMed:21849506"
FT MUTAGEN 84
FT /note="K->A: Abolishes enzyme activity and ability to form
FT a stable covalent adduct with the ADP-ribosylated
FT substrate."
FT /evidence="ECO:0000269|PubMed:23481255"
FT MUTAGEN 123
FT /note="G->E: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:21849506"
FT MUTAGEN 125
FT /note="D->A: Abolishes enzyme activity without affecting
FT ability to form a stable covalent adduct with the ADP-
FT ribosylated substrate."
FT /evidence="ECO:0000269|PubMed:21849506,
FT ECO:0000269|PubMed:23481255"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4J5R"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2LGR"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4J5R"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:4J5R"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4J5R"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4J5Q"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:4J5R"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4J5R"
SQ SEQUENCE 152 AA; 17025 MW; 8CC43CBDABA73E0B CRC64;
MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK KFGGVQELLN
QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL EAMKSHCLKN GVTDLSMPRI
GCGLDRLQWE NVSAMIEEVF EATDIKITVY TL
