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Protein

O-acetyl-ADP-ribose deacetylase 1

Gene

OARD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.

Enzyme regulationi

Subject to competitive inhibition by the product ADP-ribose.1 Publication

Kineticsi

  1. KM=182 µM for O-acetyl-ADP-ribose1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Substrate; via amide nitrogen
    Active sitei125 – 1251Proton acceptor1 Publication
    Binding sitei152 – 1521Substrate; via carboxylate

    GO - Molecular functioni

    • deacetylase activity Source: UniProtKB
    • purine nucleoside binding Source: UniProtKB

    GO - Biological processi

    • purine nucleoside metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    O-acetyl-ADP-ribose deacetylase 1 (EC:3.5.1.-)
    Gene namesi
    Name:OARD1
    Synonyms:C6orf130
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21257. OARD1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321H → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi33 – 331C → S: No effect. 1 Publication
    Mutagenesisi35 – 351S → A: Reduced catalytic activity. No effect on affinity towards substrate. 1 Publication
    Mutagenesisi83 – 831T → A: Reduced catalytic activity. No effect on affinity towards substrate.
    Mutagenesisi123 – 1231G → E: Abolishes enzyme activity. 1 Publication
    Mutagenesisi125 – 1251D → A: Abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134879529.

    Polymorphism and mutation databases

    BioMutaiOARD1.
    DMDMi38258957.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 152151O-acetyl-ADP-ribose deacetylase 1PRO_0000089529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei4 – 41Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y530.
    PaxDbiQ9Y530.
    PRIDEiQ9Y530.

    PTM databases

    PhosphoSiteiQ9Y530.

    Expressioni

    Gene expression databases

    BgeeiQ9Y530.
    CleanExiHS_C6orf130.
    ExpressionAtlasiQ9Y530. baseline and differential.
    GenevisibleiQ9Y530. HS.

    Organism-specific databases

    HPAiHPA029036.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PARP1P098745EBI-8502288,EBI-355676
    PARP10Q53GL73EBI-8502288,EBI-2857573

    Protein-protein interaction databases

    BioGridi128727. 3 interactions.
    IntActiQ9Y530. 2 interactions.
    STRINGi9606.ENSP00000416829.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196Combined sources
    Helixi21 – 233Combined sources
    Beta strandi28 – 358Combined sources
    Beta strandi41 – 433Combined sources
    Helixi45 – 528Combined sources
    Helixi55 – 617Combined sources
    Beta strandi67 – 737Combined sources
    Beta strandi76 – 8611Combined sources
    Helixi93 – 11018Combined sources
    Beta strandi114 – 1174Combined sources
    Helixi123 – 1253Combined sources
    Helixi129 – 14012Combined sources
    Beta strandi146 – 1516Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EEENMR-A11-152[»]
    2L8RNMR-A3-152[»]
    2LGRNMR-A2-152[»]
    4J5QX-ray1.35A7-152[»]
    4J5RX-ray1.25A/B11-152[»]
    4J5SX-ray1.55A/B/C/D11-152[»]
    ProteinModelPortaliQ9Y530.
    SMRiQ9Y530. Positions 12-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 152151MacroPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1257Substrate binding

    Sequence similaritiesi

    Contains 1 Macro domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG72109.
    GeneTreeiENSGT00390000006988.
    HOGENOMiHOG000012894.
    HOVERGENiHBG050914.
    InParanoidiQ9Y530.
    OMAiLFACPQT.
    PhylomeDBiQ9Y530.
    TreeFamiTF324128.

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    [Graphical view]
    PROSITEiPS51154. MACRO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y530-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK
    60 70 80 90 100
    KFGGVQELLN QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL
    110 120 130 140 150
    EAMKSHCLKN GVTDLSMPRI GCGLDRLQWE NVSAMIEEVF EATDIKITVY

    TL
    Length:152
    Mass (Da):17,025
    Last modified:November 7, 2003 - v2
    Checksum:i8CC43CBDABA73E0B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK290939 mRNA. Translation: BAF83628.1.
    AK313361 mRNA. Translation: BAG36161.1.
    AL031778 Genomic DNA. Translation: CAI20285.1.
    CH471081 Genomic DNA. Translation: EAX04011.1.
    BC011709 mRNA. Translation: AAH11709.1.
    CCDSiCCDS34445.1.
    RefSeqiNP_659500.1. NM_145063.2.
    UniGeneiHs.227457.

    Genome annotation databases

    EnsembliENST00000424266; ENSP00000416829; ENSG00000124596.
    ENST00000463088; ENSP00000420193; ENSG00000124596.
    ENST00000468811; ENSP00000420601; ENSG00000124596.
    ENST00000479950; ENSP00000420484; ENSG00000124596.
    GeneIDi221443.
    KEGGihsa:221443.
    UCSCiuc003opm.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK290939 mRNA. Translation: BAF83628.1.
    AK313361 mRNA. Translation: BAG36161.1.
    AL031778 Genomic DNA. Translation: CAI20285.1.
    CH471081 Genomic DNA. Translation: EAX04011.1.
    BC011709 mRNA. Translation: AAH11709.1.
    CCDSiCCDS34445.1.
    RefSeqiNP_659500.1. NM_145063.2.
    UniGeneiHs.227457.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EEENMR-A11-152[»]
    2L8RNMR-A3-152[»]
    2LGRNMR-A2-152[»]
    4J5QX-ray1.35A7-152[»]
    4J5RX-ray1.25A/B11-152[»]
    4J5SX-ray1.55A/B/C/D11-152[»]
    ProteinModelPortaliQ9Y530.
    SMRiQ9Y530. Positions 12-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi128727. 3 interactions.
    IntActiQ9Y530. 2 interactions.
    STRINGi9606.ENSP00000416829.

    PTM databases

    PhosphoSiteiQ9Y530.

    Polymorphism and mutation databases

    BioMutaiOARD1.
    DMDMi38258957.

    Proteomic databases

    MaxQBiQ9Y530.
    PaxDbiQ9Y530.
    PRIDEiQ9Y530.

    Protocols and materials databases

    DNASUi221443.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000424266; ENSP00000416829; ENSG00000124596.
    ENST00000463088; ENSP00000420193; ENSG00000124596.
    ENST00000468811; ENSP00000420601; ENSG00000124596.
    ENST00000479950; ENSP00000420484; ENSG00000124596.
    GeneIDi221443.
    KEGGihsa:221443.
    UCSCiuc003opm.3. human.

    Organism-specific databases

    CTDi221443.
    GeneCardsiGC06M041001.
    H-InvDBHIX0005859.
    HGNCiHGNC:21257. OARD1.
    HPAiHPA029036.
    MIMi614393. gene.
    neXtProtiNX_Q9Y530.
    PharmGKBiPA134879529.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG72109.
    GeneTreeiENSGT00390000006988.
    HOGENOMiHOG000012894.
    HOVERGENiHBG050914.
    InParanoidiQ9Y530.
    OMAiLFACPQT.
    PhylomeDBiQ9Y530.
    TreeFamiTF324128.

    Miscellaneous databases

    EvolutionaryTraceiQ9Y530.
    GenomeRNAii221443.
    NextBioi91343.
    PROiQ9Y530.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y530.
    CleanExiHS_C6orf130.
    ExpressionAtlasiQ9Y530. baseline and differential.
    GenevisibleiQ9Y530. HS.

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    [Graphical view]
    PROSITEiPS51154. MACRO. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Solution structure of the A1PP domain from human protein C6orf130."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 11-152.
    10. "Solution structure of human C6orf130, a putative Macro domain."
      Center for eukaryotic structural genomics (CESG)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR.
    11. "Orphan macrodomain (human C6ORF130) is an o-acyl-ADP-ribose deacylase: solution structure and catalytic properties."
      Peterson F.C., Chen D., Lytle B.L., Rossi M.N., Ahel I., Denu J.M., Volkman B.F.
      J. Biol. Chem. 286:35955-35965(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH ADENOSINE-5-DIPHOSPHORIBOSE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-32; CYS-33; SER-35; GLY-123 AND ASP-125, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiOARD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y530
    Secondary accession number(s): A6NEK4, A8K4H4, Q96F23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 7, 2003
    Last modified: July 22, 2015
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.