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OARD1_MOUSE
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   03-AUG-2022, entry version 113.
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; Q8R5F3; -.
DR   PRIDE; Q8R5F3; -.
DR   ProteomicsDB; 291931; -.
DR   Antibodypedia; 29984; 48 antibodies from 13 providers.
DR   DNASU; 106821; -.
DR   Ensembl; ENSMUST00000046651; ENSMUSP00000039280; ENSMUSG00000040771.
DR   Ensembl; ENSMUST00000167180; ENSMUSP00000130802; ENSMUSG00000040771.
DR   GeneID; 106821; -.
DR   KEGG; mmu:106821; -.
DR   UCSC; uc008cxu.2; mouse.
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; ERIKCVK; -.
DR   OrthoDB; 1416296at2759; -.
DR   PhylomeDB; Q8R5F3; -.
DR   TreeFam; TF324128; -.
DR   BioGRID-ORCS; 106821; 3 hits in 72 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 61 other 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: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   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
 
 
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