Full text data of OARD1
OARD1
(C6orf130)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
O-acetyl-ADP-ribose deacetylase 1; 3.5.1.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
O-acetyl-ADP-ribose deacetylase 1; 3.5.1.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y530
ID OARD1_HUMAN Reviewed; 152 AA.
AC Q9Y530; A6NEK4; A8K4H4; Q96F23;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-NOV-2003, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=O-acetyl-ADP-ribose deacetylase 1;
DE EC=3.5.1.-;
GN Name=OARD1; Synonyms=C6orf130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
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 [9]
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 [10]
RP STRUCTURE BY NMR IN COMPLEX WITH ADENOSINE-5-DIPHOSPHORIBOSE,
RP CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-32; CYS-33;
RP SER-35; GLY-123 AND ASP-125, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
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
RT deacylase: solution structure and catalytic properties.";
RL J. Biol. Chem. 286:35955-35965(2011).
CC -!- FUNCTION: Deacetylates O-acetyl-ADP ribose, a signaling molecule
CC generated by the deacetylation of acetylated lysine residues in
CC histones and other proteins. Catalyzes the deacylation of O-
CC acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-
CC ribose, yielding ADP-ribose plus acetate, propionate and butyrate,
CC respectively.
CC -!- ENZYME REGULATION: Subject to competitive inhibition by the
CC product ADP-ribose.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=182 uM for O-acetyl-ADP-ribose;
CC -!- INTERACTION:
CC P09874:PARP1; NbExp=5; IntAct=EBI-8502288, EBI-355676;
CC Q53GL7:PARP10; NbExp=3; IntAct=EBI-8502288, EBI-2857573;
CC -!- SIMILARITY: Contains 1 Macro domain.
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DR EMBL; AK290939; BAF83628.1; -; mRNA.
DR EMBL; AK313361; BAG36161.1; -; mRNA.
DR EMBL; AL031778; CAI20285.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04011.1; -; Genomic_DNA.
DR EMBL; BC011709; AAH11709.1; -; mRNA.
DR RefSeq; NP_659500.1; NM_145063.2.
DR RefSeq; XP_005248959.1; XM_005248902.1.
DR RefSeq; XP_005248960.1; XM_005248903.1.
DR UniGene; Hs.227457; -.
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 ProteinModelPortal; Q9Y530; -.
DR SMR; Q9Y530; 12-152.
DR IntAct; Q9Y530; 2.
DR STRING; 9606.ENSP00000416829; -.
DR PhosphoSite; Q9Y530; -.
DR DMDM; 38258957; -.
DR PaxDb; Q9Y530; -.
DR PRIDE; Q9Y530; -.
DR DNASU; 221443; -.
DR Ensembl; ENST00000424266; ENSP00000416829; ENSG00000124596.
DR Ensembl; ENST00000463088; ENSP00000420193; ENSG00000124596.
DR Ensembl; ENST00000468811; ENSP00000420601; ENSG00000124596.
DR Ensembl; ENST00000479950; ENSP00000420484; ENSG00000124596.
DR GeneID; 221443; -.
DR KEGG; hsa:221443; -.
DR UCSC; uc003opm.3; human.
DR CTD; 221443; -.
DR GeneCards; GC06M041001; -.
DR H-InvDB; HIX0005859; -.
DR HGNC; HGNC:21257; OARD1.
DR HPA; HPA029036; -.
DR MIM; 614393; gene.
DR neXtProt; NX_Q9Y530; -.
DR PharmGKB; PA134879529; -.
DR eggNOG; NOG72109; -.
DR HOGENOM; HOG000012894; -.
DR HOVERGEN; HBG050914; -.
DR InParanoid; Q9Y530; -.
DR OMA; EAMKTHC; -.
DR EvolutionaryTrace; Q9Y530; -.
DR GenomeRNAi; 221443; -.
DR NextBio; 91343; -.
DR ArrayExpress; Q9Y530; -.
DR Bgee; Q9Y530; -.
DR CleanEx; HS_C6orf130; -.
DR Genevestigator; Q9Y530; -.
DR GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR GO; GO:0001883; F:purine nucleoside binding; IDA:UniProtKB.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
DR InterPro; IPR002589; Macro_dom.
DR Pfam; PF01661; Macro; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydrolase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 152 O-acetyl-ADP-ribose deacetylase 1.
FT /FTId=PRO_0000089529.
FT DOMAIN 2 152 Macro.
FT REGION 119 125 Substrate binding.
FT ACT_SITE 125 125 Proton acceptor.
FT BINDING 21 21 Substrate; via amide nitrogen.
FT BINDING 152 152 Substrate; via carbonyl oxygen.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 4 4 Phosphoserine.
FT MUTAGEN 32 32 H->A: Abolishes enzyme activity.
FT MUTAGEN 33 33 C->S: No effect.
FT MUTAGEN 35 35 S->A: Reduced catalytic activity. No
FT effect on affinity towards substrate.
FT MUTAGEN 83 83 T->A: Reduced catalytic activity. No
FT effect on affinity towards substrate.
FT MUTAGEN 123 123 G->E: Abolishes enzyme activity.
FT MUTAGEN 125 125 D->A: Abolishes enzyme activity.
FT STRAND 14 19
FT HELIX 21 23
FT STRAND 28 35
FT STRAND 41 43
FT HELIX 45 52
FT HELIX 55 61
FT STRAND 67 73
FT STRAND 76 86
FT HELIX 93 110
FT STRAND 114 117
FT HELIX 123 125
FT HELIX 129 140
FT STRAND 146 151
SQ SEQUENCE 152 AA; 17025 MW; 8CC43CBDABA73E0B CRC64;
MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK KFGGVQELLN
QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL EAMKSHCLKN GVTDLSMPRI
GCGLDRLQWE NVSAMIEEVF EATDIKITVY TL
//
ID OARD1_HUMAN Reviewed; 152 AA.
AC Q9Y530; A6NEK4; A8K4H4; Q96F23;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-NOV-2003, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=O-acetyl-ADP-ribose deacetylase 1;
DE EC=3.5.1.-;
GN Name=OARD1; Synonyms=C6orf130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
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 [9]
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 [10]
RP STRUCTURE BY NMR IN COMPLEX WITH ADENOSINE-5-DIPHOSPHORIBOSE,
RP CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-32; CYS-33;
RP SER-35; GLY-123 AND ASP-125, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
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
RT deacylase: solution structure and catalytic properties.";
RL J. Biol. Chem. 286:35955-35965(2011).
CC -!- FUNCTION: Deacetylates O-acetyl-ADP ribose, a signaling molecule
CC generated by the deacetylation of acetylated lysine residues in
CC histones and other proteins. Catalyzes the deacylation of O-
CC acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-
CC ribose, yielding ADP-ribose plus acetate, propionate and butyrate,
CC respectively.
CC -!- ENZYME REGULATION: Subject to competitive inhibition by the
CC product ADP-ribose.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=182 uM for O-acetyl-ADP-ribose;
CC -!- INTERACTION:
CC P09874:PARP1; NbExp=5; IntAct=EBI-8502288, EBI-355676;
CC Q53GL7:PARP10; NbExp=3; IntAct=EBI-8502288, EBI-2857573;
CC -!- SIMILARITY: Contains 1 Macro domain.
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DR EMBL; AK290939; BAF83628.1; -; mRNA.
DR EMBL; AK313361; BAG36161.1; -; mRNA.
DR EMBL; AL031778; CAI20285.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04011.1; -; Genomic_DNA.
DR EMBL; BC011709; AAH11709.1; -; mRNA.
DR RefSeq; NP_659500.1; NM_145063.2.
DR RefSeq; XP_005248959.1; XM_005248902.1.
DR RefSeq; XP_005248960.1; XM_005248903.1.
DR UniGene; Hs.227457; -.
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 ProteinModelPortal; Q9Y530; -.
DR SMR; Q9Y530; 12-152.
DR IntAct; Q9Y530; 2.
DR STRING; 9606.ENSP00000416829; -.
DR PhosphoSite; Q9Y530; -.
DR DMDM; 38258957; -.
DR PaxDb; Q9Y530; -.
DR PRIDE; Q9Y530; -.
DR DNASU; 221443; -.
DR Ensembl; ENST00000424266; ENSP00000416829; ENSG00000124596.
DR Ensembl; ENST00000463088; ENSP00000420193; ENSG00000124596.
DR Ensembl; ENST00000468811; ENSP00000420601; ENSG00000124596.
DR Ensembl; ENST00000479950; ENSP00000420484; ENSG00000124596.
DR GeneID; 221443; -.
DR KEGG; hsa:221443; -.
DR UCSC; uc003opm.3; human.
DR CTD; 221443; -.
DR GeneCards; GC06M041001; -.
DR H-InvDB; HIX0005859; -.
DR HGNC; HGNC:21257; OARD1.
DR HPA; HPA029036; -.
DR MIM; 614393; gene.
DR neXtProt; NX_Q9Y530; -.
DR PharmGKB; PA134879529; -.
DR eggNOG; NOG72109; -.
DR HOGENOM; HOG000012894; -.
DR HOVERGEN; HBG050914; -.
DR InParanoid; Q9Y530; -.
DR OMA; EAMKTHC; -.
DR EvolutionaryTrace; Q9Y530; -.
DR GenomeRNAi; 221443; -.
DR NextBio; 91343; -.
DR ArrayExpress; Q9Y530; -.
DR Bgee; Q9Y530; -.
DR CleanEx; HS_C6orf130; -.
DR Genevestigator; Q9Y530; -.
DR GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR GO; GO:0001883; F:purine nucleoside binding; IDA:UniProtKB.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
DR InterPro; IPR002589; Macro_dom.
DR Pfam; PF01661; Macro; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydrolase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 152 O-acetyl-ADP-ribose deacetylase 1.
FT /FTId=PRO_0000089529.
FT DOMAIN 2 152 Macro.
FT REGION 119 125 Substrate binding.
FT ACT_SITE 125 125 Proton acceptor.
FT BINDING 21 21 Substrate; via amide nitrogen.
FT BINDING 152 152 Substrate; via carbonyl oxygen.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 4 4 Phosphoserine.
FT MUTAGEN 32 32 H->A: Abolishes enzyme activity.
FT MUTAGEN 33 33 C->S: No effect.
FT MUTAGEN 35 35 S->A: Reduced catalytic activity. No
FT effect on affinity towards substrate.
FT MUTAGEN 83 83 T->A: Reduced catalytic activity. No
FT effect on affinity towards substrate.
FT MUTAGEN 123 123 G->E: Abolishes enzyme activity.
FT MUTAGEN 125 125 D->A: Abolishes enzyme activity.
FT STRAND 14 19
FT HELIX 21 23
FT STRAND 28 35
FT STRAND 41 43
FT HELIX 45 52
FT HELIX 55 61
FT STRAND 67 73
FT STRAND 76 86
FT HELIX 93 110
FT STRAND 114 117
FT HELIX 123 125
FT HELIX 129 140
FT STRAND 146 151
SQ SEQUENCE 152 AA; 17025 MW; 8CC43CBDABA73E0B CRC64;
MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK KFGGVQELLN
QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL EAMKSHCLKN GVTDLSMPRI
GCGLDRLQWE NVSAMIEEVF EATDIKITVY TL
//
MIM
614393
*RECORD*
*FIELD* NO
614393
*FIELD* TI
*614393 CHROMOSOME 6 OPEN READING FRAME 130; C6ORF130
;;O-ACYL-ADP-RIBOSE DEACYLASE
read more*FIELD* TX
DESCRIPTION
O-acyl-ADP-ribose is produced by NAD(+)-dependent deacylation of
acyl-modified lysines and can function as a cell signaling molecule.
C6ORF130 is a deacylase that converts O-acetyl-ADP-ribose,
O-propionyl-ADP-ribose, and O-butyryl-ADP-ribose to ADP-ribose and
acetate, propionate, and butyrate, respectively (Peterson et al., 2011).
CLONING
Peterson et al. (2011) found that the deduced 152-amino acid C6ORF130
protein is made up almost entirely of a globular macrodomain. The
C6ORF130 macrodomain shares limited homology with the approximately
140-amino acid macrodomains of MACROD1 (610400) and MACROD2 (611567),
but C6ORF130 lacks the extended N- and C-terminal sequences of these
proteins.
GENE FUNCTION
Peterson et al. (2011) found that recombinant C6ORF130 efficiently
deacylated O-acyl-ADP-ribose, O-propionyl-ADP-ribose, and
O-butyryl-ADP-ribose to produce ADP-ribose and acetate, propionate, and
butyrate, respectively. C6ORF130 showed slight preference for substrates
with shorter acyl chain lengths. Peterson et al. (2011) also showed that
ADP-ribose functioned as a competitive feedback inhibitor. Site-directed
mutagenesis experiments revealed critical roles for ser35 and asp125 of
C6ORF130 in catalysis.
BIOCHEMICAL FEATURES
Using nuclear magnetic resonance spectroscopy, Peterson et al. (2011)
found that the macrodomain of C6ORF130 exhibited the canonical 3-layered
alpha-beta-alpha sandwich, with a central 6-stranded beta-sheet
containing a mixture of anti-parallel and parallel strands and a deep
ligand-binding cleft. ADP-ribose bound deep within the macrodomain
cleft, with the diphosphate ribose portion completely buried. A
beta-alpha loop covered the bound ADP-ribose and appeared to function as
a gate to sequester the substrate and offer flexibility to accommodate
alternative substrates.
MAPPING
Hartz (2011) mapped the C6ORF130 gene to chromosome 6p21.1 based on an
alignment of the C6ORF130 sequence (GenBank GENBANK AJ420538) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/6/2011.
2. Peterson, F. C.; Chen, D.; Lytle, B. L.; Rossi, M. N.; Ahel, I.;
Denu, J. M.; Volkman, B. F.: Orphan macrodomain protein (human C6orf130)
is an O-acyl-ADP-ribose deacylase: solution structure and catalytic
properties. J. Biol. Chem. 286: 35955-35965, 2011.
*FIELD* CD
Patricia A. Hartz: 12/13/2011
*FIELD* ED
mgross: 12/13/2011
*RECORD*
*FIELD* NO
614393
*FIELD* TI
*614393 CHROMOSOME 6 OPEN READING FRAME 130; C6ORF130
;;O-ACYL-ADP-RIBOSE DEACYLASE
read more*FIELD* TX
DESCRIPTION
O-acyl-ADP-ribose is produced by NAD(+)-dependent deacylation of
acyl-modified lysines and can function as a cell signaling molecule.
C6ORF130 is a deacylase that converts O-acetyl-ADP-ribose,
O-propionyl-ADP-ribose, and O-butyryl-ADP-ribose to ADP-ribose and
acetate, propionate, and butyrate, respectively (Peterson et al., 2011).
CLONING
Peterson et al. (2011) found that the deduced 152-amino acid C6ORF130
protein is made up almost entirely of a globular macrodomain. The
C6ORF130 macrodomain shares limited homology with the approximately
140-amino acid macrodomains of MACROD1 (610400) and MACROD2 (611567),
but C6ORF130 lacks the extended N- and C-terminal sequences of these
proteins.
GENE FUNCTION
Peterson et al. (2011) found that recombinant C6ORF130 efficiently
deacylated O-acyl-ADP-ribose, O-propionyl-ADP-ribose, and
O-butyryl-ADP-ribose to produce ADP-ribose and acetate, propionate, and
butyrate, respectively. C6ORF130 showed slight preference for substrates
with shorter acyl chain lengths. Peterson et al. (2011) also showed that
ADP-ribose functioned as a competitive feedback inhibitor. Site-directed
mutagenesis experiments revealed critical roles for ser35 and asp125 of
C6ORF130 in catalysis.
BIOCHEMICAL FEATURES
Using nuclear magnetic resonance spectroscopy, Peterson et al. (2011)
found that the macrodomain of C6ORF130 exhibited the canonical 3-layered
alpha-beta-alpha sandwich, with a central 6-stranded beta-sheet
containing a mixture of anti-parallel and parallel strands and a deep
ligand-binding cleft. ADP-ribose bound deep within the macrodomain
cleft, with the diphosphate ribose portion completely buried. A
beta-alpha loop covered the bound ADP-ribose and appeared to function as
a gate to sequester the substrate and offer flexibility to accommodate
alternative substrates.
MAPPING
Hartz (2011) mapped the C6ORF130 gene to chromosome 6p21.1 based on an
alignment of the C6ORF130 sequence (GenBank GENBANK AJ420538) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/6/2011.
2. Peterson, F. C.; Chen, D.; Lytle, B. L.; Rossi, M. N.; Ahel, I.;
Denu, J. M.; Volkman, B. F.: Orphan macrodomain protein (human C6orf130)
is an O-acyl-ADP-ribose deacylase: solution structure and catalytic
properties. J. Biol. Chem. 286: 35955-35965, 2011.
*FIELD* CD
Patricia A. Hartz: 12/13/2011
*FIELD* ED
mgross: 12/13/2011