OGA_HUMAN
ID OGA_HUMAN Reviewed; 916 AA.
AC O60502; B7WPB9; D3DR79; E9PGF9; O75166; Q86WV0; Q8IV98; Q9BVA5; Q9HAR0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:11148210, ECO:0000303|PubMed:11788610, ECO:0000305};
DE Short=OGA {ECO:0000303|PubMed:20863279};
DE EC=3.2.1.169 {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600, ECO:0000305|PubMed:20673219};
DE AltName: Full=Beta-N-acetylglucosaminidase {ECO:0000303|PubMed:11148210};
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase;
DE AltName: Full=Meningioma-expressed antigen 5 {ECO:0000303|PubMed:9811929};
DE AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE AltName: Full=Nuclear cytoplasmic O-GlcNAcase and acetyltransferase;
DE Short=NCOAT;
GN Name=OGA {ECO:0000312|HGNC:HGNC:7056};
GN Synonyms=HEXC, KIAA0679, MEA5, MGEA5;
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 [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Meningioma;
RX PubMed=9811929; DOI=10.1093/hmg/7.12.1859;
RA Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E.;
RT "Novel immunogenic antigen homologous to hyaluronidase in meningioma.";
RL Hum. Mol. Genet. 7:1859-1872(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=11341771; DOI=10.1006/bbrc.2001.4815;
RA Comtesse N., Maldener E., Meese E.;
RT "Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase
RT and a beta-N-acetylglucosaminidase.";
RL Biochem. Biophys. Res. Commun. 283:634-640(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=11148210; DOI=10.1074/jbc.m010420200;
RA Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W.;
RT "Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and
RT characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from
RT human brain.";
RL J. Biol. Chem. 276:9838-9845(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-602.
RC TISSUE=Cervix, Eye, and Skin;
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11788610; DOI=10.1074/jbc.m109656200;
RA Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., Hart G.W.;
RT "Dynamic O-glycosylation of nuclear and cytosolic proteins: further
RT characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-
RT GlcNAcase.";
RL J. Biol. Chem. 277:1755-1761(2002).
RN [10]
RP ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-174 AND ASP-175.
RX PubMed=16533067; DOI=10.1021/bi052370b;
RA Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., Vocadlo D.J.;
RT "Identification of Asp174 and Asp175 as the key catalytic residues of human
RT O-GlcNAcase by functional analysis of site-directed mutants.";
RL Biochemistry 45:3835-3844(2006).
RN [11]
RP PTM, SITE, MUTAGENESIS OF ASP-413, AND CATALYTIC ACTIVITY.
RX PubMed=18586680; DOI=10.1074/jbc.m804116200;
RA Butkinaree C., Cheung W.D., Park S., Park K., Barber M., Hart G.W.;
RT "Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3
RT during apoptosis.";
RL J. Biol. Chem. 283:23557-23566(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-69; ASP-175; VAL-255;
RP TYR-286; ASP-287 AND TRP-679.
RX PubMed=20863279; DOI=10.1042/bj20101338;
RA Schimpl M., Schuttelkopf A.W., Borodkin V.S., van Aalten D.M.;
RT "Human OGA binds substrates in a conserved peptide recognition groove.";
RL Biochem. J. 432:1-7(2010).
RN [16]
RP FUNCTION OF ISOFORMS 1 AND 3, AND CATALYTIC ACTIVITY.
RX PubMed=20673219; DOI=10.1134/s0006297910070175;
RA Li J., Huang C.L., Zhang L.W., Lin L., Li Z.H., Zhang F.W., Wang P.;
RT "Isoforms of human O-GlcNAcase show distinct catalytic efficiencies.";
RL Biochemistry (Mosc.) 75:938-943(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [22]
RP LACK OF ACETYLTRANSFERASE ACTIVITY, AND FUNCTION.
RX PubMed=24088714; DOI=10.1098/rsob.130021;
RA Rao F.V., Schuttelkopf A.W., Dorfmueller H.C., Ferenbach A.T.,
RA Navratilova I., van Aalten D.M.;
RT "Structure of a bacterial putative acetyltransferase defines the fold of
RT the human O-GlcNAcase C-terminal domain.";
RL Open Biol. 3:130021-130021(2013).
RN [23]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN TAX.
RX PubMed=28742148; DOI=10.1371/journal.ppat.1006518;
RA Groussaud D., Khair M., Tollenaere A.I., Waast L., Kuo M.S., Mangeney M.,
RA Martella C., Fardini Y., Coste S., Souidi M., Benit L., Pique C., Issad T.;
RT "Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein
RT facilitates viral transcription.";
RL PLoS Pathog. 13:E1006518-E1006518(2017).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 402-408, MUTAGENESIS OF TYR-69,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22365600; DOI=10.1016/j.chembiol.2012.01.011;
RA Schimpl M., Borodkin V.S., Gray L.J., van Aalten D.M.;
RT "Synergy of peptide and sugar in O-GlcNAcase substrate recognition.";
RL Chem. Biol. 19:173-178(2012).
CC -!- FUNCTION: [Isoform 1]: Cleaves GlcNAc but not GalNAc from O-
CC glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-
CC methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-
CC GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does
CC not bind acetyl-CoA and does not have histone acetyltransferase
CC activity (PubMed:24088714). {ECO:0000269|PubMed:11148210,
CC ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219,
CC ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714}.
CC -!- FUNCTION: [Isoform 3]: Cleaves GlcNAc but not GalNAc from O-
CC glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate
CC but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in
CC vitro), but has about six times lower specific activity than isoform 1.
CC {ECO:0000269|PubMed:20673219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O =
CC L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227;
CC EC=3.2.1.169; Evidence={ECO:0000269|PubMed:11148210,
CC ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680,
CC ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600,
CC ECO:0000305|PubMed:20673219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O
CC = L-threonyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840,
CC ChEBI:CHEBI:506227; EC=3.2.1.169;
CC Evidence={ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610,
CC ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279,
CC ECO:0000269|PubMed:22365600, ECO:0000305|PubMed:20673219};
CC -!- ACTIVITY REGULATION: Inhibited by N-acetylglucosamine and not N-
CC acetylgalactosamine. {ECO:0000269|PubMed:11148210}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for pNP-GlcNAc {ECO:0000269|PubMed:11788610};
CC Vmax=652 umol/min/mg enzyme with pNP-GLcNAc as substrate
CC {ECO:0000269|PubMed:11788610};
CC pH dependence:
CC Optimum pH is 5.7-7. {ECO:0000269|PubMed:11148210};
CC -!- SUBUNIT: Monomer (PubMed:11788610). Interacts with CLOCK (By
CC similarity). {ECO:0000250|UniProtKB:Q9EQQ9,
CC ECO:0000269|PubMed:11788610}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
CC virus 1/HTLV-1 protein Tax; this interaction increases Tax interacting
CC partner CREB1 O-GlcNAcylation. {ECO:0000269|PubMed:28742148}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:11341771}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771,
CC ECO:0000269|PubMed:11788610}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60502-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60502-2; Sequence=VSP_020866, VSP_020869;
CC Name=3; Synonyms=MGEA5s;
CC IsoId=O60502-3; Sequence=VSP_020867, VSP_020868;
CC Name=4;
CC IsoId=O60502-4; Sequence=VSP_020866;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Shows highest expression in the brain,
CC placenta and pancreas. {ECO:0000269|PubMed:11148210,
CC ECO:0000269|PubMed:11341771}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. The
CC fragments interact with each other; cleavage does not decrease enzyme
CC activity. {ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000305}.
CC -!- CAUTION: The mouse and rat orthologs were initially identified as bi-
CC functional proteins containing an N-terminal domain with O-GlcNAcase
CC activity and a C-terminal domain with histone acetyltransferase
CC activity. The histone acetyltransferase activity was detected only when
CC the protein was expressed in mammalian cells, but not when expressed in
CC bacterial cells, suggesting that the histone acetyltransferase activity
CC might be due to the presence of a contaminant. Comparison of the human
CC protein with a bacterial putative acetyltransferase (AC Q2CEE2) shows
CC that the residues important for acetyl-CoA binding are not conserved,
CC and that the residues proposed to be important for histone
CC acetyltransferase activity are not in a position where they could
CC participate in catalysis. Characterization of the human protein shows
CC that it does not bind acetyl-CoA and therefore cannot have
CC acetyltransferase activity. {ECO:0000269|PubMed:24088714,
CC ECO:0000305|PubMed:24088714}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47877.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA31654.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF036144; AAD05385.2; -; mRNA.
DR EMBL; AF307332; AAG21428.1; -; mRNA.
DR EMBL; AB014579; BAA31654.2; ALT_INIT; mRNA.
DR EMBL; AC010789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49744.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49741.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49742.1; -; Genomic_DNA.
DR EMBL; BC001343; AAH01343.1; -; mRNA.
DR EMBL; BC039583; AAH39583.2; -; mRNA.
DR EMBL; BC047877; AAH47877.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44471.1; -. [O60502-4]
DR CCDS; CCDS7520.1; -. [O60502-1]
DR PIR; T00360; T00360.
DR RefSeq; NP_001135906.1; NM_001142434.1. [O60502-4]
DR RefSeq; NP_036347.1; NM_012215.3. [O60502-1]
DR PDB; 2YDQ; X-ray; 2.60 A; T=402-408.
DR PDB; 5M7R; X-ray; 2.35 A; A/B=1-916.
DR PDB; 5M7S; X-ray; 2.40 A; A/B=1-916.
DR PDB; 5M7T; X-ray; 2.60 A; A/B=1-916.
DR PDB; 5M7U; X-ray; 2.30 A; A/B=1-916.
DR PDB; 5TKE; X-ray; 2.48 A; A/B=60-400, A/B=553-704.
DR PDB; 5UHK; X-ray; 2.97 A; A/C=56-400, B/D=544-705.
DR PDB; 5UHL; X-ray; 3.14 A; A/C=56-400, B/D=544-705.
DR PDB; 5UHO; X-ray; 3.21 A; A/C=56-400, B/D=544-705.
DR PDB; 5UHP; X-ray; 2.79 A; A/B/C/D=14-400, E/F/G/H=554-705.
DR PDB; 5UN8; X-ray; 2.13 A; A/B/C/D=60-400, A/B/C/D=553-704.
DR PDB; 5UN9; X-ray; 2.50 A; A/B=60-400, A/B=553-704.
DR PDB; 5VVO; X-ray; 2.60 A; A/B=60-400, A/B=553-704.
DR PDB; 5VVT; X-ray; 2.80 A; A/C=60-400, A/C=553-704.
DR PDB; 5VVU; X-ray; 2.70 A; A/C=60-400, A/C=553-704.
DR PDB; 5VVV; X-ray; 2.80 A; A/C=60-400, A/C=553-704.
DR PDB; 5VVX; X-ray; 2.90 A; A/C=60-400, A/C=553-704.
DR PDB; 6HKI; X-ray; 3.30 A; A/B=1-916.
DR PDB; 6PM9; X-ray; 2.86 A; A/B/C/D=14-400, E/F/G/H=553-705.
DR PDB; 7OU6; X-ray; 2.41 A; AAA/BBB=1-916.
DR PDBsum; 2YDQ; -.
DR PDBsum; 5M7R; -.
DR PDBsum; 5M7S; -.
DR PDBsum; 5M7T; -.
DR PDBsum; 5M7U; -.
DR PDBsum; 5TKE; -.
DR PDBsum; 5UHK; -.
DR PDBsum; 5UHL; -.
DR PDBsum; 5UHO; -.
DR PDBsum; 5UHP; -.
DR PDBsum; 5UN8; -.
DR PDBsum; 5UN9; -.
DR PDBsum; 5VVO; -.
DR PDBsum; 5VVT; -.
DR PDBsum; 5VVU; -.
DR PDBsum; 5VVV; -.
DR PDBsum; 5VVX; -.
DR PDBsum; 6HKI; -.
DR PDBsum; 6PM9; -.
DR PDBsum; 7OU6; -.
DR AlphaFoldDB; O60502; -.
DR SMR; O60502; -.
DR BioGRID; 115948; 70.
DR IntAct; O60502; 35.
DR MINT; O60502; -.
DR STRING; 9606.ENSP00000354850; -.
DR BindingDB; O60502; -.
DR ChEMBL; CHEMBL5921; -.
DR DrugBank; DB00428; Streptozocin.
DR GuidetoPHARMACOLOGY; 3101; -.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR GlyGen; O60502; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; O60502; -.
DR MetOSite; O60502; -.
DR PhosphoSitePlus; O60502; -.
DR SwissPalm; O60502; -.
DR BioMuta; MGEA5; -.
DR CPTAC; CPTAC-1223; -.
DR EPD; O60502; -.
DR jPOST; O60502; -.
DR MassIVE; O60502; -.
DR MaxQB; O60502; -.
DR PaxDb; O60502; -.
DR PeptideAtlas; O60502; -.
DR PRIDE; O60502; -.
DR ProteomicsDB; 20314; -.
DR ProteomicsDB; 49438; -. [O60502-1]
DR ProteomicsDB; 49439; -. [O60502-2]
DR ProteomicsDB; 49440; -. [O60502-3]
DR Antibodypedia; 31340; 191 antibodies from 28 providers.
DR DNASU; 10724; -.
DR Ensembl; ENST00000357797.9; ENSP00000350445.4; ENSG00000198408.14. [O60502-2]
DR Ensembl; ENST00000361464.8; ENSP00000354850.3; ENSG00000198408.14. [O60502-1]
DR Ensembl; ENST00000370094.7; ENSP00000359112.3; ENSG00000198408.14. [O60502-3]
DR Ensembl; ENST00000439817.5; ENSP00000409973.1; ENSG00000198408.14. [O60502-4]
DR GeneID; 10724; -.
DR KEGG; hsa:10724; -.
DR MANE-Select; ENST00000361464.8; ENSP00000354850.3; NM_012215.5; NP_036347.1.
DR UCSC; uc001ktv.3; human. [O60502-1]
DR CTD; 10724; -.
DR DisGeNET; 10724; -.
DR GeneCards; OGA; -.
DR HGNC; HGNC:7056; OGA.
DR HPA; ENSG00000198408; Low tissue specificity.
DR MIM; 604039; gene.
DR neXtProt; NX_O60502; -.
DR OpenTargets; ENSG00000198408; -.
DR PharmGKB; PA30787; -.
DR VEuPathDB; HostDB:ENSG00000198408; -.
DR eggNOG; KOG3698; Eukaryota.
DR GeneTree; ENSGT00390000007726; -.
DR HOGENOM; CLU_009837_1_0_1; -.
DR InParanoid; O60502; -.
DR OMA; ICTRTYL; -.
DR OrthoDB; 159999at2759; -.
DR PhylomeDB; O60502; -.
DR TreeFam; TF313732; -.
DR BioCyc; MetaCyc:HS03036-MON; -.
DR BRENDA; 3.2.1.169; 2681.
DR BRENDA; 3.2.1.35; 2681.
DR PathwayCommons; O60502; -.
DR SignaLink; O60502; -.
DR SIGNOR; O60502; -.
DR BioGRID-ORCS; 10724; 113 hits in 1091 CRISPR screens.
DR ChiTaRS; MGEA5; human.
DR GeneWiki; MGEA5; -.
DR GenomeRNAi; 10724; -.
DR Pharos; O60502; Tchem.
DR PRO; PR:O60502; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O60502; protein.
DR Bgee; ENSG00000198408; Expressed in sperm and 203 other tissues.
DR ExpressionAtlas; O60502; baseline and differential.
DR Genevisible; O60502; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102571; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; TAS:ProtInc.
DR GO; GO:0006516; P:glycoprotein catabolic process; TAS:ProtInc.
DR GO; GO:0009100; P:glycoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; NAS:ParkinsonsUK-UCL.
DR DisProt; DP02479; -.
DR IDEAL; IID00643; -.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Glycosidase;
KW Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..916
FT /note="Protein O-GlcNAcase"
FT /id="PRO_0000252118"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16533067"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 278..280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT SITE 413..414
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:18586680"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 346..398
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_020866"
FT VAR_SEQ 663..677
FT /note="CRSHSSAQFLIGDQE -> RCTRNNLFSSNILSL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9811929"
FT /id="VSP_020867"
FT VAR_SEQ 678..916
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9811929"
FT /id="VSP_020868"
FT VAR_SEQ 691..704
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020869"
FT VARIANT 46
FT /note="G -> E (in dbSNP:rs3740421)"
FT /id="VAR_027761"
FT VARIANT 602
FT /note="E -> K (in dbSNP:rs17853930)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027762"
FT MUTAGEN 69
FT /note="Y->K,Q: Strongly reduces affinity for glycopeptide
FT substrates. Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279,
FT ECO:0000269|PubMed:22365600"
FT MUTAGEN 69
FT /note="Y->S: Strongly reduces affinity for glycopeptide
FT substrates. Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279,
FT ECO:0000269|PubMed:22365600"
FT MUTAGEN 174
FT /note="D->A: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16533067"
FT MUTAGEN 175
FT /note="D->A: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16533067"
FT MUTAGEN 175
FT /note="D->N: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279"
FT MUTAGEN 255
FT /note="V->G,T: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279"
FT MUTAGEN 286
FT /note="Y->S: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279"
FT MUTAGEN 287
FT /note="D->A: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279"
FT MUTAGEN 413
FT /note="D->A: Abrogates cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:18586680"
FT MUTAGEN 679
FT /note="W->N: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20863279"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6PM9"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:5UHP"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 113..128
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5VVU"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5M7R"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5UHK"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:5UN8"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:5UHL"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:5M7R"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:5M7T"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 573..587
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:6HKI"
FT HELIX 605..628
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 634..661
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 662..666
FT /evidence="ECO:0007829|PDB:5M7R"
FT TURN 680..683
FT /evidence="ECO:0007829|PDB:5UN8"
FT HELIX 684..692
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 694..699
FT /evidence="ECO:0007829|PDB:5UN8"
FT TURN 710..712
FT /evidence="ECO:0007829|PDB:5M7R"
SQ SEQUENCE 916 AA; 102915 MW; 01F8A64A9B1475C6 CRC64;
MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV AGAAGGARRF
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKAS VVDGTPLVAA
PSLNATTVVT TVYQEPIMSQ GAALSGEPTT LTKEEEKKQP DEEPMDMVVE KQEETDHKND
NQILSEIVEA KMAEELKPMD TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP
GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY
FPKDEASVYK ICREMYDDGV GLPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
KMEGFPKDVV ILGRSL
