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Protein

Protein O-GlcNAcase

Gene

Mgea5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:8034696). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.By similarity1 Publication
Isoform 2: Lacks enzyme activity.1 Publication
Isoform 3: Lacks enzyme activity.1 Publication

Catalytic activityi

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.1 Publication
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.1 Publication
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Enzyme regulationi

Inhibited by Cu2+, Hg2+, Cd2+ and Zn2+ at 1 mM. Not inhibited by Co2+, Mg2+, Ca2+, Mn2+, Fe3+ and EDTA. Also inhibited by sodium chloride at 1M and 2-amino-2-hydroxymethyl-1,3-propanediol (trishydroxymethylaminomethane) at 75mM.1 Publication

Kineticsi

  1. KM=2.55 mM for pNP-O-GlcNAc1 Publication

    pH dependencei

    Optimum pH is 6.4. Activity decreases sharply at pH below 5.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. Less active at room temperature and shows very little activity at 4 degrees Celsius. Loses activity at 57 degrees Celsius within 5 minutes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei67 – 671Substrate; via carbonyl oxygenBy similarity
    Binding sitei98 – 981SubstrateBy similarity
    Binding sitei174 – 1741SubstrateBy similarity
    Active sitei175 – 1751Proton donorBy similarity
    Binding sitei219 – 2191SubstrateBy similarity
    Binding sitei285 – 2851SubstrateBy similarity
    Binding sitei313 – 3131SubstrateBy similarity
    Sitei413 – 4142Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    • beta-N-acetylglucosaminidase activity Source: RGD
    • histone acetyltransferase activity Source: RGD

    GO - Biological processi

    • aging Source: RGD
    • dATP metabolic process Source: RGD
    • histone acetylation Source: GOC
    • N-acetylglucosamine metabolic process Source: RGD
    • necrotic cell death Source: RGD
    • negative regulation of cardiac muscle adaptation Source: RGD
    • negative regulation of protein glycosylation Source: RGD
    • positive regulation of calcium ion transport Source: RGD
    • positive regulation of calcium ion transport into cytosol Source: RGD
    • positive regulation of cell killing Source: RGD
    • positive regulation of DNA metabolic process Source: RGD
    • positive regulation of glucose import Source: RGD
    • positive regulation of growth hormone secretion Source: RGD
    • positive regulation of insulin secretion Source: RGD
    • positive regulation of mitochondrial depolarization Source: RGD
    • positive regulation of protein complex disassembly Source: RGD
    • positive regulation of proteolysis Source: RGD
    • protein deglycosylation Source: Ensembl
    • protein targeting to membrane Source: RGD
    • response to steroid hormone Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein O-GlcNAcase2 Publications (EC:3.2.1.1691 Publication)
    Short name:
    OGA
    Alternative name(s):
    Beta-N-acetylhexosaminidase
    Beta-hexosaminidase
    Bifunctional protein NCOAT1 Publication
    Meningioma-expressed antigen 5
    N-acetyl-beta-D-glucosaminidase (EC:3.2.1.521 Publication)
    N-acetyl-beta-glucosaminidase
    Gene namesi
    Name:Mgea5
    Synonyms:Hexc, Mea5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi621077. Mgea5.

    Subcellular locationi

    • Nucleus 1 Publication
    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: Ensembl
    • membrane Source: Ensembl
    • mitochondrion Source: RGD
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 916916Protein O-GlcNAcasePRO_0000252120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei364 – 3641PhosphoserineBy similarity

    Post-translational modificationi

    Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8VIJ5.
    PRIDEiQ8VIJ5.

    PTM databases

    PhosphoSiteiQ8VIJ5.

    Expressioni

    Tissue specificityi

    Detected in spleen (at protein level). Ubiquitous. Expressed at highest levels in the brain and spleen.1 Publication

    Gene expression databases

    ExpressionAtlasiQ8VIJ5. baseline and differential.
    GenevisibleiQ8VIJ5. RN.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CLOCK (By similarity).By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000059568.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VIJ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 2803Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 84 family.Curated

    Phylogenomic databases

    eggNOGiCOG0454.
    HOGENOMiHOG000044964.
    HOVERGENiHBG053044.
    InParanoidiQ8VIJ5.
    KOiK15719.
    OMAiMSGDQEP.
    OrthoDBiEOG7P02H7.
    PhylomeDBiQ8VIJ5.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07555. NAGidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55729. SSF55729. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q8VIJ5-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MVQKESQAAL EERESERNAN PASVSGASLE PSAAPAPGED NPSGAGAAAG
    60 70 80 90 100
    TGAAGGARRF LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD
    110 120 130 140 150
    YKHRMFWREM YSVEEAEQLM TLISAAREYE IEFIYAISPG LDITFSNPKE
    160 170 180 190 200
    VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM CAADKEVFSS FAHAQVSITN
    210 220 230 240 250
    EIYQYLGEPE TFLFCPTEYC GTFCYPSVSQ SPYLRTVGEK LLPGIEVLWT
    260 270 280 290 300
    GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
    310 320 330 340 350
    TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED
    360 370 380 390 400
    STVSIQIKLE NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR
    410 420 430 440 450
    QVAHSGAKTS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPSA
    460 470 480 490 500
    LTKEEEKKQP DEEPMDMVVE KQEESEHKSD NQILTEIVEA KMAEELKPMD
    510 520 530 540 550
    TDKESIAESK SPEMSMQEDC INDIAPMQTD EQANKEQFVP GPNEKPLYAA
    560 570 580 590 600
    EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
    610 620 630 640 650
    SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI
    660 670 680 690 700
    MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND
    710 720 730 740 750
    LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GLPFQSQPDL
    760 770 780 790 800
    IGDKLVGGLL SLSLDYCFVL EDEDGICGYA LGTVDVTPFI KKCKISWIPF
    810 820 830 840 850
    MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP SLIKMDIHKK
    860 870 880 890 900
    VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
    910
    KMEGFPKDVV ILGRSL
    Length:916
    Mass (Da):102,918
    Last modified:March 1, 2002 - v1
    Checksum:i4BA1746F0AF2E380
    GO
    Isoform 2 (identifier: Q8VIJ5-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         250-398: Missing.

    Note: Lack hexosaminidase activity.
    Show »
    Length:767
    Mass (Da):86,010
    Checksum:i7DD1EF0F9D55E766
    GO
    Isoform 3 (identifier: Q8VIJ5-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         250-345: Missing.

    Note: Lack hexosaminidase activity.
    Show »
    Length:820
    Mass (Da):91,993
    Checksum:i0A62BBF2AF31A0FD
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei250 – 398149Missing in isoform 2. CuratedVSP_020873Add
    BLAST
    Alternative sequencei250 – 34596Missing in isoform 3. CuratedVSP_020874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY039679 mRNA. Translation: AAK72103.1.
    RefSeqiNP_571979.1. NM_131904.1. [Q8VIJ5-1]
    UniGeneiRn.162539.

    Genome annotation databases

    GeneIDi154968.
    KEGGirno:154968.
    UCSCiRGD:621077. rat. [Q8VIJ5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY039679 mRNA. Translation: AAK72103.1.
    RefSeqiNP_571979.1. NM_131904.1. [Q8VIJ5-1]
    UniGeneiRn.162539.

    3D structure databases

    ProteinModelPortaliQ8VIJ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000059568.

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    PTM databases

    PhosphoSiteiQ8VIJ5.

    Proteomic databases

    PaxDbiQ8VIJ5.
    PRIDEiQ8VIJ5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi154968.
    KEGGirno:154968.
    UCSCiRGD:621077. rat. [Q8VIJ5-1]

    Organism-specific databases

    CTDi10724.
    RGDi621077. Mgea5.

    Phylogenomic databases

    eggNOGiCOG0454.
    HOGENOMiHOG000044964.
    HOVERGENiHBG053044.
    InParanoidiQ8VIJ5.
    KOiK15719.
    OMAiMSGDQEP.
    OrthoDBiEOG7P02H7.
    PhylomeDBiQ8VIJ5.

    Miscellaneous databases

    NextBioi620868.
    PROiQ8VIJ5.

    Gene expression databases

    ExpressionAtlasiQ8VIJ5. baseline and differential.
    GenevisibleiQ8VIJ5. RN.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07555. NAGidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55729. SSF55729. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "The O-GlcNAcase gene is a candidate for diabetes susceptibility in GK rats."
      Liu K., Paterson A.J., Van Tine B.A., Konrad R.J., Parlow A.F., Jimi S., Chin E. Jr., Kudlow J.E.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Fischer 344.
    2. "Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol."
      Dong D.-L., Hart G.W.
      J. Biol. Chem. 269:19321-19330(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Spleen.
    3. "Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities."
      Toleman C., Paterson A.J., Whisenhunt T.R., Kudlow J.E.
      J. Biol. Chem. 279:53665-53673(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ISOFORMS 2 AND 3.
      Strain: GK and Sprague-Dawley.
    4. "Location and characterization of the O-GlcNAcase active site."
      Toleman C., Paterson A.J., Kudlow J.E.
      Biochim. Biophys. Acta 1760:829-839(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORMS 2 AND 3, LACK OF CATALYTIC ACTIVITY OF ISOFORMS 2 AND 3.

    Entry informationi

    Entry nameiOGA_RAT
    AccessioniPrimary (citable) accession number: Q8VIJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: March 1, 2002
    Last modified: July 22, 2015
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was initially identified as a bi-functional protein that has an N-terminal domain with O-GlcNAcase activity and a C-terminal domain that has histone acetyltransferase activity (PubMed:15485860). The protein has apparent histone acetyltransferase activity when expressed in mammalian cells, but not when expressed in bacterial cells (PubMed:15485860), suggesting that the histone acetyltransferase activity might be due to the presence of a contaminant. Characterization of the human ortholog shows that this protein does not bind acetyl-CoA and therefore cannot have acetyltransferase activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. 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.