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Q8VIJ5 (NCOAT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional protein NCOAT
Alternative name(s):
Meningioma-expressed antigen 5
Nuclear cytoplasmic O-GlcNAcase and acetyltransferase

Including the following 2 domains:

  1. Beta-hexosaminidase
    EC=3.2.1.52
    Alternative name(s):
    Beta-N-acetylhexosaminidase
    Hexosaminidase C
    N-acetyl-beta-D-glucosaminidase
    N-acetyl-beta-glucosaminidase
    O-GlcNAcase
  2. Histone acetyltransferase
    Short name=HAT
    EC=2.3.1.48
Gene names
Name:Mgea5
Synonyms:Hexc, Mea5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses hyaluronidase activity By similarity. Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3. Ref.2 Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Enzyme regulation

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. Ref.3

Subunit structure

Monomer. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Interacts with CLOCK By similarity. According to Ref.3 it is a heterodimer of an alpha and beta chain. Ref.3

Subcellular location

Nucleus. Cytoplasm Ref.3.

Tissue specificity

Ubiquitous. Expressed at highest levels in the brain and spleen. Ref.3

Post-translational modification

Proteolytically cleaved by caspase-3 By similarity.

Biophysicochemical properties

Kinetic parameters:

KM=2.55 mM for pNP-O-GlcNAc Ref.3

pH dependence:

Optimum pH is 6.4. Activity decreases sharply at pH below 5.0.

Temperature dependence:

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionAcyltransferase
Glycosidase
Hydrolase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine metabolic process

Inferred from mutant phenotype PubMed 19139380. Source: RGD

aging

Inferred from expression pattern PubMed 18185980. Source: RGD

dATP metabolic process

Inferred from mutant phenotype PubMed 17573462. Source: RGD

histone acetylation

Inferred from mutant phenotype Ref.2. Source: GOC

necrotic cell death

Inferred from mutant phenotype PubMed 16899550. Source: RGD

negative regulation of cardiac muscle adaptation

Inferred from mutant phenotype PubMed 17573462. Source: RGD

negative regulation of protein glycosylation

Inferred from mutant phenotype PubMed 16332679. Source: RGD

positive regulation of DNA metabolic process

Inferred from mutant phenotype PubMed 19139380. Source: RGD

positive regulation of calcium ion transport

Inferred from mutant phenotype PubMed 19139380. Source: RGD

positive regulation of calcium ion transport into cytosol

Inferred from mutant phenotype PubMed 16107505. Source: RGD

positive regulation of cell killing

Inferred from mutant phenotype PubMed 19139380. Source: RGD

positive regulation of glucose import

Inferred from mutant phenotype PubMed 16000877. Source: RGD

positive regulation of growth hormone secretion

Inferred from mutant phenotype PubMed 12242036. Source: RGD

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 17095531. Source: RGD

positive regulation of mitochondrial depolarization

Inferred from mutant phenotype PubMed 19139380. Source: RGD

positive regulation of protein complex disassembly

Inferred from mutant phenotype PubMed 17573462. Source: RGD

positive regulation of proteolysis

Inferred from mutant phenotype PubMed 17573462. Source: RGD

protein targeting to membrane

Inferred from mutant phenotype PubMed 16000877. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 19139380. Source: RGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

histone acetyltransferase activity

Inferred from mutant phenotype Ref.2. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VIJ5-1)

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.
Isoform 2 (identifier: Q8VIJ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     250-398: Missing.
Note: Lack hexosaminidase activity.
Isoform 3 (identifier: Q8VIJ5-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916Bifunctional protein NCOAT
PRO_0000252120

Regions

Region583 – 916334Histone acetyltransferase activity
Region695 – 814120Required for histone H4 binding By similarity

Sites

Active site1751Nucleophile; for O-GlcNAcase activity By similarity
Active site1771Proton donor; for O-GlcNAcase activity By similarity

Amino acid modifications

Modified residue3641Phosphoserine By similarity
Disulfide bond777 ↔ 793 By similarity

Natural variations

Alternative sequence250 – 398149Missing in isoform 2.
VSP_020873
Alternative sequence250 – 34596Missing in isoform 3.
VSP_020874

Experimental info

Mutagenesis8531D → N: Loss of histone acetyltransferase activity. Ref.2
Mutagenesis8841D → N: Loss of histone acetyltransferase activity. Ref.2
Mutagenesis8911Y → F: Loss of histone acetyltransferase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4BA1746F0AF2E380

FASTA916102,918
        10         20         30         40         50         60 
MVQKESQAAL EERESERNAN PASVSGASLE PSAAPAPGED NPSGAGAAAG TGAAGGARRF 

        70         80         90        100        110        120 
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM 

       130        140        150        160        170        180 
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM 

       190        200        210        220        230        240 
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPSVSQ SPYLRTVGEK 

       250        260        270        280        290        300 
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS 

       310        320        330        340        350        360 
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE 

       370        380        390        400        410        420 
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKTS VVDGTPLVAA 

       430        440        450        460        470        480 
PSLNATTVVT TVYQEPIMSQ GAALSGEPSA LTKEEEKKQP DEEPMDMVVE KQEESEHKSD 

       490        500        510        520        530        540 
NQILTEIVEA KMAEELKPMD TDKESIAESK SPEMSMQEDC INDIAPMQTD EQANKEQFVP 

       550        560        570        580        590        600 
GPNEKPLYAA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD 

       610        620        630        640        650        660 
SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW 

       670        680        690        700        710        720 
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY 

       730        740        750        760        770        780 
FPKDEASVYK ICREMYDDGV GLPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA 

       790        800        810        820        830        840 
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP 

       850        860        870        880        890        900 
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA 

       910 
KMEGFPKDVV ILGRSL 

« Hide

Isoform 2 [UniParc].

Checksum: 7DD1EF0F9D55E766
Show »

FASTA76786,010
Isoform 3 [UniParc].

Checksum: 0A62BBF2AF31A0FD
Show »

FASTA82091,993

References

[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]"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, FUNCTION, MUTAGENESIS OF ASP-853; ASP-884 AND TYR-891.
Strain: GK and Sprague-Dawley.
[3]"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, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY039679 mRNA. Translation: AAK72103.1.
RefSeqNP_571979.1. NM_131904.1.
UniGeneRn.162539.

3D structure databases

ProteinModelPortalQ8VIJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000024198.

Protein family/group databases

CAZyGH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSiteQ8VIJ5.

Proteomic databases

PaxDbQ8VIJ5.
PRIDEQ8VIJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000065172; ENSRNOP00000059568; ENSRNOG00000017822. [Q8VIJ5-1]
GeneID154968.
KEGGrno:154968.
UCSCRGD:621077. rat. [Q8VIJ5-1]

Organism-specific databases

CTD10724.
RGD621077. Mgea5.

Phylogenomic databases

eggNOGCOG0454.
GeneTreeENSGT00390000007726.
HOGENOMHOG000044964.
HOVERGENHBG053044.
InParanoidQ8VIJ5.
KOK15719.
OMALIKVDIH.
OrthoDBEOG7P02H7.
PhylomeDBQ8VIJ5.

Gene expression databases

GenevestigatorQ8VIJ5.

Family and domain databases

Gene3D3.40.630.30. 2 hits.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio620868.
PROQ8VIJ5.

Entry information

Entry nameNCOAT_RAT
AccessionPrimary (citable) accession number: Q8VIJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program