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Q9EQQ9 (NCOAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 info·DocumentsCustomize 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. Protein O-GlcNAcase
    EC=3.2.1.169
    Alternative name(s):
    Glycoside hydrolase O-GlcNAcase
    Hexosaminidase C
    N-acetyl-beta-D-glucosaminidase
    N-acetyl-beta-glucosaminidase
    O-GlcNAcase
    Short name=OGA
  2. Histone acetyltransferase
    Short name=HAT
    EC=2.3.1.48
Gene names
Name:Mgea5
Synonyms:Hexc, Kiaa0679
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

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. Possesses hyaluronidase activity By similarity. Acetylates 'Lys-8' of histone H4. Ref.6

Catalytic activity

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.

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

Subunit structure

Monomer By similarity. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Interacts with CLOCK. Ref.6 Ref.11

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Developmental stage

Expressed throughout development from blastocyst stage to embryonic day 16.5. Ref.7

Induction

Expression in the liver oscillates in a circadian manner with peak levels at CT8-CT12. Ref.11

Post-translational modification

Proteolytically cleaved by caspase-3 By similarity.

Biophysicochemical properties

Kinetic parameters:

KM=0.49 mM for pNP-GlcNAc Ref.9

pH dependence:

Optimum pH is 6.5-7.

Sequence caution

The sequence AAH41109.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAC97998.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE26311.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

dATP metabolic process

Inferred from electronic annotation. Source: Ensembl

necrotic cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle adaptation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein glycosylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell killing

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

positive regulation of growth hormone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex disassembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hydrolase activity, acting on glycosyl bonds

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9EQQ9-1)

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: Q9EQQ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-698: Missing.
     699-725: NDLFFQPPPLTPTSKVYTIRPYFPKDE → MYTTHSCLYSFFLTFFLVCCLTRLYFQ
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9EQQ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916Bifunctional protein NCOAT
PRO_0000252119

Regions

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

Sites

Active site1751Nucleophile; for O-GlcNAcase activity Ref.9
Active site1771Proton donor; for O-GlcNAcase activity Ref.9

Amino acid modifications

Modified residue3641Phosphoserine Ref.8
Disulfide bond777 ↔ 793 Ref.6

Natural variations

Alternative sequence1 – 698698Missing in isoform 2.
VSP_020870
Alternative sequence11M → MVRPRVWRSSRRVASQNGLR AFGPTDRGRRGAVAGGRRM in isoform 3.
VSP_020871
Alternative sequence699 – 72527NDLFF…FPKDE → MYTTHSCLYSFFLTFFLVCC LTRLYFQ in isoform 2.
VSP_020872

Experimental info

Mutagenesis1661C → S: No change in substrate affinity but 60% reduction in O-GlcNAcase activity. Ref.9
Mutagenesis1741D → N: 2-fold increase in substrate affinity and 77% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. No recovery of activity in the presence of sodium azide. Ref.9
Mutagenesis1751D → A: 3-fold increase in substrate affinity and 90% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 70% recovery of activity in the presence of sodium azide. Ref.9
Mutagenesis1771D → N: 2-fold decrease in substrate affinity and 96% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 40% recovery of activity in the presence of sodium azide. Ref.9
Mutagenesis7741D → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
Mutagenesis7771C → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
Mutagenesis7891F → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
Mutagenesis7931C → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
Mutagenesis7961S → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
Mutagenesis8531D → N: Retains ability to bind histone H4. Ref.6
Mutagenesis8781C → S: No effect on O-GlcNAcase activity. Ref.9
Mutagenesis8841D → N: Retains ability to bind histone H4. Ref.6
Mutagenesis8911Y → F: Retains ability to bind histone H4. Ref.6
Sequence conflict61S → T in BAE26311. Ref.3
Sequence conflict52 – 532GA → RT in BAE26311. Ref.3
Sequence conflict7421F → S in BAC97998. Ref.2

Sequences

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

Last modified October 1, 2001. Version 2.
Checksum: B2FAC6F10E03C5CA

FASTA916103,162
        10         20         30         40         50         60 
MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV VGAAGGARRF 

        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 GTFCYPNVSQ 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 GAALSGEPSV LTKEEEKKQP DEEPMDMVVE KQEEAEHKND 

       490        500        510        520        530        540 
NQILTEIVEA KMAEELRPMD TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP 

       550        560        570        580        590        600 
GPNEKPLYTA 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 GFPFQSQPDL 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: 48F3308C6C616896
Show »

FASTA21824,718
Isoform 3 [UniParc].

Checksum: 677AA03C422AECBD
Show »

FASTA954107,395

References

« Hide 'large scale' references
[1]"Mgea5, the murine homolog of a neutral-active cytosolic beta-N-acetylglucosaminidase, localized on chromosome 19."
Csoka A.B.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryonic tail.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 3).
Strain: C57BL/6J and NOD.
Tissue: Head, Mammary gland and Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Kidney and Mammary tumor.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 109-127, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"The histone acetyltransferase NCOAT contains a zinc finger-like motif involved in substrate recognition."
Toleman C.A., Paterson A.J., Kudlow J.E.
J. Biol. Chem. 281:3918-3925(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886, FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ASP-774; CYS-777; PHE-789; CYS-793; SER-796; ASP-853; ASP-884 AND TYR-891.
[7]"Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase."
Comtesse N., Maldener E., Meese E.
Biochem. Biophys. Res. Commun. 283:634-640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-166; ASP-174; ASP-175; ASP-177 AND CYS-878.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock."
Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K., Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.
Cell Metab. 17:291-302(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLOCK, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132214 mRNA. Translation: AAG43273.2.
AK129188 mRNA. Translation: BAC97998.1. Different initiation.
BC041109 mRNA. Translation: AAH41109.1. Sequence problems.
BC054821 mRNA. Translation: AAH54821.1.
AK012695 mRNA. Translation: BAB28416.1.
AK014781 mRNA. Translation: BAB29550.1.
AK077613 mRNA. Translation: BAC36900.1.
AK088774 mRNA. Translation: BAC40564.1.
AK145227 mRNA. Translation: BAE26311.1. Different initiation.
CCDSCCDS29866.1. [Q9EQQ9-1]
RefSeqNP_076288.1. NM_023799.3. [Q9EQQ9-1]
UniGeneMm.122725.
Mm.435821.
Mm.440640.
Mm.480399.

3D structure databases

ProteinModelPortalQ9EQQ9.
SMRQ9EQQ9. Positions 46-388, 717-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid217934. 4 interactions.
IntActQ9EQQ9. 2 interactions.
MINTMINT-2844950.

Protein family/group databases

CAZyGH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSiteQ9EQQ9.

Proteomic databases

MaxQBQ9EQQ9.
PaxDbQ9EQQ9.
PRIDEQ9EQQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220. [Q9EQQ9-1]
GeneID76055.
KEGGmmu:76055.
UCSCuc008hrm.1. mouse. [Q9EQQ9-2]
uc008hrn.1. mouse. [Q9EQQ9-1]

Organism-specific databases

CTD10724.
MGIMGI:1932139. Mgea5.
RougeSearch...

Phylogenomic databases

eggNOGCOG0454.
GeneTreeENSGT00390000007726.
HOVERGENHBG053044.
InParanoidQ9EQQ9.
KOK15719.
OMALIKVDIH.
OrthoDBEOG7P02H7.
PhylomeDBQ9EQQ9.
TreeFamTF313732.

Gene expression databases

ArrayExpressQ9EQQ9.
BgeeQ9EQQ9.
CleanExMM_MGEA5.
GenevestigatorQ9EQQ9.

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

ChiTaRSMGEA5. mouse.
NextBio344519.
PROQ9EQQ9.
SOURCESearch...

Entry information

Entry nameNCOAT_MOUSE
AccessionPrimary (citable) accession number: Q9EQQ9
Secondary accession number(s): Q3ULY7 expand/collapse secondary AC list , Q6ZQ71, Q8BK05, Q8BTT2, Q8CFX2, Q9CSJ4, Q9CUR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2001
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot