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Q8VIJ5

- NCOAT_RAT

UniProt

Q8VIJ5 - NCOAT_RAT

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Protein

Bifunctional protein NCOAT

Gene

Mgea5

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

Functioni

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.By similarity2 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Acetyl-CoA + [histone] = CoA + acetyl-[histone].

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
Active sitei175 – 1751Nucleophile; for O-GlcNAcase activityBy similarity
Active sitei177 – 1771Proton donor; for O-GlcNAcase activityBy similarity

GO - Molecular functioni

  1. beta-N-acetylglucosaminidase activity Source: RGD
  2. histone acetyltransferase activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. dATP metabolic process Source: RGD
  3. histone acetylation Source: GOC
  4. N-acetylglucosamine metabolic process Source: RGD
  5. necrotic cell death Source: RGD
  6. negative regulation of cardiac muscle adaptation Source: RGD
  7. negative regulation of protein glycosylation Source: RGD
  8. positive regulation of calcium ion transport Source: RGD
  9. positive regulation of calcium ion transport into cytosol Source: RGD
  10. positive regulation of cell killing Source: RGD
  11. positive regulation of DNA metabolic process Source: RGD
  12. positive regulation of glucose import Source: RGD
  13. positive regulation of growth hormone secretion Source: RGD
  14. positive regulation of insulin secretion Source: RGD
  15. positive regulation of mitochondrial depolarization Source: RGD
  16. positive regulation of protein complex disassembly Source: RGD
  17. positive regulation of proteolysis Source: RGD
  18. protein targeting to membrane Source: RGD
  19. response to steroid hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Glycosidase, Hydrolase, Transferase

Protein family/group databases

CAZyiGH84. Glycoside Hydrolase Family 84.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein NCOAT
Alternative name(s):
Meningioma-expressed antigen 5
Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
Including the following 2 domains:
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
Histone acetyltransferase (EC:2.3.1.48)
Short name:
HAT
Gene namesi
Name:Mgea5
Synonyms:Hexc, Mea5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi621077. Mgea5.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: RGD
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi853 – 8531D → N: Loss of histone acetyltransferase activity. 1 Publication
Mutagenesisi884 – 8841D → N: Loss of histone acetyltransferase activity. 1 Publication
Mutagenesisi891 – 8911Y → F: Loss of histone acetyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916Bifunctional protein NCOATPRO_0000252120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei364 – 3641PhosphoserineBy similarity
Disulfide bondi777 ↔ 793By similarity

Post-translational modificationi

Proteolytically cleaved by caspase-3.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ8VIJ5.
PRIDEiQ8VIJ5.

PTM databases

PhosphoSiteiQ8VIJ5.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at highest levels in the brain and spleen.1 Publication

Gene expression databases

ExpressionAtlasiQ8VIJ5. baseline and differential.
GenevestigatoriQ8VIJ5.

Interactioni

Subunit structurei

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 PubMed:8034696 it is a heterodimer of an alpha and beta chain.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024198.

Structurei

3D structure databases

ProteinModelPortaliQ8VIJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni583 – 916334Histone acetyltransferase activityAdd
BLAST
Regioni695 – 814120Required for histone H4 bindingBy similarityAdd
BLAST

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00390000007726.
HOGENOMiHOG000044964.
HOVERGENiHBG053044.
InParanoidiQ8VIJ5.
KOiK15719.
OMAiLIKVDIH.
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. Align

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:
EMBL
GenBank
DDBJ
Links Updated
AY039679 mRNA. Translation: AAK72103.1.
RefSeqiNP_571979.1. NM_131904.1. [Q8VIJ5-1]
UniGeneiRn.162539.

Genome annotation databases

EnsembliENSRNOT00000065172; ENSRNOP00000059568; ENSRNOG00000017822. [Q8VIJ5-1]
GeneIDi154968.
KEGGirno:154968.
UCSCiRGD:621077. rat. [Q8VIJ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY039679 mRNA. Translation: AAK72103.1 .
RefSeqi NP_571979.1. NM_131904.1. [Q8VIJ5-1 ]
UniGenei Rn.162539.

3D structure databases

ProteinModelPortali Q8VIJ5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000024198.

Protein family/group databases

CAZyi GH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSitei Q8VIJ5.

Proteomic databases

PaxDbi Q8VIJ5.
PRIDEi Q8VIJ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000065172 ; ENSRNOP00000059568 ; ENSRNOG00000017822 . [Q8VIJ5-1 ]
GeneIDi 154968.
KEGGi rno:154968.
UCSCi RGD:621077. rat. [Q8VIJ5-1 ]

Organism-specific databases

CTDi 10724.
RGDi 621077. Mgea5.

Phylogenomic databases

eggNOGi COG0454.
GeneTreei ENSGT00390000007726.
HOGENOMi HOG000044964.
HOVERGENi HBG053044.
InParanoidi Q8VIJ5.
KOi K15719.
OMAi LIKVDIH.
OrthoDBi EOG7P02H7.
PhylomeDBi Q8VIJ5.

Miscellaneous databases

NextBioi 620868.
PROi Q8VIJ5.

Gene expression databases

ExpressionAtlasi Q8VIJ5. baseline and differential.
Genevestigatori Q8VIJ5.

Family and domain databases

Gene3Di 3.40.630.30. 2 hits.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF07555. NAGidase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

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. "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.

Entry informationi

Entry nameiNCOAT_RAT
AccessioniPrimary (citable) accession number: Q8VIJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

External Data

Dasty 3