Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (EC 3.2.1.52) (N-acetyl-beta-glucosaminidase)

 OGA_RAT                 Reviewed;         916 AA.
Q8VIJ5;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
27-SEP-2017, entry version 103.
RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:8034696, ECO:0000303|Ref.1};
Short=OGA;
EC=3.2.1.169 {ECO:0000269|PubMed:8034696};
AltName: Full=Beta-N-acetylhexosaminidase;
AltName: Full=Beta-hexosaminidase;
AltName: Full=Bifunctional protein NCOAT {ECO:0000303|PubMed:15485860};
AltName: Full=Meningioma-expressed antigen 5;
AltName: Full=N-acetyl-beta-D-glucosaminidase;
EC=3.2.1.52 {ECO:0000269|PubMed:8034696};
AltName: Full=N-acetyl-beta-glucosaminidase;
Name=Mgea5; Synonyms=Hexc, Mea5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Fischer 344;
Liu K., Paterson A.J., Van Tine B.A., Konrad R.J., Parlow A.F.,
Jimi S., Chin E. Jr., Kudlow J.E.;
"The O-GlcNAcase gene is a candidate for diabetes susceptibility in GK
rats.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Spleen;
PubMed=8034696;
Dong D.-L., Hart G.W.;
"Purification and characterization of an O-GlcNAc selective N-acetyl-
beta-D-glucosaminidase from rat spleen cytosol.";
J. Biol. Chem. 269:19321-19330(1994).
[3]
IDENTIFICATION OF ISOFORMS 2 AND 3.
STRAIN=GK, and Sprague-Dawley;
PubMed=15485860; DOI=10.1074/jbc.M410406200;
Toleman C., Paterson A.J., Whisenhunt T.R., Kudlow J.E.;
"Characterization of the histone acetyltransferase (HAT) domain of a
bifunctional protein with activable O-GlcNAcase and HAT activities.";
J. Biol. Chem. 279:53665-53673(2004).
[4]
FUNCTION OF ISOFORMS 2 AND 3, AND LACK OF CATALYTIC ACTIVITY OF
ISOFORMS 2 AND 3.
PubMed=16517082; DOI=10.1016/j.bbagen.2006.01.017;
Toleman C., Paterson A.J., Kudlow J.E.;
"Location and characterization of the O-GlcNAcase active site.";
Biochim. Biophys. Acta 1760:829-839(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:O60502,
ECO:0000269|PubMed:8034696}.
-!- FUNCTION: Isoform 2: Lacks enzyme activity.
{ECO:0000269|PubMed:16517082}.
-!- FUNCTION: Isoform 3: Lacks enzyme activity.
{ECO:0000269|PubMed:16517082}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine.
{ECO:0000269|PubMed:8034696}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-
glucosamine. {ECO:0000269|PubMed:8034696}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000269|PubMed:8034696}.
-!- ENZYME REGULATION: Inhibited by Cu(2+), Hg(2+), Cd(2+) and Zn(2+)
at 1 mM. Not inhibited by Co(2+), Mg(2+), Ca(2+), Mn(2+), Fe(3+)
and EDTA. Also inhibited by sodium chloride at 1M and 2-amino-2-
hydroxymethyl-1,3-propanediol (trishydroxymethylaminomethane) at
75 mM. {ECO:0000269|PubMed:8034696}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.55 mM for pNP-O-GlcNAc {ECO:0000269|PubMed:8034696};
pH dependence:
Optimum pH is 6.4. Activity decreases sharply at pH below 5.0.
{ECO:0000269|PubMed:8034696};
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.
{ECO:0000269|PubMed:8034696};
-!- SUBUNIT: Monomer. Interacts with CLOCK (By similarity).
{ECO:0000250|UniProtKB:O60502, ECO:0000250|UniProtKB:Q9EQQ9}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8034696}.
Cytoplasm {ECO:0000269|PubMed:8034696}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8VIJ5-1; Sequence=Displayed;
Name=2;
IsoId=Q8VIJ5-2; Sequence=VSP_020873;
Note=Lack hexosaminidase activity.;
Name=3;
IsoId=Q8VIJ5-3; Sequence=VSP_020874;
Note=Lack hexosaminidase activity.;
-!- TISSUE SPECIFICITY: Detected in spleen (at protein level).
Ubiquitous. Expressed at highest levels in the brain and spleen.
{ECO:0000269|PubMed:8034696}.
-!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. The
fragments interact with each other; cleavage does not decrease
enzyme activity. {ECO:0000250|UniProtKB:O60502}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family.
{ECO:0000305}.
-!- 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.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY039679; AAK72103.1; -; mRNA.
RefSeq; NP_571979.1; NM_131904.1. [Q8VIJ5-1]
UniGene; Rn.162539; -.
ProteinModelPortal; Q8VIJ5; -.
STRING; 10116.ENSRNOP00000059568; -.
BindingDB; Q8VIJ5; -.
ChEMBL; CHEMBL3351213; -.
CAZy; GH84; Glycoside Hydrolase Family 84.
iPTMnet; Q8VIJ5; -.
PhosphoSitePlus; Q8VIJ5; -.
PaxDb; Q8VIJ5; -.
PRIDE; Q8VIJ5; -.
GeneID; 154968; -.
KEGG; rno:154968; -.
UCSC; RGD:621077; rat. [Q8VIJ5-1]
CTD; 10724; -.
RGD; 621077; Mgea5.
eggNOG; KOG3698; Eukaryota.
eggNOG; ENOG410XPBQ; LUCA.
HOGENOM; HOG000044964; -.
HOVERGEN; HBG053044; -.
InParanoid; Q8VIJ5; -.
KO; K15719; -.
OrthoDB; EOG091G02T9; -.
PhylomeDB; Q8VIJ5; -.
PRO; PR:Q8VIJ5; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q8VIJ5; RN.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
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.
GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:RGD.
GO; GO:0004402; F:histone acetyltransferase activity; IMP:RGD.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0046060; P:dATP metabolic process; IMP:RGD.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IMP:RGD.
GO; GO:0070265; P:necrotic cell death; IMP:RGD.
GO; GO:0010616; P:negative regulation of cardiac muscle adaptation; IMP:RGD.
GO; GO:0060051; P:negative regulation of protein glycosylation; IMP:RGD.
GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IMP:RGD.
GO; GO:0031343; P:positive regulation of cell killing; IMP:RGD.
GO; GO:0051054; P:positive regulation of DNA metabolic process; IMP:RGD.
GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:RGD.
GO; GO:0043243; P:positive regulation of protein complex disassembly; IMP:RGD.
GO; GO:0045862; P:positive regulation of proteolysis; IMP:RGD.
GO; GO:0006612; P:protein targeting to membrane; IMP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR011496; Beta-N-acetylglucosaminidase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF07555; NAGidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55729; SSF55729; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Glycosidase;
Hydrolase; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 916 Protein O-GlcNAcase.
/FTId=PRO_0000252120.
REGION 278 280 Substrate binding.
{ECO:0000250|UniProtKB:Q2CEE3}.
ACT_SITE 175 175 Proton donor.
{ECO:0000250|UniProtKB:O60502}.
BINDING 67 67 Substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 98 98 Substrate.
{ECO:0000250|UniProtKB:Q0TR53}.
BINDING 174 174 Substrate.
{ECO:0000250|UniProtKB:Q0TR53}.
BINDING 219 219 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 313 313 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
SITE 413 414 Cleavage; by caspase-3.
{ECO:0000250|UniProtKB:O60502}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 250 398 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_020873.
VAR_SEQ 250 345 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_020874.
SEQUENCE 916 AA; 102918 MW; 4BA1746F0AF2E380 CRC64;
MVQKESQAAL EERESERNAN PASVSGASLE PSAAPAPGED NPSGAGAAAG TGAAGGARRF
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPSVSQ SPYLRTVGEK
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKTS VVDGTPLVAA
PSLNATTVVT TVYQEPIMSQ GAALSGEPSA LTKEEEKKQP DEEPMDMVVE KQEESEHKSD
NQILTEIVEA KMAEELKPMD TDKESIAESK SPEMSMQEDC INDIAPMQTD EQANKEQFVP
GPNEKPLYAA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
SEKIEEWRSR AAKFEEMCAL 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


Related products :

Catalog number Product name Quantity
E0195h ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195h CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195h ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195r ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
E0195m ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195b ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195b ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195m CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195b CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195m ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195r CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
E0195r ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
EIAAB26576 Bifunctional protein NCOAT,Hexc,Kiaa0679,Meningioma-expressed antigen 5,Mgea5,Mouse,Mus musculus,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
EIAAB26575 Bifunctional protein NCOAT,Hexc,Mea5,Meningioma-expressed antigen 5,Mgea5,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase,Rat,Rattus norvegicus
EIAAB26577 Bifunctional protein NCOAT,HEXC,Homo sapiens,Human,KIAA0679,MEA5,Meningioma-expressed antigen 5,MGEA5,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
EM1225 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
EH3404 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
ER1177 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
E12411417 Rat N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 1
E13812064 N-Acetyl beta-D-Glucosaminidase (NAG) ELISA Kit 1
E12531317 Mouse N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 1
22842 Human N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 96T
E-EL-R0647 Rat NAGase (N-Acetyl Beta-D-Glucosaminidase) ELISA Kit 96T
E15861270 Porcine N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit
E90069Ra ELISA Kit for N-Acetyl Beta D Glucosaminidase (NAGase) 96T/Kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur