OGA_MOUSE
ID OGA_MOUSE Reviewed; 916 AA.
AC Q9EQQ9; Q3ULY7; Q6ZQ71; Q8BK05; Q8BTT2; Q8CFX2; Q9CSJ4; Q9CUR7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:16517082, ECO:0000305};
DE Short=OGA;
DE EC=3.2.1.169 {ECO:0000269|PubMed:16517082};
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase;
DE AltName: Full=Bifunctional protein NCOAT {ECO:0000303|PubMed:16356930, ECO:0000303|PubMed:16517082};
DE AltName: Full=Meningioma-expressed antigen 5 {ECO:0000303|PubMed:11341771};
DE AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
GN Name=Oga {ECO:0000250|UniProtKB:O60502}; Synonyms=Hexc, Kiaa0679, Mgea5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Csoka A.B.;
RT "Mgea5, the murine homolog of a neutral-active cytosolic beta-N-
RT acetylglucosaminidase, localized on chromosome 19.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-77 (ISOFORM 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Mammary gland, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 109-127, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886.
RX PubMed=16356930; DOI=10.1074/jbc.m510485200;
RA Toleman C.A., Paterson A.J., Kudlow J.E.;
RT "The histone acetyltransferase NCOAT contains a zinc finger-like motif
RT involved in substrate recognition.";
RL J. Biol. Chem. 281:3918-3925(2006).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=11341771; DOI=10.1006/bbrc.2001.4815;
RA Comtesse N., Maldener E., Meese E.;
RT "Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase
RT and a beta-N-acetylglucosaminidase.";
RL Biochem. Biophys. Res. Commun. 283:634-640(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-166; ASP-174;
RP ASP-175; ASP-177 AND CYS-878.
RX PubMed=16517082; DOI=10.1016/j.bbagen.2006.01.017;
RA Toleman C., Paterson A.J., Kudlow J.E.;
RT "Location and characterization of the O-GlcNAcase active site.";
RL Biochim. Biophys. Acta 1760:829-839(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH CLOCK, AND INDUCTION.
RX PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
RA Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
RA Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
RT "Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
RT regulate circadian clock.";
RL Cell Metab. 17:291-302(2013).
CC -!- FUNCTION: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins.
CC Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as
CC substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-
CC GlcNAc (in vitro) (PubMed:16517082). Does not bind acetyl-CoA and does
CC not have histone acetyltransferase activity.
CC {ECO:0000250|UniProtKB:O60502, ECO:0000269|PubMed:16517082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O =
CC L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227;
CC EC=3.2.1.169; Evidence={ECO:0000269|PubMed:16517082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O
CC = L-threonyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840,
CC ChEBI:CHEBI:506227; EC=3.2.1.169;
CC Evidence={ECO:0000269|PubMed:16517082};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mM for pNP-GlcNAc {ECO:0000269|PubMed:16517082};
CC pH dependence:
CC Optimum pH is 6.5-7. {ECO:0000269|PubMed:16517082};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with CLOCK.
CC {ECO:0000250|UniProtKB:O60502, ECO:0000269|PubMed:23395175}.
CC -!- INTERACTION:
CC Q9EQQ9; P62806: H4c1; NbExp=2; IntAct=EBI-8321615, EBI-299632;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9EQQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQQ9-2; Sequence=VSP_020870, VSP_020872;
CC Name=3;
CC IsoId=Q9EQQ9-3; Sequence=VSP_020871;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from blastocyst
CC stage to embryonic day 16.5. {ECO:0000269|PubMed:11341771}.
CC -!- INDUCTION: Expression in the liver oscillates in a circadian manner
CC with peak levels at CT8-CT12. {ECO:0000269|PubMed:23395175}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. The
CC fragments interact with each other; cleavage does not decrease enzyme
CC activity. {ECO:0000250|UniProtKB:O60502}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000305}.
CC -!- CAUTION: Was initially identified as a bi-functional protein that has
CC an N-terminal domain with O-GlcNAcase activity and a C-terminal domain
CC with histone acetyltransferase activity (PubMed:16356930). The histone
CC acetyltransferase activity was detected only when the protein was
CC expressed in mammalian cells, but not when expressed in bacterial
CC cells, suggesting that the histone acetyltransferase activity might be
CC due to the presence of a contaminant. Characterization of the human
CC protein shows that this protein does not bind acetyl-CoA and therefore
CC cannot have acetyltransferase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH41109.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC97998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE26311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF132214; AAG43273.2; -; mRNA.
DR EMBL; AK129188; BAC97998.1; ALT_INIT; mRNA.
DR EMBL; BC041109; AAH41109.1; ALT_SEQ; mRNA.
DR EMBL; BC054821; AAH54821.1; -; mRNA.
DR EMBL; AK012695; BAB28416.1; -; mRNA.
DR EMBL; AK014781; BAB29550.1; -; mRNA.
DR EMBL; AK077613; BAC36900.1; -; mRNA.
DR EMBL; AK088774; BAC40564.1; -; mRNA.
DR EMBL; AK145227; BAE26311.1; ALT_INIT; mRNA.
DR CCDS; CCDS29866.1; -. [Q9EQQ9-1]
DR RefSeq; NP_076288.1; NM_023799.3. [Q9EQQ9-1]
DR AlphaFoldDB; Q9EQQ9; -.
DR SMR; Q9EQQ9; -.
DR BioGRID; 217934; 13.
DR IntAct; Q9EQQ9; 3.
DR MINT; Q9EQQ9; -.
DR STRING; 10090.ENSMUSP00000026243; -.
DR ChEMBL; CHEMBL4523449; -.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR MoonProt; Q9EQQ9; -.
DR iPTMnet; Q9EQQ9; -.
DR PhosphoSitePlus; Q9EQQ9; -.
DR EPD; Q9EQQ9; -.
DR jPOST; Q9EQQ9; -.
DR MaxQB; Q9EQQ9; -.
DR PaxDb; Q9EQQ9; -.
DR PeptideAtlas; Q9EQQ9; -.
DR PRIDE; Q9EQQ9; -.
DR ProteomicsDB; 294070; -. [Q9EQQ9-1]
DR ProteomicsDB; 294071; -. [Q9EQQ9-2]
DR ProteomicsDB; 294072; -. [Q9EQQ9-3]
DR Antibodypedia; 31340; 191 antibodies from 28 providers.
DR Ensembl; ENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220. [Q9EQQ9-1]
DR GeneID; 76055; -.
DR KEGG; mmu:76055; -.
DR UCSC; uc008hrm.1; mouse. [Q9EQQ9-2]
DR UCSC; uc008hrn.1; mouse. [Q9EQQ9-1]
DR CTD; 10724; -.
DR MGI; MGI:1932139; Oga.
DR VEuPathDB; HostDB:ENSMUSG00000025220; -.
DR eggNOG; KOG3698; Eukaryota.
DR GeneTree; ENSGT00390000007726; -.
DR HOGENOM; CLU_009837_1_0_1; -.
DR InParanoid; Q9EQQ9; -.
DR OMA; ICTRTYL; -.
DR OrthoDB; 159999at2759; -.
DR PhylomeDB; Q9EQQ9; -.
DR TreeFam; TF313732; -.
DR BRENDA; 2.3.1.48; 3474.
DR BRENDA; 3.2.1.169; 3474.
DR BioGRID-ORCS; 76055; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Mgea5; mouse.
DR PRO; PR:Q9EQQ9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9EQQ9; protein.
DR Bgee; ENSMUSG00000025220; Expressed in saccule of membranous labyrinth and 257 other tissues.
DR ExpressionAtlas; Q9EQQ9; baseline and differential.
DR Genevisible; Q9EQQ9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR 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.
DR GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0046060; P:dATP metabolic process; ISO:MGI.
DR GO; GO:0009100; P:glycoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
DR GO; GO:0070265; P:necrotic cell death; ISO:MGI.
DR GO; GO:0010616; P:negative regulation of cardiac muscle adaptation; ISO:MGI.
DR GO; GO:0060051; P:negative regulation of protein glycosylation; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0031343; P:positive regulation of cell killing; ISO:MGI.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0006517; P:protein deglycosylation; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Glycosidase;
KW Hydrolase; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..916
FT /note="Protein O-GlcNAcase"
FT /id="PRO_0000252119"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O60502"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16517082"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 278..280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT SITE 413..414
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:O60502"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..698
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020870"
FT VAR_SEQ 1
FT /note="M -> MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020871"
FT VAR_SEQ 699..725
FT /note="NDLFFQPPPLTPTSKVYTIRPYFPKDE -> MYTTHSCLYSFFLTFFLVCCL
FT TRLYFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020872"
FT MUTAGEN 166
FT /note="C->S: No change in substrate affinity but 60%
FT reduction in O-GlcNAcase activity."
FT /evidence="ECO:0000269|PubMed:16517082"
FT MUTAGEN 174
FT /note="D->N: 2-fold increase in substrate affinity and 77%
FT reduction in O-GlcNAcase activity. Regains appreciable
FT level of catalytic efficiency in the acidic pH range. No
FT recovery of activity in the presence of sodium azide."
FT /evidence="ECO:0000269|PubMed:16517082"
FT MUTAGEN 175
FT /note="D->A: 3-fold increase in substrate affinity and 90%
FT reduction in O-GlcNAcase activity. Regains appreciable
FT level of catalytic efficiency in the acidic pH range. 70%
FT recovery of activity in the presence of sodium azide."
FT /evidence="ECO:0000269|PubMed:16517082"
FT MUTAGEN 177
FT /note="D->N: 2-fold decrease in substrate affinity and 96%
FT reduction in O-GlcNAcase activity. Regains appreciable
FT level of catalytic efficiency in the acidic pH range. 40%
FT recovery of activity in the presence of sodium azide."
FT /evidence="ECO:0000269|PubMed:16517082"
FT MUTAGEN 878
FT /note="C->S: No effect on O-GlcNAcase activity."
FT /evidence="ECO:0000269|PubMed:16517082"
FT CONFLICT 6
FT /note="S -> T (in Ref. 3; BAE26311)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="GA -> RT (in Ref. 3; BAE26311)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="F -> S (in Ref. 2; BAC97998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 103162 MW; B2FAC6F10E03C5CA CRC64;
MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV VGAAGGARRF
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKTS VVDGTPLVAA
PSLNATTVVT TVYQEPIMSQ GAALSGEPSV LTKEEEKKQP DEEPMDMVVE KQEEAEHKND
NQILTEIVEA KMAEELRPMD TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP
GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY
FPKDEASVYK ICREMYDDGV GFPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
KMEGFPKDVV ILGRSL
