ID   LYAG_MOUSE              Reviewed;         953 AA.
AC   P70699; Q3UJB2; Q8BGI6; Q91Z45;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Lysosomal alpha-glucosidase;
DE            EC=3.2.1.20 {ECO:0000250|UniProtKB:P10253};
DE   AltName: Full=Acid maltase;
DE   Flags: Precursor;
GN   Name=Gaa;
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].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RA   Ding J.H., Yang B.Z., Reuser A.J.J., Roe C.R.;
RT   "Cloning and characterization of the mouse liver cDNA encoding lysosomal
RT   alpha-glucosidase.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Brain cortex, Heart, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=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   [4]
RP   PROTEIN SEQUENCE OF 376-385, 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   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-470.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   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).
CC   -!- FUNCTION: Essential for the degradation of glycogen in lysosomes. Has
CC       highest activity on alpha-1,4-linked glycosidic linkages, but can also
CC       hydrolyze alpha-1,6-linked glucans. {ECO:0000250|UniProtKB:P10253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC         Evidence={ECO:0000250|UniProtKB:P10253};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P10253}. Lysosome
CC       membrane {ECO:0000250|UniProtKB:P10253}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; U49351; AAB06943.1; -; mRNA.
DR   EMBL; AK052211; BAC34888.1; -; mRNA.
DR   EMBL; AK088481; BAC40382.1; -; mRNA.
DR   EMBL; AK139333; BAE23960.1; -; mRNA.
DR   EMBL; AK146538; BAE27243.1; -; mRNA.
DR   EMBL; AK150970; BAE30001.1; -; mRNA.
DR   EMBL; BC010210; AAH10210.1; -; mRNA.
DR   CCDS; CCDS25713.1; -.
DR   RefSeq; NP_001152796.1; NM_001159324.2.
DR   RefSeq; NP_032090.3; NM_008064.4.
DR   AlphaFoldDB; P70699; -.
DR   SMR; P70699; -.
DR   BioGRID; 199792; 21.
DR   STRING; 10090.ENSMUSP00000101866; -.
DR   BindingDB; P70699; -.
DR   ChEMBL; CHEMBL1667668; -.
DR   DrugCentral; P70699; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GlyConnect; 2490; 10 N-Linked glycans (5 sites).
DR   GlyCosmos; P70699; 7 sites, 10 glycans.
DR   GlyGen; P70699; 8 sites, 10 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P70699; -.
DR   PhosphoSitePlus; P70699; -.
DR   SwissPalm; P70699; -.
DR   EPD; P70699; -.
DR   jPOST; P70699; -.
DR   MaxQB; P70699; -.
DR   PaxDb; 10090-ENSMUSP00000101866; -.
DR   PeptideAtlas; P70699; -.
DR   ProteomicsDB; 292061; -.
DR   Pumba; P70699; -.
DR   Antibodypedia; 32676; 380 antibodies from 33 providers.
DR   DNASU; 14387; -.
DR   Ensembl; ENSMUST00000026666.13; ENSMUSP00000026666.7; ENSMUSG00000025579.15.
DR   Ensembl; ENSMUST00000106259.9; ENSMUSP00000101866.3; ENSMUSG00000025579.15.
DR   GeneID; 14387; -.
DR   KEGG; mmu:14387; -.
DR   UCSC; uc007mqg.2; mouse.
DR   AGR; MGI:95609; -.
DR   CTD; 2548; -.
DR   MGI; MGI:95609; Gaa.
DR   VEuPathDB; HostDB:ENSMUSG00000025579; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   GeneTree; ENSGT00940000159355; -.
DR   HOGENOM; CLU_000631_11_2_1; -.
DR   InParanoid; P70699; -.
DR   OMA; PYVINHD; -.
DR   OrthoDB; 5480935at2759; -.
DR   PhylomeDB; P70699; -.
DR   TreeFam; TF314577; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR   BioGRID-ORCS; 14387; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Gaa; mouse.
DR   PRO; PR:P70699; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P70699; Protein.
DR   Bgee; ENSMUSG00000025579; Expressed in arcuate nucleus of hypothalamus and 313 other cell types or tissues.
DR   ExpressionAtlas; P70699; baseline and differential.
DR   GO; GO:0120282; C:autolysosome lumen; IMP:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IMP:MGI.
DR   GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:MGI.
DR   GO; GO:0090599; F:alpha-glucosidase activity; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR   GO; GO:0043896; F:glucan 1,6-alpha-glucosidase activity; ISO:MGI.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035904; P:aorta development; IMP:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0002086; P:diaphragm contraction; IMP:MGI.
DR   GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
DR   GO; GO:0061723; P:glycophagy; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
DR   GO; GO:0009888; P:tissue development; IMP:MGI.
DR   GO; GO:0043181; P:vacuolar sequestering; ISO:MGI.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd00111; Trefoil; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR017957; P_trefoil_CS.
DR   InterPro; IPR000519; P_trefoil_dom.
DR   InterPro; IPR044913; P_trefoil_dom_sf.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF92; LYSOSOMAL ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF00088; Trefoil; 1.
DR   SMART; SM00018; PD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR   PROSITE; PS00025; P_TREFOIL_1; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 1.
DR   Genevisible; P70699; MM.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..69
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000018569"
FT   CHAIN           70..953
FT                   /note="Lysosomal alpha-glucosidase"
FT                   /id="PRO_0000018570"
FT   DOMAIN          80..131
FT                   /note="P-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   ACT_SITE        518
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   BINDING         600
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   BINDING         616
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   BINDING         674
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        883
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        926
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        933
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        92..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        103..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT   DISULFID        533..558
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   DISULFID        647..658
FT                   /evidence="ECO:0000250|UniProtKB:P10253"
FT   CONFLICT        62
FT                   /note="K -> E (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="S -> A (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430..431
FT                   /note="EL -> DV (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        434
FT                   /note="D -> G (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="W -> C (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="G -> E (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="S -> T (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        732
FT                   /note="P -> R (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        777
FT                   /note="M -> V (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        871
FT                   /note="R -> H (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        903
FT                   /note="R -> K (in Ref. 1; AAB06943)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   953 AA;  106248 MW;  956B89685FB5FF81 CRC64;
     MNIRKPLCSN SVVGACTLIS LTTAVILGHL MLRELMLLPQ DLHESSSGLW KTYRPHHQEG
     YKPGPLHIQE QTEQPKEAPT QCDVPPSSRF DCAPDKGISQ EQCEARGCCY VPAGQVLKEP
     QIGQPWCFFP PSYPSYRLEN LSSTESGYTA TLTRTSPTFF PKDVLTLQLE VLMETDSRLH
     FKIKDPASKR YEVPLETPRV LSQAPSPLYS VEFSEEPFGV IVRRKLGGRV LLNTTVAPLF
     FADQFLQLST SLPSQHITGL GEHLSPLMLS TDWARITLWN RDTPPSQGTN LYGSHPFYLA
     LEDGGLAHGV FLLNSNAMDV ILQPSPALTW RSTGGILDVY VFLGPEPKSV VQQYLDVVGY
     PFMPPYWGLG FHLCRWGYSS TAIVRQVVEN MTRTHFPLDV QWNDLDYMDA RRDFTFNQDS
     FADFPDMVRE LHQDGRRYMM IVDPAISSAG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV
     WPGTTAFPDF TNPETLDWWQ DMVSEFHAQV PFDGMWLDMN EPSNFVRGSQ QGCPNNELEN
     PPYVPGVVGG ILQAATICAS SHQFLSTHYN LHNLYGLTEA IASSRALVKT RGTRPFVISR
     STFSGHGRYA GHWTGDVRSS WEHLAYSVPD ILQFNLLGVP LVGADICGFI GDTSEELCVR
     WTQLGAFYPF MRNHNDLNSV PQEPYRFSET AQQAMRKAFA LRYALLPYLY TLFHRAHVRG
     DTVARPLFLE FPEDPSTWSV DRQLLWGPAL LITPVLEPGK TEVTGYFPKG TWYNMQMVSV
     DSLGTLPSPS SASSFRSAVQ SKGQWLTLEA PLDTINVHLR EGYIIPLQGP SLTTTESRKQ
     PMALAVALTA SGEADGELFW DDGESLAVLE RGAYTLVTFS AKNNTIVNKL VRVTKEGAEL
     QLREVTVLGV ATAPTQVLSN GIPVSNFTYS PDNKSLAIPV SLLMGELFQI SWS
//