LYAG_MOUSE
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 03-AUG-2022, entry version 178.
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, Spleen,
RC 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 GlyGen; P70699; 7 sites, 10 N-linked glycans (5 sites).
DR iPTMnet; P70699; -.
DR PhosphoSitePlus; P70699; -.
DR SwissPalm; P70699; -.
DR EPD; P70699; -.
DR jPOST; P70699; -.
DR MaxQB; P70699; -.
DR PaxDb; P70699; -.
DR PeptideAtlas; P70699; -.
DR PRIDE; P70699; -.
DR ProteomicsDB; 292061; -.
DR Antibodypedia; 32676; 337 antibodies from 33 providers.
DR DNASU; 14387; -.
DR Ensembl; ENSMUST00000026666; ENSMUSP00000026666; ENSMUSG00000025579.
DR Ensembl; ENSMUST00000106259; ENSMUSP00000101866; ENSMUSG00000025579.
DR GeneID; 14387; -.
DR KEGG; mmu:14387; -.
DR UCSC; uc007mqg.2; mouse.
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; YDTYTRG; -.
DR OrthoDB; 151244at2759; -.
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 72 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 309 other tissues.
DR ExpressionAtlas; P70699; baseline and differential.
DR Genevisible; P70699; MM.
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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
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; cd00111; Trefoil; 1.
DR Gene3D; 2.60.40.1180; -; 2.
DR Gene3D; 4.10.110.10; -; 1.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
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 Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR Pfam; PF00088; Trefoil; 1.
DR SMART; SM00018; PD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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.
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
