LYAG_RAT
ID LYAG_RAT Reviewed; 953 AA.
AC Q6P7A9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC061753; AAH61753.1; -; mRNA.
DR RefSeq; NP_954549.1; NM_199118.1.
DR AlphaFoldDB; Q6P7A9; -.
DR SMR; Q6P7A9; -.
DR BioGRID; 266559; 1.
DR IntAct; Q6P7A9; 1.
DR STRING; 10116.ENSRNOP00000064500; -.
DR BindingDB; Q6P7A9; -.
DR ChEMBL; CHEMBL3513; -.
DR DrugCentral; Q6P7A9; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyGen; Q6P7A9; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q6P7A9; -.
DR PhosphoSitePlus; Q6P7A9; -.
DR jPOST; Q6P7A9; -.
DR PaxDb; Q6P7A9; -.
DR PRIDE; Q6P7A9; -.
DR GeneID; 367562; -.
DR KEGG; rno:367562; -.
DR CTD; 2548; -.
DR RGD; 735227; Gaa.
DR eggNOG; KOG1065; Eukaryota.
DR InParanoid; Q6P7A9; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; Q6P7A9; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR SABIO-RK; Q6P7A9; -.
DR PRO; PR:Q6P7A9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:RGD.
DR GO; GO:0090599; F:alpha-glucosidase activity; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
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:RGD.
DR GO; GO:0002086; P:diaphragm contraction; ISO:RGD.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0050884; P:neuromuscular process controlling posture; ISO:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0009888; P:tissue development; ISO:RGD.
DR GO; GO:0043181; P:vacuolar sequestering; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..69
FT /evidence="ECO:0000250"
FT /id="PRO_0000260442"
FT CHAIN 70..953
FT /note="Lysosomal alpha-glucosidase"
FT /id="PRO_0000260443"
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:0000255"
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:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 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"
SQ SEQUENCE 953 AA; 106207 MW; D99723779AD41E05 CRC64;
MNIRKPLCSN SVVGACTLVS LTTAVILGHL MLRELMLLPQ DLHESSSGLW KTYRPHHQES
YEPAPLHIQE HAEQLRAVPT QCDVTPNSRF DCAPDKGITQ EQCEARGCCW VPAGQVLNGP
VMGQPWCFFP PSYPSYRLEN LSSTESGYTA TLTRTSPTFF PKDVLTLQLE VLMETDSRLH
FMIKDPTSKR YEVPLETPRV LSQAPSPLYS VEFSEEPFGV IVRRKLGGRV LLNTTVAPLF
FADQFLQLST SLPSQHIAGL GEHLSPLMLS TEWTRITLWN RDVAPSQGVN LYGSHPFYLA
LEDGGLAHGV FLLNSNAMDV VLQPSPALTW RSTGGILDVY VFLGPEPKSV VQQYLDVVGY
PFMPPYWGLG FHLCRWGYSS TAIVRQVVEN MTRTHFPLDV QWNDLDYMDA RRDFTFNQDG
FADFPDMVHE LHQGGRRYMM IVDPAISSSG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV
WPGSTAFPDF TNPETLDWWQ DMVSEFHAQV PFDGMWIDMN EPSNFIRGSQ QGCPDNELEN
PPYVPGVVGG ALQAATICAS SHQFLSTHYN LHNLYGLTEA IASSRALVKT RGTRPFVISR
STFAGHGRYA GHWTGDVWSS WEHLAYSVPE ILQFNLLGVP LVGADICGFQ GNTTEELCVR
WTQLGAFYPF MRNHNDLNSL PQEPYRFSET AQQAMRKAFT LRYALLPYLY TLFHGAHVKG
DTVARPLFLE FPEDPSTWSV DRQLLWGPAL LITPVLEPGK TDVTGYFPKG MWYNLQMVPV
ETLGSLPSSS PASSFRSIVH SKGQWLTLEA PLDTINVHLR AGYIIPLQGP SLTTTESRKQ
PMALAVALTE SGEASGELFW DDGESLGVLE RGAYTLVTFS AKNNTIVNKL VHVTKEGGEL
QLREVTILGV TTAPTQVLSN GISVSNFTYS PDDKSLSIPV SLLMGERFQI DWS
