LYAG_PONAB
ID LYAG_PONAB Reviewed; 952 AA.
AC Q5R7A9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860209; CAH92351.1; -; mRNA.
DR RefSeq; NP_001126384.1; NM_001132912.2.
DR AlphaFoldDB; Q5R7A9; -.
DR SMR; Q5R7A9; -.
DR STRING; 9601.ENSPPYP00000009778; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GeneID; 100173365; -.
DR KEGG; pon:100173365; -.
DR CTD; 2548; -.
DR eggNOG; KOG1065; Eukaryota.
DR InParanoid; Q5R7A9; -.
DR OrthoDB; 151244at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:UniProtKB.
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; SSF57492; SSF57492; 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_0000260440"
FT CHAIN 70..952
FT /note="Lysosomal alpha-glucosidase"
FT /id="PRO_0000260441"
FT DOMAIN 80..131
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 47..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
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 952 AA; 105531 MW; 4AEC592583525C16 CRC64;
MRVRHPPCSR RLLAICALVS LATAALLGHI LLHDFLLVPR ELSGSSPVLE ETHPAHQQGA
SRPGPRDAQA HLGRPRAVPT QCDVPPNSRF DCAPDKAITR EQCDARGCCY IPAKQGLRGA
QMGQPWCFFP PSYPSYKLEN LSSSEMGYTA TLTRTTPTFF PKDILTLRLD VMMETENRLH
FTIKDPANRR YEVPLETPRV HSRAPSPLYS VEFSEEPFGV IVRRQLDGRV LLNTTVAPLF
FADQFLQLST SLPSQYITGL AEHLSPLMLS TSWTRVTLWN RDLAPTPGAN LYGSHPFYLA
LEDGGSAHGV FLLNSNAMDV VLQPSPALSW RSTGGILDVY IFLGPEPKSV VRQYLDVVGY
PFMPPYWGLG FHLCRWGYSS TAITSQVVEN MTRAHFPLDV QWNDLDYMDA RRDFTFNKDG
FRDFPAMVRE LHQGGRRYMM IVDPAISSSG PAGSYRPYDE GLRRGVFITN ETSQPLIGKV
WPGSTAFPDF TNPAALAWWE DMVAEFHDQV PFDGMWIDMN EPSNFIRGSE DGCPDNELEN
PPYVPGVVGG TLQAATICAS SHQFLSTHYN LHNLYGLTEA IASHRALVKA RGTRPFVISR
STFAGHGRYA GHWTGDVWSS WEQLASSVPE ILQFNLLGVP LVGADVCGFL GNTSEELCVR
WTQLGAFYPF MRNHNGLLNL PQEPYSFSEP AQQAMRKALT LRYALLPHLY TLFHQAHVAG
ETVARPLFLE FPKDSSTWTV DHQLLWGEAL LITPVLQAGK AEVTGYFPLG IWYDLQTVPI
EALGSLPPPP AAPREPAIHS EGQWVTLPAP LDTINVHLRA GYIIPLQGPG LTTTESRQQP
MALAVALTKG GEARGELFWD DGESLEVLER GAYTQVLFLA RNNTIVNELV HVTSEGAGLQ
LQKVTVLGVA TTPQQVLSNG VPVSNFTYSP DTKVLDIPVS LLMAEQFLIS WS
