ID   BGAL_MOUSE              Reviewed;         647 AA.
AC   P23780;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   02-SEP-2026, entry version 192.
DE   RecName: Full=Beta-galactosidase {ECO:0000305|PubMed:2124109};
DE            EC=3.2.1.23 {ECO:0000269|PubMed:2124109};
DE   AltName: Full=Acid beta-galactosidase;
DE            Short=Lactase;
DE   Flags: Precursor;
GN   Name=Glb1 {ECO:0000312|MGI:MGI:88151}; Synonyms=Bgl, Glb-1;
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 [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=2124109; DOI=10.1016/s0006-291x(05)81033-2;
RA   Nanba E., Suzuki K.;
RT   "Molecular cloning of mouse acid beta-galactosidase cDNA: sequence,
RT   expression of catalytic activity and comparison with the human enzyme.";
RL   Biochem. Biophys. Res. Commun. 173:141-148(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J;
RX   PubMed=1906271; DOI=10.1016/0006-291x(91)91793-c;
RA   Nanba E., Suzuki K.;
RT   "Organization of the mouse acid beta-galactosidase gene.";
RL   Biochem. Biophys. Res. Commun. 178:158-164(1991).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   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: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000269|PubMed:2124109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000269|PubMed:2124109};
CC   -!- SUBUNIT: Homodimer. May form higher multimers.
CC       {ECO:0000250|UniProtKB:P16278}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P16278}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; M57734; AAA37293.1; -; mRNA.
DR   EMBL; M75122; AAA37292.1; -; Genomic_DNA.
DR   EMBL; M75137; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75107; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75108; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75109; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75111; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75112; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75113; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75114; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75115; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75116; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75117; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75118; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75119; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75120; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75121; AAA37292.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS23593.1; -.
DR   PIR; A37086; A37086.
DR   RefSeq; NP_033882.1; NM_009752.2.
DR   PDB; 7KDV; EM; 4.59 A; A/C/E/G/I/K=28-647.
DR   AlphaFoldDB; P23780; -.
DR   EMDB; EMD-22830; -.
DR   SMR; P23780; -.
DR   BioGRID; 198341; 13.
DR   FunCoup; P23780; 1767.
DR   STRING; 10090.ENSMUSP00000055803; -.
DR   BindingDB; P23780; -.
DR   ChEMBL; CHEMBL1667667; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; P23780; 8 sites, No reported glycans.
DR   GlyGen; P23780; 9 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P23780; -.
DR   PhosphoSitePlus; P23780; -.
DR   SwissPalm; P23780; -.
DR   jPOST; P23780; -.
DR   PaxDb; 10090-ENSMUSP00000055803; -.
DR   PeptideAtlas; P23780; -.
DR   ProteomicsDB; 273486; -.
DR   Pumba; P23780; -.
DR   Antibodypedia; 3647; 720 antibodies from 41 providers.
DR   DNASU; 12091; -.
DR   Ensembl; ENSMUST00000063042.11; ENSMUSP00000055803.10; ENSMUSG00000045594.11.
DR   GeneID; 12091; -.
DR   KEGG; mmu:12091; -.
DR   UCSC; uc009rxj.3; mouse.
DR   AGR; MGI:88151; -.
DR   CTD; 2720; -.
DR   MGI; MGI:88151; Glb1.
DR   VEuPathDB; HostDB:ENSMUSG00000045594; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   GeneTree; ENSGT00950000182942; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   InParanoid; P23780; -.
DR   OMA; FWNIHEQ; -.
DR   OrthoDB; 1657402at2759; -.
DR   PhylomeDB; P23780; -.
DR   Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   Reactome; R-MMU-4085001; Sialic acid metabolism.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9840310; Glycosphingolipid catabolism.
DR   SABIO-RK; P23780; -.
DR   BioGRID-ORCS; 12091; 3 hits in 82 CRISPR screens.
DR   PRO; PR:P23780; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P23780; protein.
DR   Bgee; ENSMUSG00000045594; Expressed in right kidney and 254 other cell types or tissues.
DR   ExpressionAtlas; P23780; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:MGI.
DR   GO; GO:0016936; F:galactoside binding; ISO:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:GO_Central.
DR   GO; GO:0019388; P:galactose catabolic process; ISO:GO_Central.
DR   GO; GO:0006689; P:ganglioside catabolic process; IMP:FlyBase.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IMP:FlyBase.
DR   GO; GO:0042340; P:keratan sulfate proteoglycan catabolic process; IMP:FlyBase.
DR   GO; GO:0051413; P:response to cortisone; IEA:Ensembl.
DR   GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR   FunFam; 2.60.120.260:FF:000021; Beta-galactosidase; 1.
DR   FunFam; 2.60.120.260:FF:000115; Beta-galactosidase; 1.
DR   FunFam; 3.20.20.80:FF:000017; Beta-galactosidase; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PDBsum; 7KDV; -.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..29
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012190"
FT   CHAIN           30..647
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012191"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         84
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         130
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         188
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         334
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..231
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   DISULFID        628..636
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   CONFLICT        517
FT                   /note="N -> D (in Ref. 2; AAA37292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="G -> R (in Ref. 2; AAA37292)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   647 AA;  73121 MW;  0E68EAA66A10803A CRC64;
     MLRVPLCTPL PLLALLQLLG AAHGIYNVTQ RTFKLDYSRD RFLKDGQPFR YISGSIHYFR
     IPRFYWEDRL LKMKMAGLNA IQMYVPWNFH EPQPGQYEFS GDRDVEHFIQ LAHELGLLVI
     LRPGPYICAE WDMGGLPAWL LEKQSIVLRS SDPDYLVAVD KWLAVLLPKM KPLLYQNGGP
     IITVQVENEY GSYFACDYDY LRFLVHRFRY HLGNDVILFT TDGASEKMLK CGTLQDLYAT
     VDFGTGNNIT QAFLVQRKFE PKGPLINSEF YTGWLDHWGK PHSTVKTKTL ATSLYNLLAR
     GANVNLYMFI GGTNFAYWNG ANTPYEPQPT SYDYDAPLSE AGDLTKKYFA LREVIQMFKE
     VPEGPIPPST PKFAYGKVAL RKFKTVAEAL GILCPNGPVK SLYPLTFTQV KQYFGYVLYR
     TTLPQDCSNP KPIFSSPFNG VRDRAYVSVD GVPQGILDRN LMTALNIRGK AGATLDILVE
     NMGRVNYGRF INDFKGLISN MTINSTVLTN WTVFPLNTEA MVRNHLWGRE ASDEGHLDGR
     STSNSSDLIL PTFYVGNFSI PSGIPDLPQD TFIQFPGWSK GQVWINGFNL GRYWPTMGPQ
     KTLFVPRNIL TTSAPNNITV LELEFAPCSE GTPELCTVEF VDTPVIS
//