BGAL_MOUSE
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 03-AUG-2022, entry version 174.
DE RecName: Full=Beta-galactosidase;
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; 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], 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 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:0000250|UniProtKB:P16278}.
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 PDBsum; 7KDV; -.
DR AlphaFoldDB; P23780; -.
DR SMR; P23780; -.
DR BioGRID; 198341; 13.
DR STRING; 10090.ENSMUSP00000055803; -.
DR BindingDB; P23780; -.
DR ChEMBL; CHEMBL1667667; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GlyGen; P23780; 8 sites.
DR iPTMnet; P23780; -.
DR PhosphoSitePlus; P23780; -.
DR SwissPalm; P23780; -.
DR EPD; P23780; -.
DR jPOST; P23780; -.
DR PaxDb; P23780; -.
DR PeptideAtlas; P23780; -.
DR PRIDE; P23780; -.
DR ProteomicsDB; 273486; -.
DR Antibodypedia; 3647; 732 antibodies from 38 providers.
DR DNASU; 12091; -.
DR Ensembl; ENSMUST00000063042; ENSMUSP00000055803; ENSMUSG00000045594.
DR GeneID; 12091; -.
DR KEGG; mmu:12091; -.
DR UCSC; uc009rxj.3; mouse.
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; RAHPDTW; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; P23780; -.
DR TreeFam; TF314816; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR SABIO-RK; P23780; -.
DR BioGRID-ORCS; 12091; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Glb1; mouse.
DR PRO; PR:P23780; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P23780; protein.
DR Bgee; ENSMUSG00000045594; Expressed in right kidney and 252 other tissues.
DR ExpressionAtlas; P23780; baseline and differential.
DR Genevisible; P23780; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:MGI.
DR GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0019388; P:galactose catabolic process; ISO:MGI.
DR GO; GO:0051413; P:response to cortisone; IEA:Ensembl.
DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; PTHR23421; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 334
FT /ligand="substrate"
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
