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Database: UniProt
Entry: BGAL_MOUSE
LinkDB: BGAL_MOUSE
Original site: 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   13-FEB-2019, entry version 157.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   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
RT   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
CC         residues 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.
CC       {ECO:0000305}.
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   UniGene; Mm.290516; -.
DR   ProteinModelPortal; P23780; -.
DR   SMR; P23780; -.
DR   BioGrid; 198341; 1.
DR   IntAct; P23780; 1.
DR   MINT; P23780; -.
DR   STRING; 10090.ENSMUSP00000055803; -.
DR   BindingDB; P23780; -.
DR   ChEMBL; CHEMBL1667667; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
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   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   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   GeneTree; ENSGT00390000006586; -.
DR   HOGENOM; HOG000221607; -.
DR   HOVERGEN; HBG004841; -.
DR   InParanoid; P23780; -.
DR   KO; K12309; -.
DR   OMA; GWGKGIV; -.
DR   OrthoDB; 1263874at2759; -.
DR   PhylomeDB; P23780; -.
DR   TreeFam; TF314816; -.
DR   Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-MMU-4085001; Sialic acid metabolism.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   SABIO-RK; P23780; -.
DR   ChiTaRS; Glb1; mouse.
DR   PRO; PR:P23780; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000045594; Expressed in 287 organ(s), highest expression level in epithelium of small intestine.
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; ISO: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   Gene3D; 2.60.120.260; -; 2.
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   Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25     29       {ECO:0000250}.
FT                                /FTId=PRO_0000012190.
FT   CHAIN        30    647       Beta-galactosidase.
FT                                /FTId=PRO_0000012191.
FT   ACT_SITE    189    189       Proton donor.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   ACT_SITE    269    269       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING      84     84       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     130    130       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     188    188       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     334    334       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   CARBOHYD     27     27       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    500    500       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    504    504       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    510    510       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    544    544       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    617    617       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    196    231       {ECO:0000250|UniProtKB:P16278}.
FT   DISULFID    628    636       {ECO:0000250|UniProtKB:P16278}.
FT   CONFLICT    517    517       N -> D (in Ref. 2; AAA37292).
FT                                {ECO:0000305}.
FT   CONFLICT    539    539       G -> R (in Ref. 2; AAA37292).
FT                                {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
//
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