GenomeNet

Database: UniProt/SWISS-PROT
Entry: BGAL_BOVIN
LinkDB: BGAL_BOVIN
Original site: BGAL_BOVIN 
ID   BGAL_BOVIN              Reviewed;         653 AA.
AC   Q58D55; A5LIP2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   23-MAY-2018, entry version 77.
DE   RecName: Full=Beta-galactosidase;
DE            EC=3.2.1.23 {ECO:0000250|UniProtKB:P16278};
DE   AltName: Full=Acid beta-galactosidase;
DE            Short=Lactase;
DE   Flags: Precursor;
GN   Name=GLB1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Satoh Y., Yajima A., Uda Y.;
RT   "Molecular cloning and characterization of lysosomal beta-
RT   galactosidase from bovine liver.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250|UniProtKB:P16278}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000250|UniProtKB:P16278}.
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; AB325580; BAF64285.1; -; mRNA.
DR   EMBL; BT021742; AAX46589.1; -; mRNA.
DR   RefSeq; NP_001030215.1; NM_001035043.1.
DR   UniGene; Bt.6127; -.
DR   ProteinModelPortal; Q58D55; -.
DR   SMR; Q58D55; -.
DR   STRING; 9913.ENSBTAP00000020296; -.
DR   BindingDB; Q58D55; -.
DR   ChEMBL; CHEMBL3482; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q58D55; -.
DR   PRIDE; Q58D55; -.
DR   GeneID; 507188; -.
DR   KEGG; bta:507188; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000221607; -.
DR   HOVERGEN; HBG004841; -.
DR   InParanoid; Q58D55; -.
DR   KO; K12309; -.
DR   PRO; PR:Q58D55; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 3.
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; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23     27       {ECO:0000250}.
FT                                /FTId=PRO_0000283035.
FT   CHAIN        28    653       Beta-galactosidase.
FT                                /FTId=PRO_0000283036.
FT   ACT_SITE    187    187       Proton donor.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   ACT_SITE    267    267       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING      82     82       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     128    128       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     186    186       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     332    332       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     96     96       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    497    497       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    194    229       {ECO:0000250|UniProtKB:P16278}.
FT   DISULFID    625    633       {ECO:0000250|UniProtKB:P16278}.
SQ   SEQUENCE   653 AA;  73413 MW;  37ED2284A4EB4F97 CRC64;
     MPGVVRLLAL LLVPLLLGSA RGLHNATQRT FQIDYRRNRF LKDGQPFRYI SGSIHYFRVP
     RFYWKDRLLK MKMAGLNAIQ TYVAWNFHEL QPGRYNFSGD HDVEHFIQLA HELGLLVILR
     PGPYICAEWD MGGLPAWLLE KKSIVLRSSD PDYLAAVDKW LGVLLPKMRP LLYKNGGPII
     TVQVENEYGS YLSCDYDYLR FLQKRFHDHL GEDVLLFTTD GVNERLLQCG ALQGLYATVD
     FSPGTNLTAA FMLQRKFEPT GPLVNSEFYT GWLDHWGQRH STVSSKAVAF TLHDMLALGA
     NVNMYMFIGG TNFAYWNGAN IPYQPQPTSY DYDAPLSEAG DLTEKYFALR DIIQKFAKVP
     EGPIPPSTPK FAYGKVALNK LKTVEDALNI LCPSGPIKSV YPLTFIDVKQ YFGFVLYRTM
     LPEDCSDPTP LSSPLSGVHD RAYVSVNGVA QGILERESVI TLNITGKAGA TLDLLVENMG
     RVNYGSSIND FKGLVSNLTL GSKILTNWEI FPLDMEDAVR SHLGTWGGRD RGYHNKARAH
     SPPTYALPTF YVGNFTIPSG IADLPQDTFI QFPGWTKGQV WINGFNLGRY WPVRGPQMTL
     FVPQHILVTS TPNTIVVLEL EHAPCQDGGP ELCTVEFVDK PVFRTVQTHR HAN
//
DBGET integrated database retrieval system