GenomeNet

Database: UniProt
Entry: BGAL_CANLF
LinkDB: BGAL_CANLF
Original site: BGAL_CANLF 
ID   BGAL_CANLF              Reviewed;         668 AA.
AC   Q9TRY9; O62800; Q3HTI1;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   16-JAN-2019, entry version 103.
DE   RecName: Full=Beta-galactosidase;
DE            EC=3.2.1.23 {ECO:0000269|PubMed:8725782};
DE   AltName: Full=Acid beta-galactosidase;
DE            Short=Lactase;
DE   Flags: Precursor;
GN   Name=GLB1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Kreutzer R., Mueller G., Leeb T., Moritz A., Baumgaertner W.;
RT   "The entire coding region of the canine lysosomal beta-galactosidase
RT   (GLB1) gene.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-668.
RC   STRAIN=Beagle; TISSUE=Brain;
RA   Smith B.F., Georgeson M., Baker H.J.;
RT   "A partial sequence of canine lysosomal beta-galactosidase (GLB1).";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-668, CATALYTIC ACTIVITY, AND
RP   FUNCTION.
RC   TISSUE=Kidney, Muscle, Pancreas, and Testis;
RX   PubMed=8725782;
RX   DOI=10.1002/(SICI)1096-8628(19960517)63:2<340::AID-AJMG3>3.3.CO;2-Y;
RA   Ahern-Rindell A.J., Kretz K.A., O'Brien J.S.;
RT   "Comparison of the canine and human acid beta-galactosidase gene.";
RL   Am. J. Med. Genet. 63:340-345(1996).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000305|PubMed:8725782}.
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:8725782};
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; DQ196436; ABA43388.1; -; mRNA.
DR   EMBL; AF056084; AAC12775.1; -; mRNA.
DR   RefSeq; NP_001032730.1; NM_001037641.1.
DR   UniGene; Cfa.22721; -.
DR   ProteinModelPortal; Q9TRY9; -.
DR   SMR; Q9TRY9; -.
DR   STRING; 9615.ENSCAFP00000006929; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q9TRY9; -.
DR   PRIDE; Q9TRY9; -.
DR   GeneID; 403873; -.
DR   KEGG; cfa:403873; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000221607; -.
DR   HOVERGEN; HBG004841; -.
DR   InParanoid; Q9TRY9; -.
DR   KO; K12309; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000002254; 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; -; 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; Polymorphism; Reference proteome; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25     29       {ECO:0000250}.
FT                                /FTId=PRO_0000012181.
FT   CHAIN        30    668       Beta-galactosidase.
FT                                /FTId=PRO_0000012182.
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    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    499    499       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    546    546       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    556    556       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    196    231       {ECO:0000250|UniProtKB:P16278}.
FT   DISULFID    627    635       {ECO:0000250|UniProtKB:P16278}.
FT   VARIANT     280    280       Q -> P.
FT   VARIANT     442    442       D -> V.
FT   VARIANT     444    444       A -> V.
FT   CONFLICT     60     60       R -> H (in Ref. 3). {ECO:0000305}.
FT   CONFLICT    227    227       K -> L (in Ref. 3). {ECO:0000305}.
FT   CONFLICT    342    342       G -> A (in Ref. 3). {ECO:0000305}.
SQ   SEQUENCE   668 AA;  74992 MW;  56B4A4AC7357221E CRC64;
     MARPAAVRVL WALLLPLLLG SARGLRNASQ RTFTIDYSHN RFLKDGQPFR YISGSIHYSR
     VPRFYWKDRL LKMKMAGLNA IQTYVPWNFH EPQPGQYQFS GEQDVEYFIK LAHELGLLVI
     LRPGPYICAE WDMGGLPAWL LLKESIILRS SDPDYLAAVD KWLGVLLPKM KPLLYQNGGP
     IITMQVENEY GSYFTCDYDY LRFLQKLFHH HLGNDVLLFT TDGANEKFLQ CGALQGLYAT
     VDFGPGANIT AAFQIQRKSE PKGPLVNSEF YTGWLDHWGQ PHSTVRTEVV ASSLHDILAH
     GANVNLYMFI GGTNFAYWNG ANMPYQAQPT SYDYDAPLSE AGDLTEKYFA LREVIRKFEK
     VPEGFIPPST PKFAYGKVAL KKLKTVEEAL NVLCPPGPIN SLYPLTFIQV KQYFGFVMYR
     TTLPQDCSDP TPLSSPLSGV HDRAYVSVDG VPQGVMERSN VITLNITGKA GATLDLLVEN
     MGRVNYGRYI NDFKGLISNL TLGSSILTNW MIFPLNTEDA VRSHLGGWHG PNNGRHDKTF
     AHRSSNYTLP AFYMGNFSIP SGIPDLPQDT FIQFPGWTKG QVWINGFNLG RYWPARGPQM
     TLFVPRHILV TSTPNTIMVL ELEHAPCGDS GPEVCTVEFV DRPVIGAPPT PGHPPPDLSH
     RDLRLDYV
//
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