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 03-AUG-2022, entry version 115.
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; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; 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 (GLB1)
RT 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 FUNCTION.
RC TISSUE=Kidney, Muscle, Pancreas, and Testis;
RX PubMed=8725782;
RX DOI=10.1002/(sici)1096-8628(19960517)63:2<340::aid-ajmg3>3.0.co;2-x;
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 residues
CC 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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ196436; ABA43388.1; -; mRNA.
DR EMBL; AF056084; AAC12775.1; -; mRNA.
DR RefSeq; NP_001032730.1; NM_001037641.1.
DR AlphaFoldDB; Q9TRY9; -.
DR SMR; Q9TRY9; -.
DR STRING; 9612.ENSCAFP00000006929; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9TRY9; -.
DR PRIDE; Q9TRY9; -.
DR Ensembl; ENSCAFT00000007487; ENSCAFP00000006929; ENSCAFG00000004652.
DR Ensembl; ENSCAFT00030048317; ENSCAFP00030042278; ENSCAFG00030026124.
DR Ensembl; ENSCAFT00040020956; ENSCAFP00040018195; ENSCAFG00040011223.
DR Ensembl; ENSCAFT00845041332; ENSCAFP00845032404; ENSCAFG00845023378.
DR GeneID; 403873; -.
DR KEGG; cfa:403873; -.
DR CTD; 2720; -.
DR VEuPathDB; HostDB:ENSCAFG00845023378; -.
DR VGNC; VGNC:41249; GLB1.
DR eggNOG; KOG0496; Eukaryota.
DR GeneTree; ENSGT00950000182942; -.
DR InParanoid; Q9TRY9; -.
DR OrthoDB; 179316at2759; -.
DR Reactome; R-CFA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CFA-2022857; Keratan sulfate degradation.
DR Reactome; R-CFA-2024096; HS-GAG degradation.
DR Reactome; R-CFA-4085001; Sialic acid metabolism.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Proteomes; UP000002254; Chromosome 23.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; 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 Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..29
FT /evidence="ECO:0000250"
FT /id="PRO_0000012181"
FT CHAIN 30..668
FT /note="Beta-galactosidase"
FT /id="PRO_0000012182"
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 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 196..231
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT DISULFID 627..635
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT VARIANT 280
FT /note="Q -> P"
FT VARIANT 442
FT /note="D -> V"
FT VARIANT 444
FT /note="A -> V"
FT CONFLICT 60
FT /note="R -> H (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="G -> A (in Ref. 3)"
FT /evidence="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
