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Protein

Beta-galactosidase

Gene

GLB1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton donorSequence Analysis
Active sitei269 – 2691NucleophileSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_330129. HS-GAG degradation.
REACT_352535. Keratan sulfate degradation.
REACT_353177. Sialic acid metabolism.
REACT_354238. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase (EC:3.2.1.23)
Alternative name(s):
Acid beta-galactosidase
Short name:
Lactase
Gene namesi
Name:GLB1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 295By similarityPRO_0000012181
Chaini30 – 668639Beta-galactosidasePRO_0000012182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9TRY9.
PRIDEiQ9TRY9.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000006929.

Structurei

3D structure databases

ProteinModelPortaliQ9TRY9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000221607.
HOVERGENiHBG004841.
InParanoidiQ9TRY9.
KOiK12309.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR026283. B-gal_1-like.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFiPIRSF006336. B-gal. 1 hit.
PRINTSiPR00742. GLHYDRLASE35.
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9TRY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARPAAVRVL WALLLPLLLG SARGLRNASQ RTFTIDYSHN RFLKDGQPFR
60 70 80 90 100
YISGSIHYSR VPRFYWKDRL LKMKMAGLNA IQTYVPWNFH EPQPGQYQFS
110 120 130 140 150
GEQDVEYFIK LAHELGLLVI LRPGPYICAE WDMGGLPAWL LLKESIILRS
160 170 180 190 200
SDPDYLAAVD KWLGVLLPKM KPLLYQNGGP IITMQVENEY GSYFTCDYDY
210 220 230 240 250
LRFLQKLFHH HLGNDVLLFT TDGANEKFLQ CGALQGLYAT VDFGPGANIT
260 270 280 290 300
AAFQIQRKSE PKGPLVNSEF YTGWLDHWGQ PHSTVRTEVV ASSLHDILAH
310 320 330 340 350
GANVNLYMFI GGTNFAYWNG ANMPYQAQPT SYDYDAPLSE AGDLTEKYFA
360 370 380 390 400
LREVIRKFEK VPEGFIPPST PKFAYGKVAL KKLKTVEEAL NVLCPPGPIN
410 420 430 440 450
SLYPLTFIQV KQYFGFVMYR TTLPQDCSDP TPLSSPLSGV HDRAYVSVDG
460 470 480 490 500
VPQGVMERSN VITLNITGKA GATLDLLVEN MGRVNYGRYI NDFKGLISNL
510 520 530 540 550
TLGSSILTNW MIFPLNTEDA VRSHLGGWHG PNNGRHDKTF AHRSSNYTLP
560 570 580 590 600
AFYMGNFSIP SGIPDLPQDT FIQFPGWTKG QVWINGFNLG RYWPARGPQM
610 620 630 640 650
TLFVPRHILV TSTPNTIMVL ELEHAPCGDS GPEVCTVEFV DRPVIGAPPT
660
PGHPPPDLSH RDLRLDYV
Length:668
Mass (Da):74,992
Last modified:May 2, 2006 - v3
Checksum:i56B4A4AC7357221E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601R → H (PubMed:8725782).Curated
Sequence conflicti227 – 2271K → L (PubMed:8725782).Curated
Sequence conflicti342 – 3421G → A (PubMed:8725782).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801Q → P.
Natural varianti442 – 4421D → V.
Natural varianti444 – 4441A → V.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ196436 mRNA. Translation: ABA43388.1.
AF056084 mRNA. Translation: AAC12775.1.
RefSeqiNP_001032730.1. NM_001037641.1.
UniGeneiCfa.22721.

Genome annotation databases

GeneIDi403873.
KEGGicfa:403873.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ196436 mRNA. Translation: ABA43388.1.
AF056084 mRNA. Translation: AAC12775.1.
RefSeqiNP_001032730.1. NM_001037641.1.
UniGeneiCfa.22721.

3D structure databases

ProteinModelPortaliQ9TRY9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000006929.

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.

Proteomic databases

PaxDbiQ9TRY9.
PRIDEiQ9TRY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403873.
KEGGicfa:403873.

Organism-specific databases

CTDi2720.

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000221607.
HOVERGENiHBG004841.
InParanoidiQ9TRY9.
KOiK12309.

Enzyme and pathway databases

ReactomeiREACT_330129. HS-GAG degradation.
REACT_352535. Keratan sulfate degradation.
REACT_353177. Sialic acid metabolism.
REACT_354238. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi20817366.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR026283. B-gal_1-like.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFiPIRSF006336. B-gal. 1 hit.
PRINTSiPR00742. GLHYDRLASE35.
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The entire coding region of the canine lysosomal beta-galactosidase (GLB1) gene."
    Kreutzer R., Mueller G., Leeb T., Moritz A., Baumgaertner W.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  2. "A partial sequence of canine lysosomal beta-galactosidase (GLB1)."
    Smith B.F., Georgeson M., Baker H.J.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-668.
    Strain: Beagle.
    Tissue: Brain.
  3. "Comparison of the canine and human acid beta-galactosidase gene."
    Ahern-Rindell A.J., Kretz K.A., O'Brien J.S.
    Am. J. Med. Genet. 63:340-345(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-668.
    Tissue: Kidney, Muscle, Pancreas and Testis.

Entry informationi

Entry nameiBGAL_CANFA
AccessioniPrimary (citable) accession number: Q9TRY9
Secondary accession number(s): O62800, Q3HTI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: May 2, 2006
Last modified: July 22, 2015
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.