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Q9TRY9

- BGAL_CANFA

UniProt

Q9TRY9 - BGAL_CANFA

Protein

Beta-galactosidase

Gene

GLB1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (02 May 2006)
      Previous versions | rss
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    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

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_182226. Glycosphingolipid metabolism.
    REACT_182384. Keratan sulfate degradation.
    REACT_220733. HS-GAG degradation.
    REACT_222277. Sialic acid 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: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    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.

    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

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    MARPAAVRVL WALLLPLLLG SARGLRNASQ RTFTIDYSHN RFLKDGQPFR    50
    YISGSIHYSR VPRFYWKDRL LKMKMAGLNA IQTYVPWNFH EPQPGQYQFS 100
    GEQDVEYFIK LAHELGLLVI LRPGPYICAE WDMGGLPAWL LLKESIILRS 150
    SDPDYLAAVD KWLGVLLPKM KPLLYQNGGP IITMQVENEY GSYFTCDYDY 200
    LRFLQKLFHH HLGNDVLLFT TDGANEKFLQ CGALQGLYAT VDFGPGANIT 250
    AAFQIQRKSE PKGPLVNSEF YTGWLDHWGQ PHSTVRTEVV ASSLHDILAH 300
    GANVNLYMFI GGTNFAYWNG ANMPYQAQPT SYDYDAPLSE AGDLTEKYFA 350
    LREVIRKFEK VPEGFIPPST PKFAYGKVAL KKLKTVEEAL NVLCPPGPIN 400
    SLYPLTFIQV KQYFGFVMYR TTLPQDCSDP TPLSSPLSGV HDRAYVSVDG 450
    VPQGVMERSN VITLNITGKA GATLDLLVEN MGRVNYGRYI NDFKGLISNL 500
    TLGSSILTNW MIFPLNTEDA VRSHLGGWHG PNNGRHDKTF AHRSSNYTLP 550
    AFYMGNFSIP SGIPDLPQDT FIQFPGWTKG QVWINGFNLG RYWPARGPQM 600
    TLFVPRHILV TSTPNTIMVL ELEHAPCGDS GPEVCTVEFV DRPVIGAPPT 650
    PGHPPPDLSH RDLRLDYV 668
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ196436 mRNA. Translation: ABA43388.1 .
    AF056084 mRNA. Translation: AAC12775.1 .
    RefSeqi NP_001032730.1. NM_001037641.1.
    UniGenei Cfa.22721.

    3D structure databases

    ProteinModelPortali Q9TRY9.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9TRY9.
    PRIDEi Q9TRY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403873.
    KEGGi cfa:403873.

    Organism-specific databases

    CTDi 2720.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000221607.
    HOVERGENi HBG004841.
    InParanoidi Q9TRY9.
    KOi K12309.

    Enzyme and pathway databases

    Reactomei REACT_182226. Glycosphingolipid metabolism.
    REACT_182384. Keratan sulfate degradation.
    REACT_220733. HS-GAG degradation.
    REACT_222277. Sialic acid metabolism.

    Miscellaneous databases

    NextBioi 20817366.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR026283. 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 ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006336. B-gal. 1 hit.
    PRINTSi PR00742. GLHYDRLASE35.
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 83 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