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O18835

- BGLR_CANFA

UniProt

O18835 - BGLR_CANFA

Protein

Beta-glucuronidase

Gene

GUSB

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Plays an important role in the degradation of dermatan and keratan sulfates.By similarity

    Catalytic activityi

    A beta-D-glucuronoside + H2O = D-glucuronate + an alcohol.

    Enzyme regulationi

    Inhibited by L-aspartic acid.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei450 – 4501Proton donorBy similarity

    GO - Molecular functioni

    1. beta-glucuronidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucuronidase (EC:3.2.1.31)
    Gene namesi
    Name:GUSB
    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

    Pathology & Biotechi

    Involvement in diseasei

    Defects in GUSB are the cause of mucopolysaccharidosis type VII (MPS VII), an inherited disease reported in humans, mice, cats, and dogs.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 651629Beta-glucuronidasePRO_0000012158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi630 – 6301N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiO18835.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000031474.

    Structurei

    3D structure databases

    ProteinModelPortaliO18835.
    SMRiO18835. Positions 22-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000120896.
    HOVERGENiHBG004843.
    KOiK01195.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view]
    PRINTSiPR00132. GLHYDRLASE2.
    SUPFAMiSSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O18835-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGPAGAWV ALGPLLWTCG LALEGGMLYP RESPSRERKD LDGLWSFRAD    50
    FSDGRRQGFE QQWYRAPLRE SGPTLDMPVP SSFNDVGQDR QLRSFVGWVW 100
    YEREATLPRR WSQDPGTRVV LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE 150
    ADISKLVQSG PLSSCRITLA INNTLTPHTL PPGTIVYKTD ASKYPKGYFV 200
    QNTYFDFFNY AGLHRPVLLY TTPTTYIDDI TVTTGVDQDT GLVDYQIFVQ 250
    GSEHFQLEVY LLDEEGKVVA QGTGSQGRLQ VPNVHLWWPY LMHEHPAYLY 300
    SLEVRLTAQM AAGPVSDFYT LPVGIRTVAV TERQFLINGK PFYFHGVNKH 350
    EDADIRGKGF DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMQLCDRYGI 400
    VVIDESPGVG IMLVQSYSNV SLQHHLEVMG ELVRRDKNHP SVVMWSVANE 450
    PTSFLKPAAY YFKTLIAHTK ALDPSRPVTF VTNSNYEADL GAPYVDVICV 500
    NSYYSWYHDY GHMEVIQLQL ATEFENWYRT YQKPIIQSEY GAETIAGFHQ 550
    DPPLMFSEEY QKGLLEQYHL VLDQKRKEYV VGELIWNFAD FMTDQSPQRA 600
    VGNRKGIFTR QRQPKAAAFL LRERYWKLAN ETGHHRSAAK SQCLENSPFA 650
    L 651
    Length:651
    Mass (Da):74,433
    Last modified:January 1, 1998 - v1
    Checksum:iE8991B1E65C60120
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661R → H in MPS VII; loss of activity. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019759 mRNA. Translation: AAC48809.1.
    RefSeqiNP_001003191.1. NM_001003191.1.
    UniGeneiCfa.3694.

    Genome annotation databases

    GeneIDi403831.
    KEGGicfa:403831.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019759 mRNA. Translation: AAC48809.1 .
    RefSeqi NP_001003191.1. NM_001003191.1.
    UniGenei Cfa.3694.

    3D structure databases

    ProteinModelPortali O18835.
    SMRi O18835. Positions 22-631.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000031474.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Proteomic databases

    PaxDbi O18835.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403831.
    KEGGi cfa:403831.

    Organism-specific databases

    CTDi 2990.

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000120896.
    HOVERGENi HBG004843.
    KOi K01195.

    Miscellaneous databases

    NextBioi 20817327.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00132. GLHYDRLASE2.
    SUPFAMi SSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the canine beta-glucuronidase cDNA, mutation identification in canine MPS VII, and retroviral vector-mediated correction of MPS VII cells."
      Ray J., Bouvet A., Desanto C., Fyfe J.C., Xu D., Wolfe J.H., Aguirre G.D., Patterson D.F., Haskins M.E., Henthorn P.S.
      Genomics 48:248-253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MPS VII HIS-166.

    Entry informationi

    Entry nameiBGLR_CANFA
    AccessioniPrimary (citable) accession number: O18835
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 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