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Reviewed, UniProtKB/Swiss-Prot O18835 (BGLR_CANFA)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-glucuronidase
    EC=3.2.1.31
Gene names
Name: GUSB
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Inhibited by L-aspartic acid By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Lysosome.

Involvement in disease

Defects in GUSB are the cause of mucopolysaccharidosis type VII (MPS VII), an inherited disease reported in humans, mice, cats, and dogs. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   Cellular componentLysosome
   DiseaseDisease mutation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbeta-glucuronidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 651629Beta-glucuronidase
PRO_0000012158

Sites

Active site4501Proton donor By similarity

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation6301N-linked (GlcNAc...) Potential

Natural variations

Natural variant1661R → H in MPS VII; loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O18835-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E8991B1E65C60120

FASTA65174,433
        10         20         30         40         50         60 
MSRGPAGAWV ALGPLLWTCG LALEGGMLYP RESPSRERKD LDGLWSFRAD FSDGRRQGFE 

        70         80         90        100        110        120 
QQWYRAPLRE SGPTLDMPVP SSFNDVGQDR QLRSFVGWVW YEREATLPRR WSQDPGTRVV 

       130        140        150        160        170        180 
LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE ADISKLVQSG PLSSCRITLA INNTLTPHTL 

       190        200        210        220        230        240 
PPGTIVYKTD ASKYPKGYFV QNTYFDFFNY AGLHRPVLLY TTPTTYIDDI TVTTGVDQDT 

       250        260        270        280        290        300 
GLVDYQIFVQ GSEHFQLEVY LLDEEGKVVA QGTGSQGRLQ VPNVHLWWPY LMHEHPAYLY 

       310        320        330        340        350        360 
SLEVRLTAQM AAGPVSDFYT LPVGIRTVAV TERQFLINGK PFYFHGVNKH EDADIRGKGF 

       370        380        390        400        410        420 
DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMQLCDRYGI VVIDESPGVG IMLVQSYSNV 

       430        440        450        460        470        480 
SLQHHLEVMG ELVRRDKNHP SVVMWSVANE PTSFLKPAAY YFKTLIAHTK ALDPSRPVTF 

       490        500        510        520        530        540 
VTNSNYEADL GAPYVDVICV NSYYSWYHDY GHMEVIQLQL ATEFENWYRT YQKPIIQSEY 

       550        560        570        580        590        600 
GAETIAGFHQ DPPLMFSEEY QKGLLEQYHL VLDQKRKEYV VGELIWNFAD FMTDQSPQRA 

       610        620        630        640        650 
VGNRKGIFTR QRQPKAAAFL LRERYWKLAN ETGHHRSAAK SQCLENSPFA L 

« Hide

References

[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: 9521879] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MPS VII HIS-166.

Cross-references

Sequence databases

AF019759 mRNA. Translation: AAC48809.1.
RefSeqNP_001003191.1.
UniGeneCfa.3694

3D structure databases

HSSPHSSP built from PDB template 1BHG based on UniProtKB P08236.
SMRO18835. Positions 22-631.
ModBaseSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Genome annotation databases

EnsemblENSCAFG00000010193. Canis familiaris. [Contig view]
GeneID403831.
KEGGcfa:403831.

Phylogenomic databases

HOVERGENO18835.

Enzyme and pathway databases

BRENDA3.2.1.31. 463.

Family and domain databases

InterProIPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006104. Glyco_hydro_2_carb-bd.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLR_CANFA
AccessionPrimary (citable) accession number: O18835
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents