Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5R5N6 (BGLR_PONAB)

Last modified November 24, 2009. Version 31. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Beta-glucuronidase
    EC=3.2.1.31
Gene names
Name: GUSB
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Hide | Top

Protein attributes

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

Hide | Top

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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Hide | Top

Ontologies

Keywords
   Cellular componentLysosome
   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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 651629Beta-glucuronidase
PRO_0000231039

Sites

Active site4511Proton donor By similarity

Amino acid modifications

Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation6311N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict41G → R in CAH92009. Ref.1
Sequence conflict691R → Q in CAH92930. Ref.1
Sequence conflict3701F → I in CAH92009. Ref.1
Sequence conflict4061E → G in CAH92930. Ref.1
Sequence conflict4601G → D in CAH92009. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q5R5N6-1 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: A3170629BE393917

FASTA65174,772
        10         20         30         40         50         60 
MARGSAVAWA AFGPLLWGCA LGLQGGMLYP QESRSRERKE LDGLWSFRAD FSDNRRRGFE 

        70         80         90        100        110        120 
EQWYRRPLRE SGPTLDMPVP SSFNDISQDW RLRHFVGWVW YEREVILPER WTQDLHTRVV 

       130        140        150        160        170        180 
LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE ADISNLVQVG PLPSRLRITI AINNTLTPTT 

       190        200        210        220        230        240 
LPPGTIQYMN DTSKYPKGYF VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTGVEQD 

       250        260        270        280        290        300 
SGLVNYQISV KGSNLFELEA RLLDAENKVV ANGTGTQGQL KVPGASLWWP YLMHERPAYL 

       310        320        330        340        350        360 
YSLEVRLTAQ TSLGPVSDFY SLPVGIRTVA VTESQFLING KPFYFHGVNK HEDADIRGKG 

       370        380        390        400        410        420 
FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVLQMCDRHG IVVIDECPGV GLALPQFFNN 

       430        440        450        460        470        480 
VSLHHHMRVM EEVVRRDKNH PAVVMWSVAN EPASHLESAG YYLKMVIAHT KALDPSRPVT 

       490        500        510        520        530        540 
FVSNSNYAAD KGAPYVDVIC LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE 

       550        560        570        580        590        600 
YGAETIAGFH QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSLTR 

       610        620        630        640        650 
VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSPF T

« Hide

Hide | Top

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex and Kidney.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR859852 mRNA. Translation: CAH92009.1.
CR860821 mRNA. Translation: CAH92930.1.
RefSeqNP_001126724.1.
NP_001128846.1.
UniGenePab.18644
Pab.8068

3D structure databases

SMRQ5R5N6. Positions 22-632.
ModBaseSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Genome annotation databases

GeneID100173726.
100189763.

Organism-specific databases

CTD100173726.

Phylogenomic databases

HOVERGENQ5R5N6.

Enzyme and pathway databases

BRENDA3.2.1.31. 269192.

Family and domain databases

InterProIPR008979. Galactose-bd-like.
IPR006101. 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.
IPR017853. Glyco_hydro_catalytic_core.
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...

Hide | Top

Entry information

Entry nameBGLR_PONAB
AccessionPrimary (citable) accession number: Q5R5N6
Secondary accession number(s): Q5R8A1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: November 24, 2009
This is version 31 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

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