Skip Header

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

P06760 (BGLR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucuronidase
EC=3.2.1.31
Gene names
Name:Gusb
Synonyms:Gus
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Inhibited by L-aspartic acid By similarity.

Subunit structure

Homotetramer.

Subcellular location

Lysosome.

Post-translational modification

Undergoes a post-transcriptional proteolytic cleavage near its C-terminal end, which reduces its size by approximately 3 kDa. The site of this cleavage has as yet not been determined.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from direct assay PubMed 8702598. Source: RGD

   Molecular_functionbeta-glucuronidase activity

Inferred from direct assay Ref.2PubMed 8702598. Source: RGD

carbohydrate binding

Inferred from direct assay PubMed 8702598. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 648626Beta-glucuronidase
PRO_0000012163

Sites

Active site4471Proton donor By similarity

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict141Q → E in CAA68705. Ref.2
Sequence conflict211V → L in CAA68705. Ref.2
Sequence conflict4871M → L in CAA68705. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06760 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5ADE8F5234F0907E

FASTA64874,793
        10         20         30         40         50         60 
MSPRRSVCWF VLGQLLCSCA VALQGGMLFP KETPSRELKV LDGLWSFRAD YSNNRLQGFE 

        70         80         90        100        110        120 
KQWYRQPLRE SGPTLDMPVP SSFNDITQEA ELRNFIGWVW YEREAVLPQR WTQDTDRRVV 

       130        140        150        160        170        180 
LRINSAHYYA VVWVNGIHVV EHEGGHLPFE ADITKLVQSG PLTTFRVTIA INNTLTPYTL 

       190        200        210        220        230        240 
PPGTIVYKTD PSMYPKGYFV QDISFDFFNY AGLHRSVVLY TTPTTYIDDI TVTTDVDRDV 

       250        260        270        280        290        300 
GLVNYWISVQ GSDHFQLEVR LLDEDGKIVA RGTGNEGQLK VPRAHLWWPY LMHEHPAYLY 

       310        320        330        340        350        360 
SLEVTMTTPE SVSDFYTLPV GIRTVAVTKS KFLINGKPFY FQGVNKHEDS DIRGRGFDWP 

       370        380        390        400        410        420 
LLIKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI DECPGVGIVL PQSFGNVSLR 

       430        440        450        460        470        480 
HHLEVMDELV RRDKNHPAVV MWSVANEPVS SLKPAGYYFK TLIAHTKALD PTRPVTFVSN 

       490        500        510        520        530        540 
TRYDADMGAP YVDVICVNSY LSWYHDYGHL EVIQLQLTSQ FENWYKMYQK PIIQSEYGAD 

       550        560        570        580        590        600 
AVSGLHEDPP RMFSEEYQTA LLENYHLILD EKRKEYVIGE LIWNFADFMT NQSPLRVTGN 

       610        620        630        640 
KKGIFTRQRN PKMAAFILRE RYWRIANETR GYGSVPRTQC MGSRPFTF

« Hide

References

[1]"Nucleotide sequence of rat preputial gland beta-glucuronidase cDNA and in vitro insertion of its encoded polypeptide into microsomal membranes."
Nishimura Y., Rosenfeld M.G., Kreibich G., Gubler U., Sabatini D.D., Adesnik M., Andy R.
Proc. Natl. Acad. Sci. U.S.A. 83:7292-7296(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Preputial gland.
[2]"Rat liver beta-glucuronidase. cDNA cloning, sequence comparisons and expression of a chimeric protein in COS cells."
Powell P.P., Kyle J.W., Miller R.D., Pantano J., Grubb J.H., Sly W.S.
Biochem. J. 250:547-555(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-648.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M13962 mRNA. Translation: AAA41228.1.
Y00717 mRNA. Translation: CAA68705.1.
IPIIPI00776581.
PIRA25047.
RefSeqNP_058711.2. NM_017015.2.
UniGeneRn.3692.

3D structure databases

ProteinModelPortalP06760.
SMRP06760. Positions 22-628.
ModBaseSearch...

Protein-protein interaction databases

IntActP06760. 1 interaction.
STRING10116.ENSRNOP00000045033.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

PTM databases

PhosphoSiteP06760.

Proteomic databases

PaxDbP06760.
PRIDEP06760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24434.
KEGGrno:24434.

Organism-specific databases

CTD2990.
RGD2772. Gusb.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000120896.
HOVERGENHBG004843.
KOK01195.

Enzyme and pathway databases

SABIO-RKP06760.

Gene expression databases

ArrayExpressP06760.
GenevestigatorP06760.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008979. 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]
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
SUPFAMSSF49785. Gal_bind_like. 1 hit.
SSF49303. Glyco_hydro_2Ig. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP06760.
ChEMBLCHEMBL4814.
NextBio603309.

Entry information

Entry nameBGLR_RAT
AccessionPrimary (citable) accession number: P06760
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 29, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents