P12265 · BGLR_MOUSE
- ProteinBeta-glucuronidase
- GeneGusb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids648 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in the degradation of dermatan and keratan sulfates.
Catalytic activity
- a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Activity regulation
Inhibited by L-aspartic acid.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 447 | Proton donor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular space | |
Cellular Component | lysosomal lumen | |
Cellular Component | lysosome | |
Molecular Function | beta-glucuronidase activity | |
Molecular Function | carbohydrate binding | |
Molecular Function | hydrolase activity | |
Molecular Function | protein domain specific binding | |
Molecular Function | signaling receptor binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | chondroitin sulfate catabolic process | |
Biological Process | glucuronoside catabolic process | |
Biological Process | heparan sulfate proteoglycan catabolic process | |
Biological Process | hyaluronan catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-glucuronidase
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP12265
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: A small proportion is found in the endoplasmic reticulum.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 87 | in strain: C3H/HeJ | ||||
Sequence: T → I | ||||||
Natural variant | 233 | in allele GUS-SA | ||||
Sequence: I → T | ||||||
Natural variant | 428 | in allele GUS-SA | ||||
Sequence: E → K | ||||||
Natural variant | 616 | in allele GUS-SA | ||||
Sequence: F → L | ||||||
Natural variant | 642 | in allele W26; reduced retention in the endoplasmic reticulum | ||||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MSLKWSACWVALGQLLCSCALA | ||||||
Chain | PRO_0000012162 | 23-648 | Beta-glucuronidase | |||
Sequence: LKGGMLFPKESPSRELKALDGLWHFRADLSNNRLQGFEQQWYRQPLRESGPVLDMPVPSSFNDITQEAALRDFIGWVWYEREAILPRRWTQDTDMRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADISKLVQSGPLTTCRITIAINNTLTPHTLPPGTIVYKTDTSMYPKGYFVQDTSFDFFNYAGLHRSVVLYTTPTTYIDDITVITNVEQDIGLVTYWISVQGSEHFQLEVQLLDEGGKVVAHGTGNQGQLQVPSANLWWPYLMHEHPAYMYSLEVKVTTTESVTDYYTLPIGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGKGFDWPLLVKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNESLRHHLEVMEELVRRDKNHPAVVMWSVANEPSSALKPAAYYFKTLITHTKALDLTRPVTFVSNAKYDADLGAPYVDVICVNSYFSWYHDYGHLEVIQPQLNSQFENWYKTHQKPIIQSEYGADAIPGIHEDPPRMFSEEYQKAVLENYHSVLDQKRKEYVVGELIWNFADFMTNQSPLRVIGNKKGIFTRQRQPKTSAFILRERYWRIANETGGHGSGPRTQCFGSRPFTF | ||||||
Glycosylation | 172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 416 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 627 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length648
- Mass (Da)74,195
- Last updated2012-10-03 v2
- ChecksumCCD8F84C3CD6C498
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 265 | in Ref. 2; AAA37696, 3; AAA98623, 4; AAA63309 and 5; AAA37697 | ||||
Sequence: G → D | ||||||
Sequence conflict | 320 | in Ref. 2; AAA37696, 3; AAA98623 and 5; AAA37697 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03047 EMBL· GenBank· DDBJ | AAA37696.1 EMBL· GenBank· DDBJ | mRNA | ||
J02836 EMBL· GenBank· DDBJ | AAA98623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M63836 EMBL· GenBank· DDBJ | AAA63309.1 EMBL· GenBank· DDBJ | mRNA | ||
M28540 EMBL· GenBank· DDBJ | AAA63307.1 EMBL· GenBank· DDBJ | mRNA | ||
M28541 EMBL· GenBank· DDBJ | AAA63308.1 EMBL· GenBank· DDBJ | mRNA | ||
M19279 EMBL· GenBank· DDBJ | AAA37697.1 EMBL· GenBank· DDBJ | mRNA | ||
AK136519 EMBL· GenBank· DDBJ | BAE23021.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150048 EMBL· GenBank· DDBJ | BAE29265.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159526 EMBL· GenBank· DDBJ | BAE35155.1 EMBL· GenBank· DDBJ | mRNA | ||
AK162436 EMBL· GenBank· DDBJ | BAE36917.1 EMBL· GenBank· DDBJ | mRNA | ||
AC161345 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466529 EMBL· GenBank· DDBJ | EDL19485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC071226 EMBL· GenBank· DDBJ | AAH71226.1 EMBL· GenBank· DDBJ | mRNA |