Reviewed, UniProtKB/Swiss-Prot P12265 (BGLR_MOUSE)

Names and origin

Protein names

Recommended name:
    Beta-glucuronidase
    EC=3.2.1.31

Gene names

Name:	Gusb
Synonyms:	Gus, Gus-s

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Endoplasmic reticulum. Note: A small proportion is found in the endoplasmic reticulum. Ref.6
Sequence similarities	Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from direct assay. Source: MGI
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay. Source: MGI microsome Inferred from direct assay. Source: MGI
Molecular function	beta-glucuronidase activity Inferred from direct assay. Source: MGI cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22
	Chain	23 – 648	626	Beta-glucuronidase		PRO_0000012162
Sites
	Active site	447	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Glycosylation	416	1	N-linked (GlcNAc...) Potential
	Glycosylation	591	1	N-linked (GlcNAc...) Potential
	Glycosylation	627	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	87	1	T → I in strain: C3H/HeJ.
	Natural variant	233	1	I → T in allele GUS-SA.
	Natural variant	265	1	D → G in strain: YBR and C3H/HeJ.
	Natural variant	320	1	V → I in strain: YBR and C3H/HeJ.
	Natural variant	428	1	E → K in allele GUS-SA.
	Natural variant	616	1	F → L in allele GUS-SA.
	Natural variant	642	1	G → R in allele W26; reduced retention in the endoplasmic reticulum. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P12265-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 3D8C65A5DB3B96D6	FASTA	648	74,239
	10 20 30 40 50 60 MSLKWSACWV ALGQLLCSCA LALKGGMLFP KESPSRELKA LDGLWHFRAD LSNNRLQGFE 70 80 90 100 110 120 QQWYRQPLRE SGPVLDMPVP SSFNDITQEA ALRDFIGWVW YEREAILPRR WTQDTDMRVV 130 140 150 160 170 180 LRINSAHYYA VVWVNGIHVV EHEGGHLPFE ADISKLVQSG PLTTCRITIA INNTLTPHTL 190 200 210 220 230 240 PPGTIVYKTD TSMYPKGYFV QDTSFDFFNY AGLHRSVVLY TTPTTYIDDI TVITNVEQDI 250 260 270 280 290 300 GLVTYWISVQ GSEHFQLEVQ LLDEDGKVVA HGTGNQGQLQ VPSANLWWPY LMHEHPAYMY 310 320 330 340 350 360 SLEVKVTTTE SVTDYYTLPV GIRTVAVTKS KFLINGKPFY FQGVNKHEDS DIRGKGFDWP 370 380 390 400 410 420 LLVKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI DECPGVGIVL PQSFGNESLR 430 440 450 460 470 480 HHLEVMEELV RRDKNHPAVV MWSVANEPSS ALKPAAYYFK TLITHTKALD LTRPVTFVSN 490 500 510 520 530 540 AKYDADLGAP YVDVICVNSY FSWYHDYGHL EVIQPQLNSQ FENWYKTHQK PIIQSEYGAD 550 560 570 580 590 600 AIPGIHEDPP RMFSEEYQKA VLENYHSVLD QKRKEYVVGE LIWNFADFMT NQSPLRVIGN 610 620 630 640 KKGIFTRQRQ PKTSAFILRE RYWRIANETG GHGSGPRTQC FGSRPFTF

References

[1]	"DNA sequence variation within the beta-glucuronidase gene complex among inbred strains of mice." Gallagher P.M., D'Amore M.A., Lund S.D., Elliott R.W., Pazik J., Hohman C., Korfhagen T.R., Ganschow R.E. Genomics 1:145-152(1987) [PubMed: 2891607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The complete nucleotide sequence of murine beta-glucuronidase mRNA and its deduced polypeptide." Gallagher P.M., D'Amore M.A., Lund S.D., Ganschow R.E. Genomics 2:215-219(1988) [PubMed: 3397060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequence and organization of the murine beta-glucuronidase gene." D'Amore M.A., Gallagher P.M., Korfhagen T.R., Ganschow R.E. Biochemistry 27:7131-7140(1988) [PubMed: 3196706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"DNA determinants of structural and regulatory variation within the murine beta-glucuronidase gene complex." Wawrzyniak C.J., Gallagher P.M., D'Amore M.A., Carter J.E., Lund S.D., Rinchik E.M., Ganschow R.E. Mol. Cell. Biol. 9:4074-4078(1989) [PubMed: 2779578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/HeJ and YBR. Tissue: Sperm.
[5]	"Genomic organization and sequence of the Gus-s alpha allele of the murine beta-glucuronidase gene." Funkenstein B., Leary S.L., Stein J.C., Catterall J.F. Mol. Cell. Biol. 8:1160-1168(1988) [PubMed: 2835664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta-glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily." Li H., Takeuchi K.H., Manly K., Chapman V., Swank R.T. J. Biol. Chem. 265:14732-14735(1990) [PubMed: 2394691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 593-648, VARIANT ARG-642, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03047 mRNA. Translation: AAA37696.1. J02836 Genomic DNA. Translation: AAA98623.1. M63836 mRNA. Translation: AAA63309.1. M28540 mRNA. Translation: AAA63307.1. M28541 mRNA. Translation: AAA63308.1. M19279 mRNA. Translation: AAA37697.1.
IPI	IPI00309230.
PIR	A32576.
RefSeq	NP_034498.1.
UniGene	Mm.3317
3D structure databases
HSSP	HSSP built from PDB template 1BHG based on UniProtKB P08236.
SMR	P12265. Positions 22-628.
ModBase	Search...
Protein-protein interaction databases
STRING	P12265.
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Proteomic databases
PRIDE	P12265.
Genome annotation databases
Ensembl	ENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534; Mus musculus. [Genome view]
GeneID	110006.
KEGG	mmu:110006.
Organism-specific databases
CTD	110006.
MGI	MGI:95872. Gusb.
Phylogenomic databases
HOGENOM	P12265.
HOVERGEN	P12265.
Enzyme and pathway databases
BRENDA	3.2.1.31. 244.
Gene expression databases
ArrayExpress	P12265.
Bgee	P12265.
CleanEx	MM_GUSB.
Genevestigator	P12265.
GermOnline	ENSMUSG00000025534. Mus musculus.
Family and domain databases
InterPro	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. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00703. Glyco_hydro_2. 1 hit. PF02836. Glyco_hydro_2_C. 1 hit. PF02837. Glyco_hydro_2_N. 1 hit. [Graphical view]
PRINTS	PR00132. GLHYDRLASE2.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	363145.
SOURCE	Search...

Entry information

Entry name

BGLR_MOUSE

Accession

Primary (citable) accession number: P12265
Secondary accession number(s): Q61601, Q64473, Q64474

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	October 13, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)