O18835 (BGLR_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucuronidase
EC=3.2.1.31

Gene names

Name:

GUSB

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	651 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Disease	Disease mutation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-glucuronidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 651	629	Beta-glucuronidase		PRO_0000012158
Sites
	Active site	450	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Glycosylation	419	1	N-linked (GlcNAc...) Potential
	Glycosylation	630	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	166	1	R → H in MPS VII; loss of activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O18835 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E8991B1E65C60120	FASTA	651	74,433
	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

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019759 mRNA. Translation: AAC48809.1.
RefSeq	NP_001003191.1. NM_001003191.1.
UniGene	Cfa.3694.
3D structure databases
ProteinModelPortal	O18835.
SMR	O18835. Positions 22-631.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000031474.
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Proteomic databases
PaxDb	O18835.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403831.
KEGG	cfa:403831.
Organism-specific databases
CTD	2990.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000120896.
HOVERGEN	HBG004843.
KO	K01195.
Family and domain databases
Gene3D	2.60.40.320. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR008979. 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]
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.
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20817327.

Entry information

Entry name

BGLR_CANFA

Accession

Primary (citable) accession number: O18835

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program