Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-glucuronidase

Gene

GUSB

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by L-aspartic acid.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei450Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucuronidase (EC:3.2.1.31)
Gene namesi
Name:GUSB
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Defects in GUSB are the cause of mucopolysaccharidosis type VII (MPS VII), an inherited disease reported in humans, mice, cats, and dogs.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000001215823 – 651Beta-glucuronidaseAdd BLAST629

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi172N-linked (GlcNAc...)Sequence analysis1
Glycosylationi419N-linked (GlcNAc...)Sequence analysis1
Glycosylationi630N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO18835.
PRIDEiO18835.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014967.

Structurei

3D structure databases

ProteinModelPortaliO18835.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2024. Eukaryota.
COG3250. LUCA.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiO18835.
KOiK01195.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O18835-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGPAGAWV ALGPLLWTCG LALEGGMLYP RESPSRERKD LDGLWSFRAD
60 70 80 90 100
FSDGRRQGFE QQWYRAPLRE SGPTLDMPVP SSFNDVGQDR QLRSFVGWVW
110 120 130 140 150
YEREATLPRR WSQDPGTRVV LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE
160 170 180 190 200
ADISKLVQSG PLSSCRITLA INNTLTPHTL PPGTIVYKTD ASKYPKGYFV
210 220 230 240 250
QNTYFDFFNY AGLHRPVLLY TTPTTYIDDI TVTTGVDQDT GLVDYQIFVQ
260 270 280 290 300
GSEHFQLEVY LLDEEGKVVA QGTGSQGRLQ VPNVHLWWPY LMHEHPAYLY
310 320 330 340 350
SLEVRLTAQM AAGPVSDFYT LPVGIRTVAV TERQFLINGK PFYFHGVNKH
360 370 380 390 400
EDADIRGKGF DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMQLCDRYGI
410 420 430 440 450
VVIDESPGVG IMLVQSYSNV SLQHHLEVMG ELVRRDKNHP SVVMWSVANE
460 470 480 490 500
PTSFLKPAAY YFKTLIAHTK ALDPSRPVTF VTNSNYEADL GAPYVDVICV
510 520 530 540 550
NSYYSWYHDY GHMEVIQLQL ATEFENWYRT YQKPIIQSEY GAETIAGFHQ
560 570 580 590 600
DPPLMFSEEY QKGLLEQYHL VLDQKRKEYV VGELIWNFAD FMTDQSPQRA
610 620 630 640 650
VGNRKGIFTR QRQPKAAAFL LRERYWKLAN ETGHHRSAAK SQCLENSPFA

L
Length:651
Mass (Da):74,433
Last modified:January 1, 1998 - v1
Checksum:iE8991B1E65C60120
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti166R → H in MPS VII; loss of activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019759 mRNA. Translation: AAC48809.1.
RefSeqiNP_001003191.1. NM_001003191.1.
UniGeneiCfa.3694.

Genome annotation databases

GeneIDi403831.
KEGGicfa:403831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019759 mRNA. Translation: AAC48809.1.
RefSeqiNP_001003191.1. NM_001003191.1.
UniGeneiCfa.3694.

3D structure databases

ProteinModelPortaliO18835.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014967.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PaxDbiO18835.
PRIDEiO18835.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403831.
KEGGicfa:403831.

Organism-specific databases

CTDi2990.

Phylogenomic databases

eggNOGiKOG2024. Eukaryota.
COG3250. LUCA.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiO18835.
KOiK01195.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBGLR_CANLF
AccessioniPrimary (citable) accession number: O18835
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.