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Protein

Beta-glucuronidase

Gene

Gusb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by L-aspartic acid.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei447 – 4471Proton donorBy similarity

GO - Molecular functioni

  1. beta-glucuronidase activity Source: RGD
  2. carbohydrate binding Source: RGD

GO - Biological processi

  1. carbohydrate metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

SABIO-RKP06760.

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
Synonyms:Gus
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2772. Gusb.

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 648626Beta-glucuronidasePRO_0000012163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP06760.
PRIDEiP06760.

PTM databases

PhosphoSiteiP06760.

Expressioni

Gene expression databases

GenevestigatoriP06760.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP06760. 1 interaction.
STRINGi10116.ENSRNOP00000045033.

Structurei

3D structure databases

ProteinModelPortaliP06760.
SMRiP06760. Positions 22-628.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP06760.
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.
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]
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.

P06760-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPRRSVCWF VLGQLLCSCA VALQGGMLFP KETPSRELKV LDGLWSFRAD
60 70 80 90 100
YSNNRLQGFE KQWYRQPLRE SGPTLDMPVP SSFNDITQEA ELRNFIGWVW
110 120 130 140 150
YEREAVLPQR WTQDTDRRVV LRINSAHYYA VVWVNGIHVV EHEGGHLPFE
160 170 180 190 200
ADITKLVQSG PLTTFRVTIA INNTLTPYTL PPGTIVYKTD PSMYPKGYFV
210 220 230 240 250
QDISFDFFNY AGLHRSVVLY TTPTTYIDDI TVTTDVDRDV GLVNYWISVQ
260 270 280 290 300
GSDHFQLEVR LLDEDGKIVA RGTGNEGQLK VPRAHLWWPY LMHEHPAYLY
310 320 330 340 350
SLEVTMTTPE SVSDFYTLPV GIRTVAVTKS KFLINGKPFY FQGVNKHEDS
360 370 380 390 400
DIRGRGFDWP LLIKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI
410 420 430 440 450
DECPGVGIVL PQSFGNVSLR HHLEVMDELV RRDKNHPAVV MWSVANEPVS
460 470 480 490 500
SLKPAGYYFK TLIAHTKALD PTRPVTFVSN TRYDADMGAP YVDVICVNSY
510 520 530 540 550
LSWYHDYGHL EVIQLQLTSQ FENWYKMYQK PIIQSEYGAD AVSGLHEDPP
560 570 580 590 600
RMFSEEYQTA LLENYHLILD EKRKEYVIGE LIWNFADFMT NQSPLRVTGN
610 620 630 640
KKGIFTRQRN PKMAAFILRE RYWRIANETR GYGSVPRTQC MGSRPFTF
Length:648
Mass (Da):74,793
Last modified:January 1, 1988 - v1
Checksum:i5ADE8F5234F0907E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Q → E in CAA68705. (PubMed:3355537)Curated
Sequence conflicti21 – 211V → L in CAA68705. (PubMed:3355537)Curated
Sequence conflicti487 – 4871M → L in CAA68705. (PubMed:3355537)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13962 mRNA. Translation: AAA41228.1.
Y00717 mRNA. Translation: CAA68705.1.
PIRiA25047.
RefSeqiNP_058711.2. NM_017015.2.
UniGeneiRn.3692.

Genome annotation databases

GeneIDi24434.
KEGGirno:24434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13962 mRNA. Translation: AAA41228.1.
Y00717 mRNA. Translation: CAA68705.1.
PIRiA25047.
RefSeqiNP_058711.2. NM_017015.2.
UniGeneiRn.3692.

3D structure databases

ProteinModelPortaliP06760.
SMRiP06760. Positions 22-628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06760. 1 interaction.
STRINGi10116.ENSRNOP00000045033.

Chemistry

BindingDBiP06760.
ChEMBLiCHEMBL4814.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

PTM databases

PhosphoSiteiP06760.

Proteomic databases

PaxDbiP06760.
PRIDEiP06760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24434.
KEGGirno:24434.

Organism-specific databases

CTDi2990.
RGDi2772. Gusb.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP06760.
KOiK01195.

Enzyme and pathway databases

SABIO-RKP06760.

Miscellaneous databases

NextBioi603309.

Gene expression databases

GenevestigatoriP06760.

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.
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]
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...

Publicationsi

  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.

Entry informationi

Entry nameiBGLR_RAT
AccessioniPrimary (citable) accession number: P06760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 4, 2015
This is version 116 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

External Data

Dasty 3

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 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.