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Protein

Beta-glucuronidase

Gene

Gusb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

  • carbohydrate metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_343711. HS-GAG degradation.
REACT_353590. Hyaluronan uptake and degradation.

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, Gus-s
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:95872. Gusb.

Subcellular locationi

  • Lysosome 1 Publication
  • Endoplasmic reticulum 1 Publication

  • Note: A small proportion is found in the endoplasmic reticulum.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 648626Beta-glucuronidasePRO_0000012162Add
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

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP12265.
PRIDEiP12265.

PTM databases

PhosphoSiteiP12265.

Expressioni

Gene expression databases

CleanExiMM_GUSB.
ExpressionAtlasiP12265. baseline and differential.
GenevisibleiP12265. MM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP12265. 2 interactions.
MINTiMINT-4089235.
STRINGi10090.ENSMUSP00000026613.

Structurei

3D structure databases

ProteinModelPortaliP12265.
SMRiP12265. Positions 22-628.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3250.
GeneTreeiENSGT00390000001752.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP12265.
KOiK01195.
OMAiRHEDYPI.
OrthoDBiEOG7288QR.
TreeFamiTF300685.

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.

P12265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKWSACWV ALGQLLCSCA LALKGGMLFP KESPSRELKA LDGLWHFRAD
60 70 80 90 100
LSNNRLQGFE QQWYRQPLRE SGPVLDMPVP SSFNDITQEA ALRDFIGWVW
110 120 130 140 150
YEREAILPRR WTQDTDMRVV LRINSAHYYA VVWVNGIHVV EHEGGHLPFE
160 170 180 190 200
ADISKLVQSG PLTTCRITIA INNTLTPHTL PPGTIVYKTD TSMYPKGYFV
210 220 230 240 250
QDTSFDFFNY AGLHRSVVLY TTPTTYIDDI TVITNVEQDI GLVTYWISVQ
260 270 280 290 300
GSEHFQLEVQ LLDEGGKVVA HGTGNQGQLQ VPSANLWWPY LMHEHPAYMY
310 320 330 340 350
SLEVKVTTTE SVTDYYTLPI GIRTVAVTKS KFLINGKPFY FQGVNKHEDS
360 370 380 390 400
DIRGKGFDWP LLVKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI
410 420 430 440 450
DECPGVGIVL PQSFGNESLR HHLEVMEELV RRDKNHPAVV MWSVANEPSS
460 470 480 490 500
ALKPAAYYFK TLITHTKALD LTRPVTFVSN AKYDADLGAP YVDVICVNSY
510 520 530 540 550
FSWYHDYGHL EVIQPQLNSQ FENWYKTHQK PIIQSEYGAD AIPGIHEDPP
560 570 580 590 600
RMFSEEYQKA VLENYHSVLD QKRKEYVVGE LIWNFADFMT NQSPLRVIGN
610 620 630 640
KKGIFTRQRQ PKTSAFILRE RYWRIANETG GHGSGPRTQC FGSRPFTF
Length:648
Mass (Da):74,195
Last modified:October 3, 2012 - v2
Checksum:iCCD8F84C3CD6C498
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 2651G → D in AAA37696 (PubMed:3397060).Curated
Sequence conflicti265 – 2651G → D in AAA98623 (PubMed:3196706).Curated
Sequence conflicti265 – 2651G → D in AAA63309 (PubMed:2779578).Curated
Sequence conflicti265 – 2651G → D in AAA37697 (PubMed:2835664).Curated
Sequence conflicti320 – 3201I → V in AAA37696 (PubMed:3397060).Curated
Sequence conflicti320 – 3201I → V in AAA98623 (PubMed:3196706).Curated
Sequence conflicti320 – 3201I → V in AAA37697 (PubMed:2835664).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871T → I in strain: C3H/HeJ.
Natural varianti233 – 2331I → T in allele GUS-SA.
Natural varianti428 – 4281E → K in allele GUS-SA.
Natural varianti616 – 6161F → L in allele GUS-SA.
Natural varianti642 – 6421G → R in allele W26; reduced retention in the endoplasmic reticulum. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK136519 mRNA. Translation: BAE23021.1.
AK150048 mRNA. Translation: BAE29265.1.
AK159526 mRNA. Translation: BAE35155.1.
AK162436 mRNA. Translation: BAE36917.1.
AC161345 Genomic DNA. No translation available.
CH466529 Genomic DNA. Translation: EDL19485.1.
BC071226 mRNA. Translation: AAH71226.1.
CCDSiCCDS19705.1.
PIRiA32576.
RefSeqiNP_034498.1. NM_010368.1.
UniGeneiMm.3317.

Genome annotation databases

EnsembliENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534.
GeneIDi110006.
KEGGimmu:110006.
UCSCiuc008ztt.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK136519 mRNA. Translation: BAE23021.1.
AK150048 mRNA. Translation: BAE29265.1.
AK159526 mRNA. Translation: BAE35155.1.
AK162436 mRNA. Translation: BAE36917.1.
AC161345 Genomic DNA. No translation available.
CH466529 Genomic DNA. Translation: EDL19485.1.
BC071226 mRNA. Translation: AAH71226.1.
CCDSiCCDS19705.1.
PIRiA32576.
RefSeqiNP_034498.1. NM_010368.1.
UniGeneiMm.3317.

3D structure databases

ProteinModelPortaliP12265.
SMRiP12265. Positions 22-628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12265. 2 interactions.
MINTiMINT-4089235.
STRINGi10090.ENSMUSP00000026613.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

PTM databases

PhosphoSiteiP12265.

Proteomic databases

PaxDbiP12265.
PRIDEiP12265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534.
GeneIDi110006.
KEGGimmu:110006.
UCSCiuc008ztt.1. mouse.

Organism-specific databases

CTDi2990.
MGIiMGI:95872. Gusb.

Phylogenomic databases

eggNOGiCOG3250.
GeneTreeiENSGT00390000001752.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP12265.
KOiK01195.
OMAiRHEDYPI.
OrthoDBiEOG7288QR.
TreeFamiTF300685.

Enzyme and pathway databases

ReactomeiREACT_343711. HS-GAG degradation.
REACT_353590. Hyaluronan uptake and degradation.

Miscellaneous databases

ChiTaRSiGusb. mouse.
NextBioi363145.
PROiP12265.
SOURCEiSearch...

Gene expression databases

CleanExiMM_GUSB.
ExpressionAtlasiP12265. baseline and differential.
GenevisibleiP12265. MM.

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

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Cecum.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  8. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Mammary tumor.
  10. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 593-648, VARIANT ARG-642, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiBGLR_MOUSE
AccessioniPrimary (citable) accession number: P12265
Secondary accession number(s): Q61601
, Q64473, Q64474, Q6IR10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 3, 2012
Last modified: June 24, 2015
This is version 143 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.