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P12265 (BGLR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucuronidase

EC=3.2.1.31
Gene names
Name:Gusb
Synonyms:Gus, Gus-s
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.10

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Lysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from direct assay PubMed 4841576. Source: MGI

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from direct assay PubMed 4841576. Source: MGI

   Molecular_functionbeta-glucuronidase activity

Inferred from direct assay PubMed 1914521PubMed 4777306PubMed 4841576PubMed 7203014. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 648626Beta-glucuronidase
PRO_0000012162

Sites

Active site4471Proton donor By similarity

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential

Natural variations

Natural variant871T → I in strain: C3H/HeJ.
Natural variant2331I → T in allele GUS-SA.
Natural variant4281E → K in allele GUS-SA.
Natural variant6161F → L in allele GUS-SA.
Natural variant6421G → R in allele W26; reduced retention in the endoplasmic reticulum. Ref.10

Experimental info

Sequence conflict2651G → D in AAA37696. Ref.2
Sequence conflict2651G → D in AAA98623. Ref.3
Sequence conflict2651G → D in AAA63309. Ref.4
Sequence conflict2651G → D in AAA37697. Ref.5
Sequence conflict3201I → V in AAA37696. Ref.2
Sequence conflict3201I → V in AAA98623. Ref.3
Sequence conflict3201I → V in AAA37697. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P12265 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: CCD8F84C3CD6C498

FASTA64874,195
        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 LLDEGGKVVA HGTGNQGQLQ VPSANLWWPY LMHEHPAYMY 

       310        320        330        340        350        360 
SLEVKVTTTE SVTDYYTLPI 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 

« Hide

References

« Hide 'large scale' 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] [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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19705.1.
PIRA32576.
RefSeqNP_034498.1. NM_010368.1.
UniGeneMm.3317.

3D structure databases

ProteinModelPortalP12265.
SMRP12265. Positions 22-628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP12265. 2 interactions.
MINTMINT-4089235.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

PTM databases

PhosphoSiteP12265.

Proteomic databases

PaxDbP12265.
PRIDEP12265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534.
GeneID110006.
KEGGmmu:110006.
UCSCuc008ztt.1. mouse.

Organism-specific databases

CTD2990.
MGIMGI:95872. Gusb.

Phylogenomic databases

eggNOGCOG3250.
GeneTreeENSGT00390000001752.
HOGENOMHOG000120896.
HOVERGENHBG004843.
InParanoidP12265.
KOK01195.
OMANAHLWWP.
OrthoDBEOG7288QR.
TreeFamTF300685.

Gene expression databases

ArrayExpressP12265.
CleanExMM_GUSB.
GenevestigatorP12265.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008979. 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]
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
SUPFAMSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGUSB. mouse.
NextBio363145.
PROP12265.
SOURCESearch...

Entry information

Entry nameBGLR_MOUSE
AccessionPrimary (citable) accession number: P12265
Secondary accession number(s): Q61601 expand/collapse secondary AC list , Q64473, Q64474, Q6IR10
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries