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P12265

- BGLR_MOUSE

UniProt

P12265 - BGLR_MOUSE

Protein

Beta-glucuronidase

Gene

Gusb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: MGI

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_196554. Hyaluronan uptake and degradation.
    REACT_198967. HS-GAG 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: 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

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. lysosome Source: MGI

    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

    ArrayExpressiP12265.
    CleanExiMM_GUSB.
    GenevestigatoriP12265.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP12265. 2 interactions.
    MINTiMINT-4089235.

    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.
    OMAiNAHLWWP.
    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

    MSLKWSACWV ALGQLLCSCA LALKGGMLFP KESPSRELKA LDGLWHFRAD    50
    LSNNRLQGFE QQWYRQPLRE SGPVLDMPVP SSFNDITQEA ALRDFIGWVW 100
    YEREAILPRR WTQDTDMRVV LRINSAHYYA VVWVNGIHVV EHEGGHLPFE 150
    ADISKLVQSG PLTTCRITIA INNTLTPHTL PPGTIVYKTD TSMYPKGYFV 200
    QDTSFDFFNY AGLHRSVVLY TTPTTYIDDI TVITNVEQDI GLVTYWISVQ 250
    GSEHFQLEVQ LLDEGGKVVA HGTGNQGQLQ VPSANLWWPY LMHEHPAYMY 300
    SLEVKVTTTE SVTDYYTLPI GIRTVAVTKS KFLINGKPFY FQGVNKHEDS 350
    DIRGKGFDWP LLVKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI 400
    DECPGVGIVL PQSFGNESLR HHLEVMEELV RRDKNHPAVV MWSVANEPSS 450
    ALKPAAYYFK TLITHTKALD LTRPVTFVSN AKYDADLGAP YVDVICVNSY 500
    FSWYHDYGHL EVIQPQLNSQ FENWYKTHQK PIIQSEYGAD AIPGIHEDPP 550
    RMFSEEYQKA VLENYHSVLD QKRKEYVVGE LIWNFADFMT NQSPLRVIGN 600
    KKGIFTRQRQ PKTSAFILRE RYWRIANETG GHGSGPRTQC FGSRPFTF 648
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS19705.1.
    PIRi A32576.
    RefSeqi NP_034498.1. NM_010368.1.
    UniGenei Mm.3317.

    3D structure databases

    ProteinModelPortali P12265.
    SMRi P12265. Positions 22-628.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P12265. 2 interactions.
    MINTi MINT-4089235.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    PTM databases

    PhosphoSitei P12265.

    Proteomic databases

    PaxDbi P12265.
    PRIDEi P12265.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026613 ; ENSMUSP00000026613 ; ENSMUSG00000025534 .
    GeneIDi 110006.
    KEGGi mmu:110006.
    UCSCi uc008ztt.1. mouse.

    Organism-specific databases

    CTDi 2990.
    MGIi MGI:95872. Gusb.

    Phylogenomic databases

    eggNOGi COG3250.
    GeneTreei ENSGT00390000001752.
    HOGENOMi HOG000120896.
    HOVERGENi HBG004843.
    InParanoidi P12265.
    KOi K01195.
    OMAi NAHLWWP.
    OrthoDBi EOG7288QR.
    TreeFami TF300685.

    Enzyme and pathway databases

    Reactomei REACT_196554. Hyaluronan uptake and degradation.
    REACT_198967. HS-GAG degradation.

    Miscellaneous databases

    ChiTaRSi GUSB. mouse.
    NextBioi 363145.
    PROi P12265.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12265.
    CleanExi MM_GUSB.
    Genevestigatori P12265.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    InterProi 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 ]
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00132. GLHYDRLASE2.
    SUPFAMi SSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 135 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