BGLR_MOUSE
ID BGLR_MOUSE Reviewed; 648 AA.
AC P12265; Q61601; Q64473; Q64474; Q6IR10;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Beta-glucuronidase;
DE EC=3.2.1.31;
DE Flags: Precursor;
GN Name=Gusb; Synonyms=Gus, Gus-s;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2891607; DOI=10.1016/0888-7543(87)90006-1;
RA Gallagher P.M., D'Amore M.A., Lund S.D., Elliott R.W., Pazik J., Hohman C.,
RA Korfhagen T.R., Ganschow R.E.;
RT "DNA sequence variation within the beta-glucuronidase gene complex among
RT inbred strains of mice.";
RL Genomics 1:145-152(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3397060; DOI=10.1016/0888-7543(88)90005-5;
RA Gallagher P.M., D'Amore M.A., Lund S.D., Ganschow R.E.;
RT "The complete nucleotide sequence of murine beta-glucuronidase mRNA and its
RT deduced polypeptide.";
RL Genomics 2:215-219(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3196706; DOI=10.1021/bi00418a070;
RA D'Amore M.A., Gallagher P.M., Korfhagen T.R., Ganschow R.E.;
RT "Complete sequence and organization of the murine beta-glucuronidase
RT gene.";
RL Biochemistry 27:7131-7140(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ, and YBR; TISSUE=Sperm;
RX PubMed=2779578; DOI=10.1128/mcb.9.9.4074-4078.1989;
RA Wawrzyniak C.J., Gallagher P.M., D'Amore M.A., Carter J.E., Lund S.D.,
RA Rinchik E.M., Ganschow R.E.;
RT "DNA determinants of structural and regulatory variation within the murine
RT beta-glucuronidase gene complex.";
RL Mol. Cell. Biol. 9:4074-4078(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2835664; DOI=10.1128/mcb.8.3.1160-1168.1988;
RA Funkenstein B., Leary S.L., Stein J.C., Catterall J.F.;
RT "Genomic organization and sequence of the Gus-s alpha allele of the murine
RT beta-glucuronidase gene.";
RL Mol. Cell. Biol. 8:1160-1168(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE OF 593-648, VARIANT ARG-642, AND SUBCELLULAR LOCATION.
RX PubMed=2394691; DOI=10.1016/s0021-9258(18)77172-x;
RA Li H., Takeuchi K.H., Manly K., Chapman V., Swank R.T.;
RT "The propeptide of beta-glucuronidase. Further evidence of its involvement
RT in compartmentalization of beta-glucuronidase and sequence similarity with
RT portions of the reactive site region of the serpin superfamily.";
RL J. Biol. Chem. 265:14732-14735(1990).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC keratan sulfates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2394691}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:2394691}. Note=A small
CC proportion is found in the endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; J03047; AAA37696.1; -; mRNA.
DR EMBL; J02836; AAA98623.1; -; Genomic_DNA.
DR EMBL; M63836; AAA63309.1; -; mRNA.
DR EMBL; M28540; AAA63307.1; -; mRNA.
DR EMBL; M28541; AAA63308.1; -; mRNA.
DR EMBL; M19279; AAA37697.1; -; mRNA.
DR EMBL; AK136519; BAE23021.1; -; mRNA.
DR EMBL; AK150048; BAE29265.1; -; mRNA.
DR EMBL; AK159526; BAE35155.1; -; mRNA.
DR EMBL; AK162436; BAE36917.1; -; mRNA.
DR EMBL; AC161345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19485.1; -; Genomic_DNA.
DR EMBL; BC071226; AAH71226.1; -; mRNA.
DR CCDS; CCDS19705.1; -.
DR PIR; A32576; A32576.
DR RefSeq; NP_034498.1; NM_010368.1.
DR AlphaFoldDB; P12265; -.
DR SMR; P12265; -.
DR BioGRID; 225218; 20.
DR CORUM; P12265; -.
DR STRING; 10090.ENSMUSP00000026613; -.
DR BindingDB; P12265; -.
DR ChEMBL; CHEMBL4523185; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GlyGen; P12265; 3 sites.
DR iPTMnet; P12265; -.
DR PhosphoSitePlus; P12265; -.
DR SwissPalm; P12265; -.
DR EPD; P12265; -.
DR jPOST; P12265; -.
DR PaxDb; P12265; -.
DR PeptideAtlas; P12265; -.
DR PRIDE; P12265; -.
DR ProteomicsDB; 273451; -.
DR Antibodypedia; 14064; 392 antibodies from 36 providers.
DR DNASU; 110006; -.
DR Ensembl; ENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534.
DR GeneID; 110006; -.
DR KEGG; mmu:110006; -.
DR UCSC; uc008ztt.1; mouse.
DR CTD; 2990; -.
DR MGI; MGI:95872; Gusb.
DR VEuPathDB; HostDB:ENSMUSG00000025534; -.
DR eggNOG; KOG2024; Eukaryota.
DR GeneTree; ENSGT00390000001752; -.
DR HOGENOM; CLU_006501_6_1_1; -.
DR InParanoid; P12265; -.
DR OMA; IHDHVGW; -.
DR OrthoDB; 653343at2759; -.
DR PhylomeDB; P12265; -.
DR TreeFam; TF300685; -.
DR BRENDA; 3.2.1.31; 3474.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 110006; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Gusb; mouse.
DR PRO; PR:P12265; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P12265; protein.
DR Bgee; ENSMUSG00000025534; Expressed in stroma of bone marrow and 255 other tissues.
DR ExpressionAtlas; P12265; baseline and differential.
DR Genevisible; P12265; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0004566; F:beta-glucuronidase activity; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:MGI.
DR GO; GO:0019391; P:glucuronoside catabolic process; IDA:MGI.
DR GO; GO:0030214; P:hyaluronan catabolic process; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF49303; SSF49303; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT CHAIN 23..648
FT /note="Beta-glucuronidase"
FT /id="PRO_0000012162"
FT ACT_SITE 447
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 87
FT /note="T -> I (in strain: C3H/HeJ)"
FT VARIANT 233
FT /note="I -> T (in allele GUS-SA)"
FT VARIANT 428
FT /note="E -> K (in allele GUS-SA)"
FT VARIANT 616
FT /note="F -> L (in allele GUS-SA)"
FT VARIANT 642
FT /note="G -> R (in allele W26; reduced retention in the
FT endoplasmic reticulum)"
FT /evidence="ECO:0000269|PubMed:2394691"
FT CONFLICT 265
FT /note="G -> D (in Ref. 2; AAA37696, 3; AAA98623, 4;
FT AAA63309 and 5; AAA37697)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="I -> V (in Ref. 2; AAA37696, 3; AAA98623 and 5;
FT AAA37697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 74195 MW; CCD8F84C3CD6C498 CRC64;
MSLKWSACWV ALGQLLCSCA LALKGGMLFP KESPSRELKA LDGLWHFRAD LSNNRLQGFE
QQWYRQPLRE SGPVLDMPVP SSFNDITQEA ALRDFIGWVW YEREAILPRR WTQDTDMRVV
LRINSAHYYA VVWVNGIHVV EHEGGHLPFE ADISKLVQSG PLTTCRITIA INNTLTPHTL
PPGTIVYKTD TSMYPKGYFV QDTSFDFFNY AGLHRSVVLY TTPTTYIDDI TVITNVEQDI
GLVTYWISVQ GSEHFQLEVQ LLDEGGKVVA HGTGNQGQLQ VPSANLWWPY LMHEHPAYMY
SLEVKVTTTE SVTDYYTLPI GIRTVAVTKS KFLINGKPFY FQGVNKHEDS DIRGKGFDWP
LLVKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI DECPGVGIVL PQSFGNESLR
HHLEVMEELV RRDKNHPAVV MWSVANEPSS ALKPAAYYFK TLITHTKALD LTRPVTFVSN
AKYDADLGAP YVDVICVNSY FSWYHDYGHL EVIQPQLNSQ FENWYKTHQK PIIQSEYGAD
AIPGIHEDPP RMFSEEYQKA VLENYHSVLD QKRKEYVVGE LIWNFADFMT NQSPLRVIGN
KKGIFTRQRQ PKTSAFILRE RYWRIANETG GHGSGPRTQC FGSRPFTF
