P12265 (BGLR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucuronidase
EC=3.2.1.31

Gene names

Name:	Gusb
Synonyms:	Gus, Gus-s

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from direct assay PubMed 4841576. Source: MGI
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 4841576. Source: MGI
Molecular_function	beta-glucuronidase activity Inferred from direct assay PubMed 1914521PubMed 4777306PubMed 4841576PubMed 7203014. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22
	Chain	23 – 648	626	Beta-glucuronidase		PRO_0000012162
Sites
	Active site	447	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Glycosylation	416	1	N-linked (GlcNAc...) Potential
	Glycosylation	591	1	N-linked (GlcNAc...) Potential
	Glycosylation	627	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	87	1	T → I in strain: C3H/HeJ.
	Natural variant	233	1	I → T in allele GUS-SA.
	Natural variant	428	1	E → K in allele GUS-SA.
	Natural variant	616	1	F → L in allele GUS-SA.
	Natural variant	642	1	G → R in allele W26; reduced retention in the endoplasmic reticulum. Ref.10
Experimental info
	Sequence conflict	265	1	G → D in AAA37696. Ref.2
	Sequence conflict	265	1	G → D in AAA98623. Ref.3
	Sequence conflict	265	1	G → D in AAA63309. Ref.4
	Sequence conflict	265	1	G → D in AAA37697. Ref.5
	Sequence conflict	320	1	I → V in AAA37696. Ref.2
	Sequence conflict	320	1	I → V in AAA98623. Ref.3
	Sequence conflict	320	1	I → V in AAA37697. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P12265 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: CCD8F84C3CD6C498	FASTA	648	74,195
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00309230.
PIR	A32576.
RefSeq	NP_034498.1. NM_010368.1.
UniGene	Mm.3317.
3D structure databases
ProteinModelPortal	P12265.
SMR	P12265. Positions 22-628.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
PTM databases
PhosphoSite	P12265.
Proteomic databases
PaxDb	P12265.
PRIDE	P12265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026613; ENSMUSP00000026613; ENSMUSG00000025534.
GeneID	110006.
KEGG	mmu:110006.
Organism-specific databases
CTD	2990.
MGI	MGI:95872. Gusb.
Phylogenomic databases
eggNOG	COG3250.
GeneTree	ENSGT00390000001752.
HOGENOM	HOG000120896.
HOVERGEN	HBG004843.
InParanoid	P12265.
KO	K01195.
OMA	GHMEVIQ.
OrthoDB	EOG4X97GN.
Gene expression databases
CleanEx	MM_GUSB.
Genevestigator	P12265.
GermOnline	ENSMUSG00000025534. Mus musculus.
Family and domain databases
Gene3D	2.60.40.320. 1 hit. 3.20.20.80. 1 hit.
InterPro	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]
Pfam	PF00703. Glyco_hydro_2. 1 hit. PF02836. Glyco_hydro_2_C. 1 hit. PF02837. Glyco_hydro_2_N. 1 hit. [Graphical view]
PRINTS	PR00132. GLHYDRLASE2.
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GUSB. mouse.
NextBio	363145.
SOURCE	Search...

Entry information

Entry name

BGLR_MOUSE

Accession

Primary (citable) accession number: P12265
Secondary accession number(s): Q61601 , Q64473, Q64474, Q6IR10

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program