P17439 (GLCM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucosylceramidase
EC=3.2.1.45

Alternative name(s):
Acid beta-glucosidase
Beta-glucocerebrosidase
D-glucosyl-N-acylsphingosine glucohydrolase

Gene names

Name:

Gba

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	515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.
Subunit structure	Interacts with SCARB2 By similarity.
Subcellular location	Lysosome membrane; Peripheral membrane protein. Note: Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 30 family.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Lysosome Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara ceramide biosynthetic process Inferred from electronic annotation. Source: Compara glucosylceramide catabolic process Inferred from electronic annotation. Source: Compara negative regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara negative regulation of interleukin-6 production Inferred from electronic annotation. Source: Compara positive regulation of protein dephosphorylation Inferred from electronic annotation. Source: Compara sphingosine biosynthetic process Inferred from electronic annotation. Source: Compara termination of signal transduction Inferred from electronic annotation. Source: Compara
Cellular_component	lysosomal lumen Inferred from direct assay PubMed 18022370. Source: BHF-UCL lysosomal membrane Inferred from direct assay PubMed 18022370. Source: BHF-UCL
Molecular_function	glucosylceramidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SCARB2	Q14108	1	EBI-1564504,EBI-1564650	From a different organism.
Scarb2	O35114	1	EBI-1564504,EBI-1564519

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	By similarity
	Chain	20 – 515	496	Glucosylceramidase		PRO_0000012178
Sites
	Active site	254	1	Proton donor By similarity
	Active site	358	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Glycosylation	165	1	N-linked (GlcNAc...) (high mannose) Ref.7
	Glycosylation	289	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	480	1	N-linked (GlcNAc...) Potential
	Disulfide bond	23 ↔ 35		By similarity
	Disulfide bond	37 ↔ 42		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17439 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 7CCD9176085FE2CB	FASTA	515	57,622
	10 20 30 40 50 60 MAARLIGFFL FQAVSWAYGA QPCIPKSFGY SSVVCVCNAS YCDSLDPVTL PALGTFSRYE 70 80 90 100 110 120 STRRGRRMEL SVGAIQANRT GTGLLLTLQP EKKFQKVKGF GGAMTDATAL NILALSPPTQ 130 140 150 160 170 180 KLLLRSYFST NGIEYNIIRV PMASCDFSIR VYTYADTPND FQLSNFSLPE EDTKLKIPLI 190 200 210 220 230 240 HQALKMSSRP ISLFASPWTS PTWLKTNGRV NGKGSLKGQP GDIFHQTWAN YFVKFLDAYA 250 260 270 280 290 300 KYGLRFWAVT AENEPTAGLF TGYPFQCLGF TPEHQRDFIS RDLGPALANS SHDVKLLMLD 310 320 330 340 350 360 DQRLLLPRWA EVVLSDPEAA KYVHGIAVHW YMDFLAPAKA TLGETHRLFP NTMLFASEAC 370 380 390 400 410 420 VGSKFWEQSV RLGSWDRGMQ YSHSIITNLL YHVTGWTDWN LALNPEGGPN WVRNFVDSPI 430 440 450 460 470 480 IVDIPKDAFY KQPMFYHLGH FSKFIPEGSQ RVALVASEST DLETVALLRP DGSAVVVVLN 490 500 510 RSSEDVPLTI SDPDLGFLET VSPGYSIHTY LWRRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the chromosomal localization of murine and human glucocerebrosidase genes and of the deduced amino acid sequences." O'Neill R.R., Tokoru T., Kozak C.A., Brady R.O. Proc. Natl. Acad. Sci. U.S.A. 86:5049-5053(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Comparative sequence analysis of the mouse and human GBA locus." Sinclair G., Wilson M.D., McKinnel L., Koop B.F., Choy F.Y.M. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"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.
[4]	"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: FVB/N. Tissue: Mammary gland.
[5]	"Molecular and functional characterization of the murine glucocerebrosidase gene." Carstea E.D., Murray G.J., O'Neill R.R. Biochem. Biophys. Res. Commun. 184:1477-1483(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18. Strain: BALB/c.
[6]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 210-217, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[7]	"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis." Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S. Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-165, MASS SPECTROMETRY. Tissue: Epidermis.
[8]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-289, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24119 mRNA. Translation: AAA37671.1. AY115108 Genomic DNA. Translation: AAM66757.1. AK082767 mRNA. Translation: BAC38609.1. BC006663 mRNA. Translation: AAH06663.1. M89949 Genomic DNA. Translation: AAA37665.1.
IPI	IPI00108811.
PIR	A32931.
RefSeq	NP_001070879.1. NM_001077411.1. NP_032120.1. NM_008094.4.
UniGene	Mm.5031.
3D structure databases
ProteinModelPortal	P17439.
SMR	P17439. Positions 20-515.
ModBase	Search...
Protein-protein interaction databases
IntAct	P17439. 3 interactions.
MINT	MINT-4096112.
STRING	10090.ENSMUSP00000076589.
Protein family/group databases
CAZy	GH30. Glycoside Hydrolase Family 30.
PTM databases
PhosphoSite	P17439.
Proteomic databases
PaxDb	P17439.
PRIDE	P17439.
Protocols and materials databases
DNASU	14466.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000077367; ENSMUSP00000076589; ENSMUSG00000028048. ENSMUST00000167998; ENSMUSP00000130660; ENSMUSG00000028048.
GeneID	14466.
KEGG	mmu:14466.
UCSC	uc008pyb.1. mouse.
Organism-specific databases
CTD	2629.
MGI	MGI:95665. Gba.
Phylogenomic databases
eggNOG	COG5520.
GeneTree	ENSGT00390000009464.
HOGENOM	HOG000270031.
HOVERGEN	HBG002285.
InParanoid	P17439.
KO	K01201.
OMA	HRLFPNT.
OrthoDB	EOG43XV3S.
Gene expression databases
Bgee	P17439.
CleanEx	MM_GBA.
Genevestigator	P17439.
GermOnline	ENSMUSG00000028048. Mus musculus.
Family and domain databases
Gene3D	2.60.40.1180. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR013780. Glyco_hydro_13_b. IPR001139. Glyco_hydro_30. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR11069. PTHR11069. 1 hit.
Pfam	PF02055. Glyco_hydro_30. 1 hit. [Graphical view]
PRINTS	PR00843. GLHYDRLASE30.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
BindingDB	P17439.
ChEMBL	CHEMBL2278.
NextBio	286116.
SOURCE	Search...

Entry information

Entry name

GLCM_MOUSE

Accession

Primary (citable) accession number: P17439
Secondary accession number(s): Q78NR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program