Reviewed, UniProtKB/Swiss-Prot Q69ZF3 (GBA2_MOUSE)

Names and origin

Protein names

Recommended name:
    Non-lysosomal glucosylceramidase
      Short name=NLGase
    EC=3.2.1.45
Alternative name(s):
    Glucosylceramidase 2
    Beta-glucocerebrosidase 2
      Short name=Beta-glucosidase 2

Gene names

Name:	Gba2
Synonyms:	Kiaa1605

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Ref.5
Catalytic activity	D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.
Subcellular location	Cell membrane; Single-pass membrane protein By similarity. Note: Not localized to lipid rafts By similarity.
Tissue specificity	Widely expressed at low level. Highly expressed in testis and brain. Ref.5
Disruption phenotype	Mice have a normal bile acid metabolism but males exhibit impaired fertility due to glucosylceramides accumulation. Ref.5
Sequence similarities	Belongs to the non-lysosomal glucosylceramidase family.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	glucosylceramide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-glucosidase activity Inferred from sequence or structural similarity. Source: UniProtKB glucosylceramidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 918	918	Non-lysosomal glucosylceramidase		PRO_0000283759
Regions
	Topological domain	1 – 678	678	Extracellular Potential
	Transmembrane	679 – 699	21	Potential
	Topological domain	700 – 918	219	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	385	1	V → I in BAC40785. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q69ZF3-1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: EABE7B50B96B0B59	FASTA	918	103,294
	10 20 30 40 50 60 MVTCVPASEQ VGCAERDSQV YCEDTGGTEA VRVTDCGSPE DSGPQDEPSY CNSEDSGQLM 70 80 90 100 110 120 ASYEGKARGY QVPPFGWRIC LAHEFAEKRR PFQANNISLS NLVKHLGMGL RYLKWWYRKT 130 140 150 160 170 180 HVEKKTPFID MLNSLPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ 190 200 210 220 230 240 FIVCLRRDGR TVYQQVLSLE LPNVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT 250 260 270 280 290 300 CRQVTPILPH DYQDSSLPVG VFVWDVENEG DETLDVSITF SMRNGLGGED DAAGSLWNEP 310 320 330 340 350 360 FRLEQGGTTV QGLLLHHPTP PNPYTMAVAA RCTADTTVTH TTAFDPNGTG QQVWQDLLQD 370 380 390 400 410 420 GQLDSPAGQS TPTQKGEGIA GAVCVSSKLL PRSRCCLEFS LAWDMPKIMF GAKSQVHYRR 430 440 450 460 470 480 YTRFFGSDGD VAPALSHYAL CHYADWEDRI SAWQNPVLDD RTLPAWYKSA LFNELYFLAD 490 500 510 520 530 540 GGTVWLEVPA DSLPEGLGGS MRQLRSTLQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM 550 560 570 580 590 600 LWPKLELSLQ YDMALATLKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY 610 620 630 640 650 660 LIHDTADWKD LNLKFVLQIY RDYYLTGDQG FLEDMWPVCL AVMESEMKFD KDQDGLIENG 670 680 690 700 710 720 GYADQTYDAW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQERFASIL CRGREAYERL 730 740 750 760 770 780 LWNGRYYNYD SSSHPQSRSI MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALQTIFELN 790 800 810 820 830 840 VQAFAGGAMG AVNGMHPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY 850 860 870 880 890 900 RTVWERLGLA FQTPEAYCQQ QVFRSLAYMR PLSIWAMQLA LQQQQHKKSR RPSVTQGTGL 910 STQPECGPKR SLANLNSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD.
[3]	"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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility." Yildiz Y., Matern H., Thompson B., Allegood J.C., Warren R.L., Ramirez D.M.O., Hammer R.E., Hamra F.K., Matern S., Russell D.W. J. Clin. Invest. 116:2985-2994(2006) [PubMed: 17080196] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK173213 mRNA. Translation: BAD32491.1. Different initiation. AK089192 mRNA. Translation: BAC40785.1. AL732626 Genomic DNA. Translation: CAM17042.1. BC056935 mRNA. Translation: AAH56935.1.
IPI	IPI00225123.
RefSeq	NP_766280.2.
UniGene	Mm.229444
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q69ZF3.
Proteomic databases
PRIDE	Q69ZF3.
Genome annotation databases
Ensembl	ENSMUST00000030189; ENSMUSP00000030189; ENSMUSG00000028467; Mus musculus. [Genome view]
GeneID	230101.
KEGG	mmu:230101.
UCSC	uc008sqi.1. mouse.
Organism-specific databases
CTD	230101.
MGI	MGI:2654325. Gba2.
Rouge	Search...
Phylogenomic databases
HOVERGEN	Q69ZF3.
OMA	NYTAYQD.
Enzyme and pathway databases
BRENDA	3.2.1.45. 244.
Gene expression databases
ArrayExpress	Q69ZF3.
Bgee	Q69ZF3.
CleanEx	MM_GBA2.
Genevestigator	Q69ZF3.
Family and domain databases
InterPro	IPR014551. Beta_glucosidase_GBA2-type. IPR006775. Glucosylceramidase. [Graphical view]
Pfam	PF04685. DUF608. 1 hit. [Graphical view]
PIRSF	PIRSF028944. Beta_gluc_GBA2. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	379792.
SOURCE	Search...

Entry information

Entry name

GBA2_MOUSE

Accession

Primary (citable) accession number: Q69ZF3
Secondary accession number(s): Q6PGM3, Q8BTN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	November 3, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)