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Reviewed, UniProtKB/Swiss-Prot Q69ZF3 (GBA2_MOUSE)

Last modified November 3, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Non-lysosomal glucosylceramidase
PRO_0000283759

Regions

Topological domain1 – 678678Extracellular Potential
Transmembrane679 – 69921 Potential
Topological domain700 – 918219Cytoplasmic Potential

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3851V → I in BAC40785. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q69ZF3-1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: EABE7B50B96B0B59

FASTA918103,294
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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

AK173213 mRNA. Translation: BAD32491.1. Different initiation.
AK089192 mRNA. Translation: BAC40785.1.
AL732626 Genomic DNA. Translation: CAM17042.1.
BC056935 mRNA. Translation: AAH56935.1.
IPIIPI00225123.
RefSeqNP_766280.2.
UniGeneMm.229444

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ69ZF3.

Proteomic databases

PRIDEQ69ZF3.

Genome annotation databases

EnsemblENSMUST00000030189; ENSMUSP00000030189; ENSMUSG00000028467; Mus musculus. [Genome view]
GeneID230101.
KEGGmmu:230101.
UCSCuc008sqi.1. mouse.

Organism-specific databases

CTD230101.
MGIMGI:2654325. Gba2.
RougeSearch...

Phylogenomic databases

HOVERGENQ69ZF3.
OMANYTAYQD.

Enzyme and pathway databases

BRENDA3.2.1.45. 244.

Gene expression databases

ArrayExpressQ69ZF3.
BgeeQ69ZF3.
CleanExMM_GBA2.
GenevestigatorQ69ZF3.

Family and domain databases

InterProIPR014551. Beta_glucosidase_GBA2-type.
IPR006775. Glucosylceramidase.
[Graphical view]
PfamPF04685. DUF608. 1 hit.
[Graphical view]
PIRSFPIRSF028944. Beta_gluc_GBA2. 1 hit.
ProtoNetSearch...

Other Resources

NextBio379792.
SOURCESearch...

Entry information

Entry nameGBA2_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents