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Q69ZF3 (GBA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-lysosomal glucosylceramidase

Short name=NLGase
EC=3.2.1.45
Alternative name(s):
Beta-glucocerebrosidase 2
Short name=Beta-glucosidase 2
Glucosylceramidase 2
Gene names
Name:Gba2
Synonyms:Kiaa1605
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) 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. Plays a role in central nevous system development By similarity. Required for proper formation of motor neuron axons By similarity. Ref.5

Catalytic activity

D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine. Ref.6

Enzyme regulation

Enzymatic activity is dependent on membrane association and requires the presence of lipids. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Not localized to lipid rafts By similarity. Ref.6

Tissue specificity

Widely expressed at low level. Highly expressed in testis and brain. Ref.5 Ref.6

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.

Sequence caution

The sequence BAD32491.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Non-lysosomal glucosylceramidase
PRO_0000283759

Experimental info

Sequence conflict3851V → I in BAC40785. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q69ZF3 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[6]"The non-lysosomal beta-glucosidase GBA2 is a non-integral membrane-associated protein at the endoplasmic reticulum (ER) and Golgi."
Korschen H.G., Yildiz Y., Raju D.N., Schonauer S., Bonigk W., Jansen V., Kremmer E., Kaupp U.B., Wachten D.
J. Biol. Chem. 288:3381-3393(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK173213 mRNA. Translation: BAD32491.1. Different initiation.
AK089192 mRNA. Translation: BAC40785.1.
AL732626 Genomic DNA. Translation: CAM17042.1.
BC056935 mRNA. Translation: AAH56935.1.
CCDSCCDS18103.1.
RefSeqNP_766280.2. NM_172692.3.
UniGeneMm.229444.

3D structure databases

ProteinModelPortalQ69ZF3.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ69ZF3.
ChEMBLCHEMBL5614.

Protein family/group databases

CAZyGH116. Glycoside Hydrolase Family 116.

PTM databases

PhosphoSiteQ69ZF3.

Proteomic databases

PaxDbQ69ZF3.
PRIDEQ69ZF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030189; ENSMUSP00000030189; ENSMUSG00000028467.
GeneID230101.
KEGGmmu:230101.
UCSCuc008sqi.2. mouse.

Organism-specific databases

CTD57704.
MGIMGI:2654325. Gba2.
RougeSearch...

Phylogenomic databases

eggNOGCOG4354.
GeneTreeENSGT00390000010998.
HOGENOMHOG000234168.
HOVERGENHBG105975.
InParanoidQ69ZF3.
KOK17108.
OMAYQLPGQN.
OrthoDBEOG7ZGX2B.
PhylomeDBQ69ZF3.
TreeFamTF313888.

Gene expression databases

ArrayExpressQ69ZF3.
BgeeQ69ZF3.
CleanExMM_GBA2.
GenevestigatorQ69ZF3.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view]
PfamPF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view]
PIRSFPIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMSSF48208. SSF48208. 2 hits.
ProtoNetSearch...

Other

NextBio379792.
PROQ69ZF3.
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: July 9, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries