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Q5M868 (GBA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length912 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity. Plays a role in central nevous system development By similarity. Required for proper formation of motor neuron axons By similarity.

Catalytic activity

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

Enzyme regulation

Enzymatic activity is dependent on membrane association and requires the presence of lipids By similarity.

Subcellular location

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

Sequence similarities

Belongs to the non-lysosomal glucosylceramidase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5M868-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5M868-2)

The sequence of this isoform differs from the canonical sequence as follows:
     181-195: FIVCLRRDGRTVYQQ → VRKGAGRRRSDSWLA
     196-912: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 912912Non-lysosomal glucosylceramidase
PRO_0000283760

Natural variations

Alternative sequence181 – 19515FIVCL…TVYQQ → VRKGAGRRRSDSWLA in isoform 2.
VSP_024385
Alternative sequence196 – 912717Missing in isoform 2.
VSP_024386

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: C4A47C8C5F3D248A

FASTA912102,747
        10         20         30         40         50         60 
MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY CNSEDSGQLM 

        70         80         90        100        110        120 
ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS NLVKHFGMGL RYLKWWYRKT 

       130        140        150        160        170        180 
QVEKKTPFID MFNSVPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ 

       190        200        210        220        230        240 
FIVCLRRDGR TVYQQVLSLE LPSVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT 

       250        260        270        280        290        300 
CRQITPILPH DYQDSSLPVG VFVWDVENEG DETLDVSIMF SMRNGLGGED DAAGGLWNEP 

       310        320        330        340        350        360 
FRLEQDGTTV QGLLLHHPTP PNPYTMAVAA RHTADTTVTY TTAFDPDSTG QQVWQDLLQD 

       370        380        390        400        410        420 
GQLDSPAGQS TPTQRGEGVA GAVCASSKLL PRGRCCLEFS LAWDMPRIMF GAKGQVHYRR 

       430        440        450        460        470        480 
YTRFFGSDGD VAPALSHYAL CQYAGWENSI SAWQNPVLDD RSLPAWYKSA LFNELYFLAD 

       490        500        510        520        530        540 
GGTVWLEVPE DSLPEELGGS MYQLRPILQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM 

       550        560        570        580        590        600 
LWPKLELSLQ YDMALATFKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY 

       610        620        630        640        650        660 
LIHDTADWKD LNLKFVLQVY RDYYLTGDQG FLKDMWPVCL AVMESEMKFD KDQDGLIENG 

       670        680        690        700        710        720 
GYADQTYDGW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQDKFSSIL CRGREAYERL 

       730        740        750        760        770        780 
LWNGRYYNYD SSSQPQSRSV MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALKTIFELN 

       790        800        810        820        830        840 
VQAFAGGAMG AVNGMQPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY 

       850        860        870        880        890        900 
RTVWERLGLA FQTPEAYCQQ RVFRSLAYMR PLSIWAMQLA LQQQQHKKNS SRPAVTQGTA 

       910 
PSQPECGPKR SL 

« Hide

Isoform 2 [UniParc].

Checksum: 15E7B9B8FA13E3A3
Show »

FASTA19521,993

References

[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"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] (ISOFORM 2).
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03040369 Genomic DNA. No translation available.
BC088200 mRNA. Translation: AAH88200.1.
UniGeneRn.146071.

3D structure databases

ProteinModelPortalQ5M868.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000022002.

Protein family/group databases

CAZyGH116. Glycoside Hydrolase Family 116.

Proteomic databases

PaxDbQ5M868.
PRIDEQ5M868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1305598. rat. [Q5M868-1]

Organism-specific databases

RGD1305598. Gba2.

Phylogenomic databases

eggNOGCOG4354.
HOGENOMHOG000234168.
HOVERGENHBG105975.
InParanoidQ5M868.
PhylomeDBQ5M868.
TreeFamTF313888.

Gene expression databases

GenevestigatorQ5M868.

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. 1 hit.
ProtoNetSearch...

Other

PROQ5M868.

Entry information

Entry nameGBA2_RAT
AccessionPrimary (citable) accession number: Q5M868
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 66 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries