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P17439 (GLCM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosylceramidase

EC=3.2.1.45
Alternative name(s):
Acid beta-glucosidase
Beta-glucocerebrosidase
D-glucosyl-N-acylsphingosine glucohydrolase
Gene names
Name:Gba
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processLipid metabolism
Sphingolipid metabolism
   Cellular componentLysosome
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

ceramide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

glucosylceramide catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of water loss via skin

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to thyroid hormone

Inferred from electronic annotation. Source: Ensembl

skin morphogenesis

Inferred from electronic annotation. Source: Ensembl

sphingosine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

termination of signal transduction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentlysosomal lumen

Inferred from direct assay PubMed 18022370. Source: BHF-UCL

lysosomal membrane

Inferred from direct assay PubMed 18022370. Source: BHF-UCL

   Molecular_functionglucosylceramidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor binding

Inferred from physical interaction PubMed 18022370. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SCARB2Q141081EBI-1564504,EBI-1564650From a different organism.
Scarb2O351141EBI-1564504,EBI-1564519

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 515496Glucosylceramidase
PRO_0000012178

Sites

Active site2541Proton donor By similarity
Active site3581Nucleophile By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) (high mannose) Ref.7
Glycosylation2891N-linked (GlcNAc...) Ref.8
Glycosylation4801N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 35 By similarity
Disulfide bond37 ↔ 42 By similarity

Sequences

Sequence LengthMass (Da)Tools
P17439 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 7CCD9176085FE2CB

FASTA51557,622
        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 

« Hide

References

« Hide '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. 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: 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, IDENTIFICATION BY 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.
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.
+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.
PIRA32931.
RefSeqNP_001070879.1. NM_001077411.1.
NP_032120.1. NM_008094.4.
UniGeneMm.5031.

3D structure databases

ProteinModelPortalP17439.
SMRP17439. Positions 20-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17439. 4 interactions.
MINTMINT-4096112.
STRING10090.ENSMUSP00000076589.

Chemistry

BindingDBP17439.
ChEMBLCHEMBL2278.

Protein family/group databases

CAZyGH30. Glycoside Hydrolase Family 30.

PTM databases

PhosphoSiteP17439.

Proteomic databases

PaxDbP17439.
PRIDEP17439.

Protocols and materials databases

DNASU14466.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077367; ENSMUSP00000076589; ENSMUSG00000028048.
ENSMUST00000167998; ENSMUSP00000130660; ENSMUSG00000028048.
GeneID14466.
KEGGmmu:14466.
UCSCuc008pyb.1. mouse.

Organism-specific databases

CTD2629.
MGIMGI:95665. Gba.

Phylogenomic databases

eggNOGCOG5520.
GeneTreeENSGT00390000009464.
HOGENOMHOG000270031.
HOVERGENHBG002285.
InParanoidP17439.
KOK01201.
OMAAAKYVWG.
OrthoDBEOG76DTRZ.
PhylomeDBP17439.
TreeFamTF314254.

Gene expression databases

BgeeP17439.
CleanExMM_GBA.
GenevestigatorP17439.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013780. Glyco_hydro_13_b.
IPR001139. Glyco_hydro_30.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR11069. PTHR11069. 1 hit.
PfamPF02055. Glyco_hydro_30. 1 hit.
[Graphical view]
PRINTSPR00843. GLHYDRLASE30.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

NextBio286116.
PROP17439.
SOURCESearch...

Entry information

Entry nameGLCM_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 119 of the entry and version 1 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