Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P17439

- GLCM_MOUSE

UniProt

P17439 - GLCM_MOUSE

Protein

Glucosylceramidase

Gene

Gba

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei254 – 2541Proton donorBy similarity
    Active sitei358 – 3581NucleophileBy similarity

    GO - Molecular functioni

    1. glucosylceramidase activity Source: UniProtKB-EC
    2. receptor binding Source: BHF-UCL

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cellular response to tumor necrosis factor Source: Ensembl
    3. ceramide biosynthetic process Source: Ensembl
    4. glucosylceramide catabolic process Source: Ensembl
    5. negative regulation of interleukin-6 production Source: Ensembl
    6. negative regulation of MAP kinase activity Source: Ensembl
    7. positive regulation of protein dephosphorylation Source: Ensembl
    8. regulation of water loss via skin Source: Ensembl
    9. response to estrogen Source: Ensembl
    10. response to glucocorticoid Source: Ensembl
    11. response to pH Source: Ensembl
    12. response to testosterone Source: Ensembl
    13. response to thyroid hormone Source: Ensembl
    14. skin morphogenesis Source: Ensembl
    15. sphingosine biosynthetic process Source: Ensembl
    16. termination of signal transduction Source: Ensembl

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Sphingolipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199008. Glycosphingolipid metabolism.

    Protein family/group databases

    CAZyiGH30. Glycoside Hydrolase Family 30.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucosylceramidase (EC:3.2.1.45)
    Alternative name(s):
    Acid beta-glucosidase
    Beta-glucocerebrosidase
    D-glucosyl-N-acylsphingosine glucohydrolase
    Gene namesi
    Name:Gba
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:95665. Gba.

    Subcellular locationi

    Lysosome membrane; Peripheral membrane protein
    Note: Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2.By similarity

    GO - Cellular componenti

    1. lysosomal lumen Source: BHF-UCL
    2. lysosomal membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 515496GlucosylceramidasePRO_0000012178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 35By similarity
    Disulfide bondi37 ↔ 42By similarity
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...) (high mannose)1 Publication
    Glycosylationi289 – 2891N-linked (GlcNAc...)1 Publication
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP17439.
    PaxDbiP17439.
    PRIDEiP17439.

    PTM databases

    PhosphoSiteiP17439.

    Expressioni

    Gene expression databases

    BgeeiP17439.
    CleanExiMM_GBA.
    GenevestigatoriP17439.

    Interactioni

    Subunit structurei

    Interacts with SCARB2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SCARB2Q141081EBI-1564504,EBI-1564650From a different organism.
    Scarb2O351141EBI-1564504,EBI-1564519

    Protein-protein interaction databases

    IntActiP17439. 4 interactions.
    MINTiMINT-4096112.
    STRINGi10090.ENSMUSP00000076589.

    Structurei

    3D structure databases

    ProteinModelPortaliP17439.
    SMRiP17439. Positions 20-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 30 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5520.
    GeneTreeiENSGT00390000009464.
    HOGENOMiHOG000270031.
    HOVERGENiHBG002285.
    InParanoidiP17439.
    KOiK01201.
    OMAiRWAQVVL.
    OrthoDBiEOG76DTRZ.
    PhylomeDBiP17439.
    TreeFamiTF314254.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR013780. Glyco_hydro_13_b.
    IPR001139. Glyco_hydro_30.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR11069. PTHR11069. 1 hit.
    PfamiPF02055. Glyco_hydro_30. 1 hit.
    [Graphical view]
    PRINTSiPR00843. GLHYDRLASE30.
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17439-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARLIGFFL FQAVSWAYGA QPCIPKSFGY SSVVCVCNAS YCDSLDPVTL    50
    PALGTFSRYE STRRGRRMEL SVGAIQANRT GTGLLLTLQP EKKFQKVKGF 100
    GGAMTDATAL NILALSPPTQ KLLLRSYFST NGIEYNIIRV PMASCDFSIR 150
    VYTYADTPND FQLSNFSLPE EDTKLKIPLI HQALKMSSRP ISLFASPWTS 200
    PTWLKTNGRV NGKGSLKGQP GDIFHQTWAN YFVKFLDAYA KYGLRFWAVT 250
    AENEPTAGLF TGYPFQCLGF TPEHQRDFIS RDLGPALANS SHDVKLLMLD 300
    DQRLLLPRWA EVVLSDPEAA KYVHGIAVHW YMDFLAPAKA TLGETHRLFP 350
    NTMLFASEAC VGSKFWEQSV RLGSWDRGMQ YSHSIITNLL YHVTGWTDWN 400
    LALNPEGGPN WVRNFVDSPI IVDIPKDAFY KQPMFYHLGH FSKFIPEGSQ 450
    RVALVASEST DLETVALLRP DGSAVVVVLN RSSEDVPLTI SDPDLGFLET 500
    VSPGYSIHTY LWRRQ 515
    Length:515
    Mass (Da):57,622
    Last modified:August 1, 1990 - v1
    Checksum:i7CCD9176085FE2CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS17493.1.
    PIRiA32931.
    RefSeqiNP_001070879.1. NM_001077411.1.
    NP_032120.1. NM_008094.4.
    UniGeneiMm.5031.

    Genome annotation databases

    EnsembliENSMUST00000077367; ENSMUSP00000076589; ENSMUSG00000028048.
    ENSMUST00000167998; ENSMUSP00000130660; ENSMUSG00000028048.
    GeneIDi14466.
    KEGGimmu:14466.
    UCSCiuc008pyb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS17493.1.
    PIRi A32931.
    RefSeqi NP_001070879.1. NM_001077411.1.
    NP_032120.1. NM_008094.4.
    UniGenei Mm.5031.

    3D structure databases

    ProteinModelPortali P17439.
    SMRi P17439. Positions 20-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P17439. 4 interactions.
    MINTi MINT-4096112.
    STRINGi 10090.ENSMUSP00000076589.

    Chemistry

    BindingDBi P17439.
    ChEMBLi CHEMBL2278.

    Protein family/group databases

    CAZyi GH30. Glycoside Hydrolase Family 30.

    PTM databases

    PhosphoSitei P17439.

    Proteomic databases

    MaxQBi P17439.
    PaxDbi P17439.
    PRIDEi P17439.

    Protocols and materials databases

    DNASUi 14466.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077367 ; ENSMUSP00000076589 ; ENSMUSG00000028048 .
    ENSMUST00000167998 ; ENSMUSP00000130660 ; ENSMUSG00000028048 .
    GeneIDi 14466.
    KEGGi mmu:14466.
    UCSCi uc008pyb.1. mouse.

    Organism-specific databases

    CTDi 2629.
    MGIi MGI:95665. Gba.

    Phylogenomic databases

    eggNOGi COG5520.
    GeneTreei ENSGT00390000009464.
    HOGENOMi HOG000270031.
    HOVERGENi HBG002285.
    InParanoidi P17439.
    KOi K01201.
    OMAi RWAQVVL.
    OrthoDBi EOG76DTRZ.
    PhylomeDBi P17439.
    TreeFami TF314254.

    Enzyme and pathway databases

    Reactomei REACT_199008. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 286116.
    PROi P17439.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17439.
    CleanExi MM_GBA.
    Genevestigatori P17439.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR013780. Glyco_hydro_13_b.
    IPR001139. Glyco_hydro_30.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR11069. PTHR11069. 1 hit.
    Pfami PF02055. Glyco_hydro_30. 1 hit.
    [Graphical view ]
    PRINTSi PR00843. GLHYDRLASE30.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiGLCM_MOUSE
    AccessioniPrimary (citable) accession number: P17439
    Secondary accession number(s): Q78NR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3