Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P17439

- GLCM_MOUSE

UniProt

P17439 - GLCM_MOUSE

(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)

Protein

Glucosylceramidase

Gene

Gba

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  2. lysosomal lumen Source: BHF-UCL
  3. lysosomal membrane Source: BHF-UCL
Complete GO annotation...

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

        10         20         30         40         50
MAARLIGFFL FQAVSWAYGA QPCIPKSFGY SSVVCVCNAS YCDSLDPVTL
60 70 80 90 100
PALGTFSRYE STRRGRRMEL SVGAIQANRT GTGLLLTLQP EKKFQKVKGF
110 120 130 140 150
GGAMTDATAL NILALSPPTQ KLLLRSYFST NGIEYNIIRV PMASCDFSIR
160 170 180 190 200
VYTYADTPND FQLSNFSLPE EDTKLKIPLI HQALKMSSRP ISLFASPWTS
210 220 230 240 250
PTWLKTNGRV NGKGSLKGQP GDIFHQTWAN YFVKFLDAYA KYGLRFWAVT
260 270 280 290 300
AENEPTAGLF TGYPFQCLGF TPEHQRDFIS RDLGPALANS SHDVKLLMLD
310 320 330 340 350
DQRLLLPRWA EVVLSDPEAA KYVHGIAVHW YMDFLAPAKA TLGETHRLFP
360 370 380 390 400
NTMLFASEAC VGSKFWEQSV RLGSWDRGMQ YSHSIITNLL YHVTGWTDWN
410 420 430 440 450
LALNPEGGPN WVRNFVDSPI IVDIPKDAFY KQPMFYHLGH FSKFIPEGSQ
460 470 480 490 500
RVALVASEST DLETVALLRP DGSAVVVVLN RSSEDVPLTI SDPDLGFLET
510
VSPGYSIHTY LWRRQ
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_001077411.2.
NP_032120.1. NM_008094.5.
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_001077411.2.
NP_032120.1. NM_008094.5.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 124 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