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Q23892 (GLUA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:
Lysosomal beta glucosidase

EC=3.2.1.21
Gene names
Name:gluA
ORF Names:DDB_G0292810
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Subcellular location

Lysosome Ref.4.

Post-translational modification

Glycosylated. The polyoligosaccharides are of the high-mannose type and are highly substituted with both phosphate and sulfate moieties. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Caution

Ref.1 reports 2 different N-termini by direct protein sequencing: mature protein either starts at Ile-70 or Ser-74.

Sequence caution

The sequence AAA74233.1 differs from that shown. Reason: Frameshift at positions 393, 397, 399, 402 and 409.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 6945
PRO_0000361523
Chain70 – 821752Lysosomal beta glucosidase
PRO_0000361524

Regions

Compositional bias461 – 4666Poly-Ala
Compositional bias571 – 5755Poly-Val

Sites

Active site3631 By similarity

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation5351N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Glycosylation7031N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2901D → N in AAA74233. Ref.1
Sequence conflict474 – 4752QN → LF in AAA74233. Ref.1
Sequence conflict7251Missing in AAA74233. Ref.1
Sequence conflict7371T → TVT in AAA74233. Ref.1
Sequence conflict8061Q → P in AAA74233. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q23892 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 297758E5007DD13D

FASTA82189,344
        10         20         30         40         50         60 
MKTIKSLFLL SLLIVNLLIS STYGSSIRVS IVGGEEAEVI EKPRTFGNKR ELKLEYSQIY 

        70         80         90        100        110        120 
PKKQLNQENI NFMSARDTFV DNLMSKMSIT EKIGQMTQLD ITTLTSPNTI TINETTLAYY 

       130        140        150        160        170        180 
AKTYYIGSYL NSPVSGGLAG DIHHINSSVW LDMINTIQTI VIEGSPNKIP MIYGLDSVHG 

       190        200        210        220        230        240 
ANYVHKATLF PHNTGLAATF NIEHATTAAQ ITSKDTVAVG IPWVFAPVLG IGVQPLWSRI 

       250        260        270        280        290        300 
YETFGEDPYV ASMMGAAAVR GFQGGNNSFD GPINAPSAVC TAKHYFGYSD PTSGKDRTAA 

       310        320        330        340        350        360 
WIPERMLRRY FLPSFAEAIT GAGAGTIMIN SGEVNGVPMH TSYKYLTEVL RGELQFEGVA 

       370        380        390        400        410        420 
VTDWQDIEKL VYFHHTAGSA EEAILQALDA GIDMSMVPLD LSFPIILAEM VAAGTVPESR 

       430        440        450        460        470        480 
LDLSVRRILN LKYALGLFSN PYPNPNAAIV DTIGQVQDRE AAAATAEESI TLLQNKNNIL 

       490        500        510        520        530        540 
PLNTNTIKNV LLTGPSADSI RNLNGGWSVH WQGAYEDSEF PFGTSILTGL REITNDTADF 

       550        560        570        580        590        600 
NIQYTIGHEI GVPTNQTSID EAVELAQSSD VVVVVIGELP EAETPGDIYD LSMDPNEVLL 

       610        620        630        640        650        660 
LQQLVDTGKP VVLILVEARP RILPPDLVYS CAAVLMAYLP GSEGGKPIAN ILMGNVNPSG 

       670        680        690        700        710        720 
RLPLTYPGTT GDIGVPYYHK YSENGVTTPL FQFGDGLSYT TFNYTNLACS NCKPISGQSG 

       730        740        750        760        770        780 
NYTGVLGQSY TFTVTVTNNG NVQGKDSVLL YLSDLWAQVT PEVKMLRGFQ KVDLMPAKSQ 

       790        800        810        820 
QISFTLNAYE FSFIGVDNKI TLESGQFIIM VGNQQLGLYL Q 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the full-length cDNA encoding the developmentally regulated lysosomal enzyme beta-glucosidase in Dictyostelium discoideum."
Bush J., Richardson J., Cardelli J.
J. Biol. Chem. 269:1468-1476(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-78; 74-82; 204-213 AND 583-592, DEVELOPMENTAL STAGE.
Strain: AX3.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester."
Freeze H.H., Yeh R., Miller A.L., Kornfeld S.
J. Biol. Chem. 258:14874-14879(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[4]"Lysosomal enzymes in Dictyostelium discoideum are transported to lysosomes at distinctly different rates."
Cardelli J.A., Golumbeski G.S., Dimond R.L.
J. Cell Biol. 102:1264-1270(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L21014 mRNA. Translation: AAA74233.1. Frameshift.
AAFI02000197 Genomic DNA. Translation: EAL60954.1.
PIRA49881.

3D structure databases

ProteinModelPortalQ23892.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0215373.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PRIDEQ23892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0215373; DDB0215373; DDB_G0292810.
KEGGddi:DDB_G0292810.

Organism-specific databases

dictyBaseDDB_G0292810. gluA.

Phylogenomic databases

eggNOGCOG1472.
KOK05349.
OMAITINETT.
PhylomeDBQ23892.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetSearch...

Other

PROQ23892.

Entry information

Entry nameGLUA_DICDI
AccessionPrimary (citable) accession number: Q23892
Secondary accession number(s): Q54CI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: April 16, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase