Reviewed, UniProtKB/Swiss-Prot Q23892 (GLUA_DICDI)

Names and origin

Protein names

Recommended name:
    Lysosomal beta glucosidase
    EC=3.2.1.21

Gene names

Name:	gluA
ORF Names:	DDB_G0292810

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	821 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 69	45			PRO_0000361523
	Chain	70 – 821	752	Lysosomal beta glucosidase		PRO_0000361524
Regions
	Compositional bias	461 – 466	6	Poly-Ala
	Compositional bias	571 – 575	5	Poly-Val
Sites
	Active site	363	1	By similarity
Amino acid modifications
	Glycosylation	113	1	N-linked (GlcNAc...) Potential
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	535	1	N-linked (GlcNAc...) Potential
	Glycosylation	555	1	N-linked (GlcNAc...) Potential
	Glycosylation	703	1	N-linked (GlcNAc...) Potential
	Glycosylation	721	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	290	1	D → N in AAA74233. Ref.1
	Sequence conflict	474 – 475	2	QN → LF in AAA74233. Ref.1
	Sequence conflict	725	1	Missing in AAA74233. Ref.1
	Sequence conflict	737	1	T → TVT in AAA74233. Ref.1
	Sequence conflict	806	1	Q → P in AAA74233. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q23892-1 [UniParc]. Last modified January 20, 2009. Version 2. Checksum: 297758E5007DD13D	FASTA	821	89,344
	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

References

	« Hide 'large scale' referencesShow '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: 8288612] [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. , 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: 15875012] [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: 6228551] [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: 3082890] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L21014 mRNA. Translation: AAA74233.1. Frameshift. AAFI02000197 Genomic DNA. Translation: EAL60954.1.
PIR	A49881.
RefSeq	XP_629427.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q23892.
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Genome annotation databases
GeneID	3386031.
GenomeReviews	Gene locus gluA in contig CM000155_GR.
KEGG	ddi:DDB_0215373.
Organism-specific databases
dictyBase	DDB_G0292810. gluA.
Phylogenomic databases
OMA	TITINET.
Family and domain databases
InterPro	IPR019800. Glyco_hydro_3_AS. IPR002772. Glyco_hydro_3_C. IPR001764. Glyco_hydro_3_N. [Graphical view]
Pfam	PF01915. Glyco_hydro_3_C. 1 hit. [Graphical view]
PRINTS	PR00133. GLHYDRLASE3.
PROSITE	PS00775. GLYCOSYL_HYDROL_F3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLUA_DICDI

Accession

Primary (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:	November 3, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)