GLUA_DICDI
ID GLUA_DICDI Reviewed; 821 AA.
AC Q23892; Q54CI9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Lysosomal beta glucosidase;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=gluA; ORFNames=DDB_G0292810;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-78; 74-82; 204-213 AND
RP 583-592, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=8288612; DOI=10.1016/s0021-9258(17)42280-0;
RA Bush J., Richardson J., Cardelli J.;
RT "Molecular cloning and characterization of the full-length cDNA encoding
RT the developmentally regulated lysosomal enzyme beta-glucosidase in
RT Dictyostelium discoideum.";
RL J. Biol. Chem. 269:1468-1476(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP GLYCOSYLATION.
RX PubMed=6228551; DOI=10.1016/s0021-9258(17)43745-8;
RA Freeze H.H., Yeh R., Miller A.L., Kornfeld S.;
RT "Structural analysis of the asparagine-linked oligosaccharides from three
RT lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual
RT acid-stable phosphodiester.";
RL J. Biol. Chem. 258:14874-14879(1983).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=3082890; DOI=10.1083/jcb.102.4.1264;
RA Cardelli J.A., Golumbeski G.S., Dimond R.L.;
RT "Lysosomal enzymes in Dictyostelium discoideum are transported to lysosomes
RT at distinctly different rates.";
RL J. Cell Biol. 102:1264-1270(1986).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:3082890}.
CC -!- PTM: Glycosylated. The polyoligosaccharides are of the high-mannose
CC type and are highly substituted with both phosphate and sulfate
CC moieties. {ECO:0000269|PubMed:6228551}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
CC -!- CAUTION: PubMed:8288612 reports 2 different N-termini by direct protein
CC sequencing: mature protein either starts at Ile-70 or Ser-74.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74233.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L21014; AAA74233.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000197; EAL60954.1; -; Genomic_DNA.
DR PIR; A49881; A49881.
DR RefSeq; XP_629427.1; XM_629425.1.
DR AlphaFoldDB; Q23892; -.
DR SMR; Q23892; -.
DR STRING; 44689.DDB0215373; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q23892; -.
DR EnsemblProtists; EAL60954; EAL60954; DDB_G0292810.
DR GeneID; 8628946; -.
DR KEGG; ddi:DDB_G0292810; -.
DR dictyBase; DDB_G0292810; gluA.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR InParanoid; Q23892; -.
DR OMA; TLITDWD; -.
DR PhylomeDB; Q23892; -.
DR PRO; PR:Q23892; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR GO; GO:0008422; F:beta-glucosidase activity; IMP:dictyBase.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..69
FT /evidence="ECO:0000269|PubMed:8288612"
FT /id="PRO_0000361523"
FT CHAIN 70..821
FT /note="Lysosomal beta glucosidase"
FT /id="PRO_0000361524"
FT ACT_SITE 363
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 290
FT /note="D -> N (in Ref. 1; AAA74233)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..475
FT /note="QN -> LF (in Ref. 1; AAA74233)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="Missing (in Ref. 1; AAA74233)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="T -> TVT (in Ref. 1; AAA74233)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="Q -> P (in Ref. 1; AAA74233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 89344 MW; 297758E5007DD13D CRC64;
MKTIKSLFLL SLLIVNLLIS STYGSSIRVS IVGGEEAEVI EKPRTFGNKR ELKLEYSQIY
PKKQLNQENI NFMSARDTFV DNLMSKMSIT EKIGQMTQLD ITTLTSPNTI TINETTLAYY
AKTYYIGSYL NSPVSGGLAG DIHHINSSVW LDMINTIQTI VIEGSPNKIP MIYGLDSVHG
ANYVHKATLF PHNTGLAATF NIEHATTAAQ ITSKDTVAVG IPWVFAPVLG IGVQPLWSRI
YETFGEDPYV ASMMGAAAVR GFQGGNNSFD GPINAPSAVC TAKHYFGYSD PTSGKDRTAA
WIPERMLRRY FLPSFAEAIT GAGAGTIMIN SGEVNGVPMH TSYKYLTEVL RGELQFEGVA
VTDWQDIEKL VYFHHTAGSA EEAILQALDA GIDMSMVPLD LSFPIILAEM VAAGTVPESR
LDLSVRRILN LKYALGLFSN PYPNPNAAIV DTIGQVQDRE AAAATAEESI TLLQNKNNIL
PLNTNTIKNV LLTGPSADSI RNLNGGWSVH WQGAYEDSEF PFGTSILTGL REITNDTADF
NIQYTIGHEI GVPTNQTSID EAVELAQSSD VVVVVIGELP EAETPGDIYD LSMDPNEVLL
LQQLVDTGKP VVLILVEARP RILPPDLVYS CAAVLMAYLP GSEGGKPIAN ILMGNVNPSG
RLPLTYPGTT GDIGVPYYHK YSENGVTTPL FQFGDGLSYT TFNYTNLACS NCKPISGQSG
NYTGVLGQSY TFTVTVTNNG NVQGKDSVLL YLSDLWAQVT PEVKMLRGFQ KVDLMPAKSQ
QISFTLNAYE FSFIGVDNKI TLESGQFIIM VGNQQLGLYL Q
