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   24-JAN-2024, entry version 121.
DE   RecName: Full=Lysosomal beta glucosidase;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=gluA; ORFNames=DDB_G0292810;
OS   Dictyostelium discoideum (Social amoeba).
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.Q23892; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q23892; 7 sites, No reported glycans.
DR   PaxDb; 44689-DDB0215373; -.
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; MSAYHSY; -.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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
//