ID   BGAL8_ARATH             Reviewed;         852 AA.
AC   Q9SCV4; Q96257; Q9SK11;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Beta-galactosidase 8;
DE            Short=Lactase 8;
DE            EC=3.2.1.23;
DE   AltName: Full=Protein AR782;
DE   Flags: Precursor;
GN   Name=BGAL8; OrderedLocusNames=At2g28470; ORFNames=T17D12.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gy I., Kreis M., Lecharny A.;
RT   "The beta-galactosidases are encoding by a multigene family in Arabidopsis
RT   thaliana.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 647-852.
RX   PubMed=9287109; DOI=10.1016/s0014-5793(97)00871-5;
RA   Hirayama T., Ishida C., Kuromori T., Obata S., Shimoda C., Yamamoto M.,
RA   Shinozaki K., Ohto C.;
RT   "Functional cloning of a cDNA encoding Mei2-like protein from Arabidopsis
RT   thaliana using a fission yeast pheromone receptor deficient mutant.";
RL   FEBS Lett. 413:16-20(1997).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16267099; DOI=10.1093/pcp/pci223;
RA   Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT   "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 47:55-63(2006).
RN   [6]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17466346; DOI=10.1016/j.phytochem.2007.03.021;
RA   Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P.,
RA   Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT   family 35.";
RL   Phytochemistry 68:1510-1520(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SCV4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, flowers and siliques.
CC       {ECO:0000269|PubMed:16267099, ECO:0000269|PubMed:17466346}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD21482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ270304; CAB64744.1; -; mRNA.
DR   EMBL; AC006587; AAD21482.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08127.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62009.1; -; Genomic_DNA.
DR   EMBL; D88744; BAA13685.1; -; mRNA.
DR   PIR; C84685; C84685.
DR   RefSeq; NP_001324192.1; NM_001336165.1. [Q9SCV4-1]
DR   RefSeq; NP_850121.1; NM_179790.3. [Q9SCV4-1]
DR   AlphaFoldDB; Q9SCV4; -.
DR   SMR; Q9SCV4; -.
DR   STRING; 3702.Q9SCV4; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCV4; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT2G28470-1; -.
DR   ProteomicsDB; 240654; -. [Q9SCV4-1]
DR   EnsemblPlants; AT2G28470.1; AT2G28470.1; AT2G28470. [Q9SCV4-1]
DR   EnsemblPlants; AT2G28470.3; AT2G28470.3; AT2G28470. [Q9SCV4-1]
DR   GeneID; 817395; -.
DR   Gramene; AT2G28470.1; AT2G28470.1; AT2G28470. [Q9SCV4-1]
DR   Gramene; AT2G28470.3; AT2G28470.3; AT2G28470. [Q9SCV4-1]
DR   KEGG; ath:AT2G28470; -.
DR   Araport; AT2G28470; -.
DR   TAIR; AT2G28470; BGAL8.
DR   eggNOG; KOG0496; Eukaryota.
DR   InParanoid; Q9SCV4; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; Q9SCV4; -.
DR   BioCyc; ARA:AT2G28470-MONOMER; -.
DR   PRO; PR:Q9SCV4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SCV4; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041392; GHD.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   PANTHER; PTHR23421:SF124; BETA-GALACTOSIDASE 2-RELATED; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
DR   Genevisible; Q9SCV4; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..852
FT                   /note="Beta-galactosidase 8"
FT                   /id="PRO_5000065882"
FT   DOMAIN          766..852
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        807
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        568
FT                   /note="V -> M (in Ref. 1; CAB64744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647..648
FT                   /note="FT -> TA (in Ref. 4; BAA13685)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   852 AA;  93210 MW;  54DCFB09790EE045 CRC64;
     MEIAAKMVKV RKMEMILLLI LVIVVAATAA NVTYDHRALV IDGKRKVLIS GSIHYPRSTP
     EMWPELIQKS KDGGLDVIET YVFWSGHEPE KNKYNFEGRY DLVKFVKLAA KAGLYVHLRI
     GPYVCAEWNY GGFPVWLHFV PGIKFRTDNE PFKEEMQRFT TKIVDLMKQE KLYASQGGPI
     ILSQIENEYG NIDSAYGAAA KSYIKWSASM ALSLDTGVPW NMCQQTDAPD PMINTCNGFY
     CDQFTPNSNN KPKMWTENWS GWFLGFGDPS PYRPVEDLAF AVARFYQRGG TFQNYYMYHG
     GTNFDRTSGG PLISTSYDYD APIDEYGLLR QPKWGHLRDL HKAIKLCEDA LIATDPTITS
     LGSNLEAAVY KTESGSCAAF LANVDTKSDA TVTFNGKSYN LPAWSVSILP DCKNVAFNTA
     KINSATESTA FARQSLKPDG GSSAELGSQW SYIKEPIGIS KADAFLKPGL LEQINTTADK
     SDYLWYSLRT DIKGDETFLD EGSKAVLHIE SLGQVVYAFI NGKLAGSGHG KQKISLDIPI
     NLVTGTNTID LLSVTVGLAN YGAFFDLVGA GITGPVTLKS AKGGSSIDLA SQQWTYQVGL
     KGEDTGLATV DSSEWVSKSP LPTKQPLIWY KTTFDAPSGS EPVAIDFTGT GKGIAWVNGQ
     SIGRYWPTSI AGNGGCTESC DYRGSYRANK CLKNCGKPSQ TLYHVPRSWL KPSGNILVLF
     EEMGGDPTQI SFATKQTGSN LCLTVSQSHP PPVDTWTSDS KISNRNRTRP VLSLKCPIST
     QVIFSIKFAS FGTPKGTCGS FTQGHCNSSR SLSLVQKACI GLRSCNVEVS TRVFGEPCRG
     VVKSLAVEAS CS
//