ID BGAL3_ARATH Reviewed; 856 AA. AC Q9SCV9; O23243; Q0WLZ5; Q42150; Q42317; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 04-NOV-2026, entry version 160. DE RecName: Full=Beta-galactosidase 3; DE Short=Lactase 3; DE EC=3.2.1.23; DE Flags: Precursor; GN Name=BGAL3; OrderedLocusNames=At4g36360; GN ORFNames=C7A10.1000, F23E13.200; 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] (ISOFORM 1). 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=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis RT thaliana."; RL Nature 391:485-488(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [4] 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 [5] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-856 (ISOFORM 1). RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-740. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.; RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [9] 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=2; CC Name=1; CC IsoId=Q9SCV9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9SCV9-2; Sequence=VSP_027466; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17466346}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA18137.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB16852.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAB80302.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ270299; CAB64739.1; -; mRNA. DR EMBL; Z99708; CAB16852.1; ALT_INIT; Genomic_DNA. DR EMBL; AL022141; CAA18137.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161589; CAB80302.1; ALT_INIT; Genomic_DNA. DR EMBL; CP002687; AEE86646.1; -; Genomic_DNA. DR EMBL; CP002687; AEE86647.1; -; Genomic_DNA. DR EMBL; OZ408686; CAO7050120.1; -; Genomic_DNA. DR EMBL; AY056285; AAL07134.1; -; mRNA. DR EMBL; AY091432; AAM14371.1; -; mRNA. DR EMBL; AK230040; BAF01862.1; -; mRNA. DR EMBL; Z37275; CAA85537.1; -; mRNA. DR PIR; B85429; B85429. DR PIR; T04600; T04600. DR RefSeq; NP_568001.1; NM_119799.4. [Q9SCV9-1] DR RefSeq; NP_849506.1; NM_179175.2. [Q9SCV9-2] DR AlphaFoldDB; Q9SCV9; -. DR SMR; Q9SCV9; -. DR BioGRID; 15070; 1. DR FunCoup; Q9SCV9; 139. DR IntAct; Q9SCV9; 1. DR STRING; 3702.Q9SCV9; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR GlyCosmos; Q9SCV9; 1 site, No reported glycans. DR GlyGen; Q9SCV9; 1 site. DR PaxDb; 3702-Q9SCV9; -. DR ProteomicsDB; 240680; -. [Q9SCV9-1] DR GeneID; 829788; -. DR KEGG; ath:AT4G36360; -. DR Araport; AT4G36360; -. DR TAIR; AT4G36360; BGAL3. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_007853_4_0_1; -. DR InParanoid; Q9SCV9; -. DR OrthoDB; 1657402at2759; -. DR PhylomeDB; Q9SCV9; -. DR BioCyc; ARA:AT4G36360-MONOMER; -. DR PRO; PR:Q9SCV9; -. DR Proteomes; UP000006548; Chromosome 4. DR Proteomes; UP001984100; Chromosome 4. DR ExpressionAtlas; Q9SCV9; baseline and differential. DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; ISM:TAIR. DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0004565; F:beta-galactosidase activity; IDA:TAIR. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0019388; P:galactose catabolic process; IBA:GO_Central. DR GO; GO:0009827; P:plant-type cell wall modification; IBA:GO_Central. DR CDD; cd22842; Gal_Rha_Lectin_BGal; 1. DR FunFam; 2.60.120.260:FF:000061; Beta-galactosidase; 1. DR FunFam; 2.60.120.260:FF:000076; Beta-galactosidase; 1. DR FunFam; 2.60.120.740:FF:000002; Beta-galactosidase; 1. DR FunFam; 3.20.20.80:FF:000021; Beta-galactosidase; 1. DR Gene3D; 2.60.120.740; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR048913; BetaGal_gal-bd. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR017853; GH_hydrolase_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; IPR000922; Lectin_gal-bd_dom. DR InterPro; IPR043159; Lectin_gal-bd_sf. DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1. DR Pfam; PF21467; BetaGal_gal-bd; 2. DR Pfam; PF17834; GHD; 1. DR Pfam; PF01301; Glyco_hydro_35; 1. DR Pfam; PF02140; SUEL_Lectin; 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. PE 2: Evidence at transcript level; KW Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..856 FT /note="Beta-galactosidase 3" FT /id="PRO_0000293091" FT DOMAIN 760..846 FT /note="SUEL-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT ACT_SITE 189 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 258 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT CARBOHYD 468 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 811 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_027466" FT CONFLICT 656 FT /note="V -> L (in Ref. 8; CAA85537)" FT /evidence="ECO:0000305" FT CONFLICT 683 FT /note="K -> L (in Ref. 8; CAA85537)" FT /evidence="ECO:0000305" SQ SEQUENCE 856 AA; 95193 MW; 245C03A09493C785 CRC64; MREMGTGDSA SRLILWFCLG FLILGVGFVQ CGVTYDRKAL LINGQRRILF SGSIHYPRST PDMWEDLIQK AKDGGIDVIE TYVFWNLHEP SPGKYDFEGR NDLVRFVKTI HKAGLYAHLR IGPYVCAEWN FGGFPVWLKY VPGISFRTDN EPFKRAMKGF TERIVELMKS ENLFESQGGP IILSQIENEY GRQGQLLGAE GHNYMTWAAK MAIATETGVP WVMCKEDDAP DPVINTCNGF YCDSFAPNKP YKPLIWTEAW SGWFTEFGGP MHHRPVQDLA FGVARFIQKG GSFVNYYMYH GGTNFGRTAG GPFVTTSYDY DAPIDEYGLI RQPKYGHLKE LHRAIKMCEK ALVSADPVVT SIGNKQQAHV YSAESGDCSA FLANYDTESA ARVLFNNVHY NLPPWSISIL PDCRNAVFNT AKVGVQTSQM EMLPTDTKNF QWESYLEDLS SLDDSSTFTT HGLLEQINVT RDTSDYLWYM TSVDIGDSES FLHGGELPTL IIQSTGHAVH IFVNGQLSGS AFGTRQNRRF TYQGKINLHS GTNRIALLSV AVGLPNVGGH FESWNTGILG PVALHGLSQG KMDLSWQKWT YQVGLKGEAM NLAFPTNTPS IGWMDASLTV QKPQPLTWHK TYFDAPEGNE PLALDMEGMG KGQIWVNGES IGRYWTAFAT GDCSHCSYTG TYKPNKCQTG CGQPTQRWYH VPRAWLKPSQ NLLVIFEELG GNPSTVSLVK RSVSGVCAEV SEYHPNIKNW QIESYGKGQT FHRPKVHLKC SPGQAIASIK FASFGTPLGT CGSYQQGECH AATSYAILER KCVGKARCAV TISNSNFGKD PCPNVLKRLT VEAVCAPETS VSTWRP //