BGAL3_ARATH
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 03-AUG-2022, entry version 143.
DE RecName: Full=Beta-galactosidase 3;
DE Short=Lactase 3;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL3; OrderedLocusNames=At4g36360; 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 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 [6]
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 [7]
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 [8]
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};
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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; 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 IntAct; Q9SCV9; 1.
DR STRING; 3702.AT4G36360.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCV9; -.
DR PRIDE; Q9SCV9; -.
DR ProteomicsDB; 240680; -. [Q9SCV9-1]
DR EnsemblPlants; AT4G36360.1; AT4G36360.1; AT4G36360. [Q9SCV9-1]
DR EnsemblPlants; AT4G36360.2; AT4G36360.2; AT4G36360. [Q9SCV9-2]
DR GeneID; 829788; -.
DR Gramene; AT4G36360.1; AT4G36360.1; AT4G36360. [Q9SCV9-1]
DR Gramene; AT4G36360.2; AT4G36360.2; AT4G36360. [Q9SCV9-2]
DR KEGG; ath:AT4G36360; -.
DR Araport; AT4G36360; -.
DR TAIR; locus:2115310; AT4G36360.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCV9; -.
DR OMA; SGECSAF; -.
DR PhylomeDB; Q9SCV9; -.
DR BioCyc; ARA:AT4G36360-MON; -.
DR PRO; PR:Q9SCV9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCV9; baseline and differential.
DR Genevisible; Q9SCV9; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.740; -; 1.
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; PTHR23421; 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; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
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. 7; CAA85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="K -> L (in Ref. 7; 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
