BGA12_ARATH
ID BGA12_ARATH Reviewed; 728 AA.
AC Q9SCV0; Q8LPL0; Q9SZI5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Beta-galactosidase 12;
DE Short=Lactase 12;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL12; OrderedLocusNames=At4g26140; ORFNames=F20B18.250;
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=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 [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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [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 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=Q9SCV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SCV0-2; Sequence=VSP_026465, VSP_026466, VSP_026467;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher expression levels in roots
CC and siliques. {ECO:0000269|PubMed:16267099}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site and to an intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB39679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79469.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ270308; CAB64748.1; -; mRNA.
DR EMBL; AL049483; CAB39679.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161564; CAB79469.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85162.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85163.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67751.1; -; Genomic_DNA.
DR EMBL; AY099612; AAM20463.1; -; mRNA.
DR EMBL; BT000267; AAN15586.1; -; mRNA.
DR PIR; T04269; T04269.
DR RefSeq; NP_001329560.1; NM_001341777.1. [Q9SCV0-2]
DR RefSeq; NP_194344.2; NM_118747.3. [Q9SCV0-2]
DR RefSeq; NP_849553.1; NM_179222.2. [Q9SCV0-1]
DR AlphaFoldDB; Q9SCV0; -.
DR SMR; Q9SCV0; -.
DR BioGRID; 14007; 1.
DR STRING; 3702.AT4G26140.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCV0; -.
DR PRIDE; Q9SCV0; -.
DR ProteomicsDB; 240758; -. [Q9SCV0-1]
DR EnsemblPlants; AT4G26140.1; AT4G26140.1; AT4G26140. [Q9SCV0-1]
DR EnsemblPlants; AT4G26140.2; AT4G26140.2; AT4G26140. [Q9SCV0-2]
DR EnsemblPlants; AT4G26140.3; AT4G26140.3; AT4G26140. [Q9SCV0-2]
DR GeneID; 828720; -.
DR Gramene; AT4G26140.1; AT4G26140.1; AT4G26140. [Q9SCV0-1]
DR Gramene; AT4G26140.2; AT4G26140.2; AT4G26140. [Q9SCV0-2]
DR Gramene; AT4G26140.3; AT4G26140.3; AT4G26140. [Q9SCV0-2]
DR KEGG; ath:AT4G26140; -.
DR Araport; AT4G26140; -.
DR TAIR; locus:2120830; AT4G26140.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCV0; -.
DR OMA; RGNCGNC; -.
DR PhylomeDB; Q9SCV0; -.
DR PRO; PR:Q9SCV0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCV0; baseline and differential.
DR Genevisible; Q9SCV0; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 PANTHER; PTHR23421; PTHR23421; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..728
FT /note="Beta-galactosidase 12"
FT /id="PRO_5000065885"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 418..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026465"
FT VAR_SEQ 624..638
FT /note="STFDSPTGNEPLALD -> VRETEESMNHDHQQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026466"
FT VAR_SEQ 639..728
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026467"
SQ SEQUENCE 728 AA; 81533 MW; 75EB099914A7BA65 CRC64;
MGLNFREKAW ILLGILCCSS LICSVKAIVT YDRKAVIING QRRILLSGSI HYPRSTPEMW
PDLIQKAKDG GLDVIQTYVF WNGHEPSPGQ YYFEDRYDLV KFIKVVQQAG LYVHLRIGPY
VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK AAMQKFTEKI VRMMKEEKLF ETQGGPIILS
QIENEYGPIE WEIGAPGKAY TKWVAEMAQG LSTGVPWIMC KQDDAPNSII NTCNGFYCEN
FKPNSDNKPK MWTENWTGWF TEFGGAVPYR PAEDIALSVA RFIQNGGSFI NYYMYHGGTN
FDRTAGEFIA TSYDYDAPLD EYGLPREPKY SHLKRLHKVI KLCEPALVSA DPTVTSLGDK
QEAHVFKSKS SCAAFLSNYN TSSAARVLFG GSTYDLPPWS VSILPDCKTE YYNTAKVQVR
TSSIHMKMVP TNTPFSWGSY NEEIPSANDN GTFSQDGLVE QISITRDKTD YFWYLTDITI
SPDEKFLTGE DPLLTIGSAG HALHVFVNGQ LAGTAYGSLE KPKLTFSQKI KLHAGVNKLA
LLSTAAGLPN VGVHYETWNT GVLGPVTLNG VNSGTWDMTK WKWSYKIGTK GEALSVHTLA
GSSTVEWKEG SLVAKKQPLT WYKSTFDSPT GNEPLALDMN TMGKGQMWIN GQNIGRHWPA
YTARGKCERC SYAGTFTEKK CLSNCGEASQ RWYHVPRSWL KPTNNLVIVL EEWGGEPNGI
SLVKRTAK
