ID BGA14_ARATH Reviewed; 887 AA.
AC Q9SCU8; F4JUE4; Q9SZN8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=Beta-galactosidase 14;
DE Short=Lactase 14;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL14; OrderedLocusNames=At4g38590; ORFNames=F20M13.150;
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=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 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=Q9SCU8-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB80523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ270310; CAB64750.1; -; mRNA.
DR EMBL; AL035540; CAB37515.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T05687; T05687.
DR AlphaFoldDB; Q9SCU8; -.
DR SMR; Q9SCU8; -.
DR STRING; 3702.Q9SCU8; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GlyCosmos; Q9SCU8; 4 sites, No reported glycans.
DR PaxDb; 3702-AT4G38590-2; -.
DR ProteomicsDB; 240759; -. [Q9SCU8-1]
DR Araport; AT4G38590; -.
DR TAIR; AT4G38590; BGAL14.
DR eggNOG; KOG0495; Eukaryota.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCU8; -.
DR PhylomeDB; Q9SCU8; -.
DR PRO; PR:Q9SCU8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCU8; baseline and differential.
DR Genevisible; Q9SCU8; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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:SF52; BETA-GALACTOSIDASE 14; 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.
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..887
FT /note="Beta-galactosidase 14"
FT /id="PRO_5000065887"
FT DOMAIN 752..838
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT REGION 838..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..874
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 57
FT /note="L -> F (in Ref. 1; CAB64750)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="H -> D (in Ref. 1; CAB64750)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="V -> A (in Ref. 1; CAB64750)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="K -> E (in Ref. 1; CAB64750)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="A -> G (in Ref. 1; CAB64750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 101222 MW; 58486CB4B949508D CRC64;
MSKSSRIRMK SRTRYLIAIL LVISLCSKAS SHDDEKKKKG VTYDGTSLII NGKRELLFSG
SVHYPRSTPH MWPSIIDKAR IGGLNTIQTY VFWNVHEPEQ GKYDFKGRFD LVKFIKLIHE
KGLYVTLRLG PFIQAEWNHG GLPYWLREVP DVYFRTNNEP FKEHTERYVR KILGMMKEEK
LFASQGGPII LGQIENEYNA VQLAYKENGE KYIKWAANLV ESMNLGIPWV MCKQNDAPGN
LINACNGRHC GDTFPGPNRH DKPSLWTENW TTQFRVFGDP PTQRTVEDIA FSVARYFSKN
GSHVNYYMYH GGTNFGRTSA HFVTTRYYDD APLDEFGLEK APKYGHLKHV HRALRLCKKA
LFWGQLRAQT LGPDTEVRYY EQPGTKVCAA FLSNNNTRDT NTIKFKGQDY VLPSRSISIL
PDCKTVVYNT AQIVAQHSWR DFVKSEKTSK GLKFEMFSEN IPSLLDGDSL IPGELYYLTK
DKTDYAWYTT SVKIDEDDFP DQKGLKTILR VASLGHALIV YVNGEYAGKA HGRHEMKSFE
FAKPVNFKTG DNRISILGVL TGLPDSGSYM EHRFAGPRAI SIIGLKSGTR DLTENNEWGH
LAGLEGEKKE VYTEEGSKKV KWEKDGKRKP LTWYKTYFET PEGVNAVAIR MKAMGKGLIW
VNGIGVGRYW MSFLSPLGEP TQTEYHIPRS FMKGEKKKNM LVILEEEPGV KLESIDFVLV
NRDTICSNVG EDYPVSVKSW KREGPKIVSR SKDMRLKAVM RCPPEKQMVE VQFASFGDPT
GTCGNFTMGK CSASKSKEVV EKECLGRNYC SIVVARETFG DKGCPEIVKT LAVQVKCEKK
EGKQDEKKKK EDKDEEEEDD EDDDEEEEEE DKENKDTKDM ENKNQDM
//
