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BGA14_ARATH
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   25-MAY-2022, entry version 129.
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.AT4G38590.2; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q9SCU8; -.
DR   PRIDE; Q9SCU8; -.
DR   ProteomicsDB; 240759; -. [Q9SCU8-1]
DR   Araport; AT4G38590; -.
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   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..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
 
 
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