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Q9SCU8

- BGA14_ARATH

UniProt

Q9SCU8 - BGA14_ARATH

Protein

Beta-galactosidase 14

Gene

BGAL14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei197 – 1971Proton donorSequence Analysis
    Active sitei268 – 2681NucleophileSequence Analysis

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:GQT-2802-MONOMER.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase 14 (EC:3.2.1.23)
    Short name:
    Lactase 14
    Gene namesi
    Name:BGAL14
    Ordered Locus Names:At4g38590
    ORF Names:F20M13.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G38590.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 887856Beta-galactosidase 14PRO_5000065887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9SCU8.
    PRIDEiQ9SCU8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9SCU8.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SCU8.
    SMRiQ9SCU8. Positions 41-709.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini752 – 83887SUEL-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated
    Contains 1 SUEL-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000239919.
    InParanoidiQ9SCU8.
    PhylomeDBiQ9SCU8.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR006104. Glyco_hydro_2_N.
    IPR019801. Glyco_hydro_35_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR001944. Glycoside_Hdrlase_35.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000922. Lectin_gal-bd_dom.
    [Graphical view]
    PANTHERiPTHR23421. PTHR23421. 1 hit.
    PfamiPF02140. Gal_Lectin. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view]
    PRINTSiPR00742. GLHYDRLASE35.
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    PS50228. SUEL_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9SCU8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSKSSRIRMK SRTRYLIAIL LVISLCSKAS SHDDEKKKKG VTYDGTSLII    50
    NGKRELLFSG SVHYPRSTPH MWPSIIDKAR IGGLNTIQTY VFWNVHEPEQ 100
    GKYDFKGRFD LVKFIKLIHE KGLYVTLRLG PFIQAEWNHG GLPYWLREVP 150
    DVYFRTNNEP FKEHTERYVR KILGMMKEEK LFASQGGPII LGQIENEYNA 200
    VQLAYKENGE KYIKWAANLV ESMNLGIPWV MCKQNDAPGN LINACNGRHC 250
    GDTFPGPNRH DKPSLWTENW TTQFRVFGDP PTQRTVEDIA FSVARYFSKN 300
    GSHVNYYMYH GGTNFGRTSA HFVTTRYYDD APLDEFGLEK APKYGHLKHV 350
    HRALRLCKKA LFWGQLRAQT LGPDTEVRYY EQPGTKVCAA FLSNNNTRDT 400
    NTIKFKGQDY VLPSRSISIL PDCKTVVYNT AQIVAQHSWR DFVKSEKTSK 450
    GLKFEMFSEN IPSLLDGDSL IPGELYYLTK DKTDYAWYTT SVKIDEDDFP 500
    DQKGLKTILR VASLGHALIV YVNGEYAGKA HGRHEMKSFE FAKPVNFKTG 550
    DNRISILGVL TGLPDSGSYM EHRFAGPRAI SIIGLKSGTR DLTENNEWGH 600
    LAGLEGEKKE VYTEEGSKKV KWEKDGKRKP LTWYKTYFET PEGVNAVAIR 650
    MKAMGKGLIW VNGIGVGRYW MSFLSPLGEP TQTEYHIPRS FMKGEKKKNM 700
    LVILEEEPGV KLESIDFVLV NRDTICSNVG EDYPVSVKSW KREGPKIVSR 750
    SKDMRLKAVM RCPPEKQMVE VQFASFGDPT GTCGNFTMGK CSASKSKEVV 800
    EKECLGRNYC SIVVARETFG DKGCPEIVKT LAVQVKCEKK EGKQDEKKKK 850
    EDKDEEEEDD EDDDEEEEEE DKENKDTKDM ENKNQDM 887
    Length:887
    Mass (Da):101,222
    Last modified:July 10, 2007 - v2
    Checksum:i58486CB4B949508D
    GO

    Sequence cautioni

    The sequence AEE86951.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80523.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571L → F in CAB64750. 1 PublicationCurated
    Sequence conflicti70 – 701H → D in CAB64750. 1 PublicationCurated
    Sequence conflicti286 – 2861V → A in CAB64750. 1 PublicationCurated
    Sequence conflicti627 – 6271K → E in CAB64750. 1 PublicationCurated
    Sequence conflicti653 – 6531A → G in CAB64750. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270310 mRNA. Translation: CAB64750.1.
    AL035540 Genomic DNA. Translation: CAB37515.1. Sequence problems.
    AL161593 Genomic DNA. Translation: CAB80523.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86951.1. Sequence problems.
    PIRiT05687.
    RefSeqiNP_195571.2. NM_120020.3.
    UniGeneiAt.70242.

    Genome annotation databases

    EnsemblPlantsiAT4G38590.1; AT4G38590.1; AT4G38590.
    GeneIDi830016.
    KEGGiath:AT4G38590.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270310 mRNA. Translation: CAB64750.1 .
    AL035540 Genomic DNA. Translation: CAB37515.1 . Sequence problems.
    AL161593 Genomic DNA. Translation: CAB80523.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86951.1 . Sequence problems.
    PIRi T05687.
    RefSeqi NP_195571.2. NM_120020.3.
    UniGenei At.70242.

    3D structure databases

    ProteinModelPortali Q9SCU8.
    SMRi Q9SCU8. Positions 41-709.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9SCU8.
    PRIDEi Q9SCU8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G38590.1 ; AT4G38590.1 ; AT4G38590 .
    GeneIDi 830016.
    KEGGi ath:AT4G38590.

    Organism-specific databases

    GeneFarmi 517. 90.
    TAIRi AT4G38590.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000239919.
    InParanoidi Q9SCU8.
    PhylomeDBi Q9SCU8.

    Enzyme and pathway databases

    BioCyci ARA:GQT-2802-MONOMER.

    Gene expression databases

    Genevestigatori Q9SCU8.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    IPR006104. Glyco_hydro_2_N.
    IPR019801. Glyco_hydro_35_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR001944. Glycoside_Hdrlase_35.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000922. Lectin_gal-bd_dom.
    [Graphical view ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF02140. Gal_Lectin. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    PS50228. SUEL_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The beta-galactosidases are encoding by a multigene family in Arabidopsis thaliana."
      Gy I., Kreis M., Lecharny A.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35."
      Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.
      Phytochemistry 68:1510-1520(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGA14_ARATH
    AccessioniPrimary (citable) accession number: Q9SCU8
    Secondary accession number(s): F4JUE4, Q9SZN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3