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Q9SCV0

- BGA12_ARATH

UniProt

Q9SCV0 - BGA12_ARATH

Protein

Beta-galactosidase 12

Gene

BGAL12

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 1 (01 May 2000)
      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 sitei185 – 1851Proton donorSequence Analysis
    Active sitei254 – 2541NucleophileSequence Analysis

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT4G26140-MONOMER.
    ARA:GQT-2664-MONOMER.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase 12 (EC:3.2.1.23)
    Short name:
    Lactase 12
    Gene namesi
    Name:BGAL12
    Ordered Locus Names:At4g26140
    ORF Names:F20B18.250
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G26140.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell
    2. cell wall Source: TAIR

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 728701Beta-galactosidase 12PRO_5000065885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9SCV0.
    PRIDEiQ9SCV0.

    Expressioni

    Tissue specificityi

    Ubiquitous, with higher expression levels in roots and siliques.1 Publication

    Gene expression databases

    GenevestigatoriQ9SCV0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SCV0.
    SMRiQ9SCV0. Positions 29-726.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000239919.
    InParanoidiQ9SCV0.
    OMAiNSIINTC.
    PhylomeDBiQ9SCV0.

    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.
    [Graphical view]
    PANTHERiPTHR23421. PTHR23421. 1 hit.
    PfamiPF02837. Glyco_hydro_2_N. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view]
    PRINTSiPR00742. GLHYDRLASE35.
    SUPFAMiSSF49785. SSF49785. 3 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9SCV0-1) [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

    MGLNFREKAW ILLGILCCSS LICSVKAIVT YDRKAVIING QRRILLSGSI    50
    HYPRSTPEMW PDLIQKAKDG GLDVIQTYVF WNGHEPSPGQ YYFEDRYDLV 100
    KFIKVVQQAG LYVHLRIGPY VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK 150
    AAMQKFTEKI VRMMKEEKLF ETQGGPIILS QIENEYGPIE WEIGAPGKAY 200
    TKWVAEMAQG LSTGVPWIMC KQDDAPNSII NTCNGFYCEN FKPNSDNKPK 250
    MWTENWTGWF TEFGGAVPYR PAEDIALSVA RFIQNGGSFI NYYMYHGGTN 300
    FDRTAGEFIA TSYDYDAPLD EYGLPREPKY SHLKRLHKVI KLCEPALVSA 350
    DPTVTSLGDK QEAHVFKSKS SCAAFLSNYN TSSAARVLFG GSTYDLPPWS 400
    VSILPDCKTE YYNTAKVQVR TSSIHMKMVP TNTPFSWGSY NEEIPSANDN 450
    GTFSQDGLVE QISITRDKTD YFWYLTDITI SPDEKFLTGE DPLLTIGSAG 500
    HALHVFVNGQ LAGTAYGSLE KPKLTFSQKI KLHAGVNKLA LLSTAAGLPN 550
    VGVHYETWNT GVLGPVTLNG VNSGTWDMTK WKWSYKIGTK GEALSVHTLA 600
    GSSTVEWKEG SLVAKKQPLT WYKSTFDSPT GNEPLALDMN TMGKGQMWIN 650
    GQNIGRHWPA YTARGKCERC SYAGTFTEKK CLSNCGEASQ RWYHVPRSWL 700
    KPTNNLVIVL EEWGGEPNGI SLVKRTAK 728
    Length:728
    Mass (Da):81,533
    Last modified:May 1, 2000 - v1
    Checksum:i75EB099914A7BA65
    GO
    Isoform 2 (identifier: Q9SCV0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         418-419: Missing.
         624-638: STFDSPTGNEPLALD → VRETEESMNHDHQQS
         639-728: Missing.

    Note: May be due to a competing acceptor splice site and to an intron retention. No experimental confirmation available.

    Show »
    Length:636
    Mass (Da):71,357
    Checksum:i11F0DC8FDB69283D
    GO

    Sequence cautioni

    The sequence CAB39679.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB79469.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei418 – 4192Missing in isoform 2. 1 PublicationVSP_026465
    Alternative sequencei624 – 63815STFDS…PLALD → VRETEESMNHDHQQS in isoform 2. 1 PublicationVSP_026466Add
    BLAST
    Alternative sequencei639 – 72890Missing in isoform 2. 1 PublicationVSP_026467Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270308 mRNA. Translation: CAB64748.1.
    AL049483 Genomic DNA. Translation: CAB39679.1. Sequence problems.
    AL161564 Genomic DNA. Translation: CAB79469.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85162.1.
    CP002687 Genomic DNA. Translation: AEE85163.1.
    AY099612 mRNA. Translation: AAM20463.1.
    BT000267 mRNA. Translation: AAN15586.1.
    PIRiT04269.
    RefSeqiNP_194344.2. NM_118747.2. [Q9SCV0-2]
    NP_849553.1. NM_179222.1. [Q9SCV0-1]
    UniGeneiAt.2962.

    Genome annotation databases

    EnsemblPlantsiAT4G26140.1; AT4G26140.1; AT4G26140. [Q9SCV0-1]
    GeneIDi828720.
    KEGGiath:AT4G26140.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270308 mRNA. Translation: CAB64748.1 .
    AL049483 Genomic DNA. Translation: CAB39679.1 . Sequence problems.
    AL161564 Genomic DNA. Translation: CAB79469.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85162.1 .
    CP002687 Genomic DNA. Translation: AEE85163.1 .
    AY099612 mRNA. Translation: AAM20463.1 .
    BT000267 mRNA. Translation: AAN15586.1 .
    PIRi T04269.
    RefSeqi NP_194344.2. NM_118747.2. [Q9SCV0-2 ]
    NP_849553.1. NM_179222.1. [Q9SCV0-1 ]
    UniGenei At.2962.

    3D structure databases

    ProteinModelPortali Q9SCV0.
    SMRi Q9SCV0. Positions 29-726.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9SCV0.
    PRIDEi Q9SCV0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G26140.1 ; AT4G26140.1 ; AT4G26140 . [Q9SCV0-1 ]
    GeneIDi 828720.
    KEGGi ath:AT4G26140.

    Organism-specific databases

    GeneFarmi 514. 90.
    TAIRi AT4G26140.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000239919.
    InParanoidi Q9SCV0.
    OMAi NSIINTC.
    PhylomeDBi Q9SCV0.

    Enzyme and pathway databases

    BioCyci ARA:AT4G26140-MONOMER.
    ARA:GQT-2664-MONOMER.

    Gene expression databases

    Genevestigatori Q9SCV0.

    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.
    [Graphical view ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF02837. Glyco_hydro_2_N. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SUPFAMi SSF49785. SSF49785. 3 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 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] (ISOFORM 1).
    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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
    5. "Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana."
      Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.
      Plant Cell Physiol. 47:55-63(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "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 nameiBGA12_ARATH
    AccessioniPrimary (citable) accession number: Q9SCV0
    Secondary accession number(s): Q8LPL0, Q9SZI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 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