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Q9SCV9

- BGAL3_ARATH

UniProt

Q9SCV9 - BGAL3_ARATH

Protein

Beta-galactosidase 3

Gene

BGAL3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (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 sitei189 – 1891Proton donorSequence Analysis
    Active sitei258 – 2581NucleophileSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT4G36360-MONOMER.
    ARA:GQT-587-MONOMER.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase 3 (EC:3.2.1.23)
    Short name:
    Lactase 3
    Gene namesi
    Name:BGAL3
    Ordered Locus Names:At4g36360
    ORF Names:C7A10.1000, F23E13.200
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G36360.

    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 – 856825Beta-galactosidase 3PRO_0000293091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9SCV9.
    PRIDEiQ9SCV9.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9SCV9.
    GenevestigatoriQ9SCV9.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRL1Q9ZPS91EBI-2294048,EBI-2292728

    Protein-protein interaction databases

    IntActiQ9SCV9. 1 interaction.
    STRINGi3702.AT4G36360.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SCV9.
    SMRiQ9SCV9. Positions 33-735.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini760 – 84687SUEL-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.
    InParanoidiQ9SCV9.
    OMAiQTSQMEM.
    PhylomeDBiQ9SCV9.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    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.
    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]

    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: Q9SCV9-1) [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

    MREMGTGDSA SRLILWFCLG FLILGVGFVQ CGVTYDRKAL LINGQRRILF    50
    SGSIHYPRST PDMWEDLIQK AKDGGIDVIE TYVFWNLHEP SPGKYDFEGR 100
    NDLVRFVKTI HKAGLYAHLR IGPYVCAEWN FGGFPVWLKY VPGISFRTDN 150
    EPFKRAMKGF TERIVELMKS ENLFESQGGP IILSQIENEY GRQGQLLGAE 200
    GHNYMTWAAK MAIATETGVP WVMCKEDDAP DPVINTCNGF YCDSFAPNKP 250
    YKPLIWTEAW SGWFTEFGGP MHHRPVQDLA FGVARFIQKG GSFVNYYMYH 300
    GGTNFGRTAG GPFVTTSYDY DAPIDEYGLI RQPKYGHLKE LHRAIKMCEK 350
    ALVSADPVVT SIGNKQQAHV YSAESGDCSA FLANYDTESA ARVLFNNVHY 400
    NLPPWSISIL PDCRNAVFNT AKVGVQTSQM EMLPTDTKNF QWESYLEDLS 450
    SLDDSSTFTT HGLLEQINVT RDTSDYLWYM TSVDIGDSES FLHGGELPTL 500
    IIQSTGHAVH IFVNGQLSGS AFGTRQNRRF TYQGKINLHS GTNRIALLSV 550
    AVGLPNVGGH FESWNTGILG PVALHGLSQG KMDLSWQKWT YQVGLKGEAM 600
    NLAFPTNTPS IGWMDASLTV QKPQPLTWHK TYFDAPEGNE PLALDMEGMG 650
    KGQIWVNGES IGRYWTAFAT GDCSHCSYTG TYKPNKCQTG CGQPTQRWYH 700
    VPRAWLKPSQ NLLVIFEELG GNPSTVSLVK RSVSGVCAEV SEYHPNIKNW 750
    QIESYGKGQT FHRPKVHLKC SPGQAIASIK FASFGTPLGT CGSYQQGECH 800
    AATSYAILER KCVGKARCAV TISNSNFGKD PCPNVLKRLT VEAVCAPETS 850
    VSTWRP 856
    Length:856
    Mass (Da):95,193
    Last modified:May 1, 2000 - v1
    Checksum:i245C03A09493C785
    GO
    Isoform 2 (identifier: Q9SCV9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         811-811: Missing.

    Note: Derived from EST data. May be due to a competing acceptor splice site. No experimental confirmation available.

    Show »
    Length:855
    Mass (Da):95,065
    Checksum:i7314CADC0D9A9E1A
    GO

    Sequence cautioni

    The sequence CAB16852.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB80302.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA18137.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti656 – 6561V → L in CAA85537. 1 PublicationCurated
    Sequence conflicti683 – 6831K → L in CAA85537. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei811 – 8111Missing in isoform 2. CuratedVSP_027466

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270299 mRNA. Translation: CAB64739.1.
    Z99708 Genomic DNA. Translation: CAB16852.1. Different initiation.
    AL022141 Genomic DNA. Translation: CAA18137.1. Sequence problems.
    AL161589 Genomic DNA. Translation: CAB80302.1. Different initiation.
    CP002687 Genomic DNA. Translation: AEE86646.1.
    CP002687 Genomic DNA. Translation: AEE86647.1.
    AY056285 mRNA. Translation: AAL07134.1.
    AY091432 mRNA. Translation: AAM14371.1.
    AK230040 mRNA. Translation: BAF01862.1.
    Z37275 mRNA. Translation: CAA85537.1.
    PIRiB85429.
    T04600.
    RefSeqiNP_568001.1. NM_119799.3. [Q9SCV9-1]
    NP_849506.1. NM_179175.2. [Q9SCV9-2]
    UniGeneiAt.703.

    Genome annotation databases

    EnsemblPlantsiAT4G36360.1; AT4G36360.1; AT4G36360. [Q9SCV9-1]
    GeneIDi829788.
    KEGGiath:AT4G36360.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270299 mRNA. Translation: CAB64739.1 .
    Z99708 Genomic DNA. Translation: CAB16852.1 . Different initiation.
    AL022141 Genomic DNA. Translation: CAA18137.1 . Sequence problems.
    AL161589 Genomic DNA. Translation: CAB80302.1 . Different initiation.
    CP002687 Genomic DNA. Translation: AEE86646.1 .
    CP002687 Genomic DNA. Translation: AEE86647.1 .
    AY056285 mRNA. Translation: AAL07134.1 .
    AY091432 mRNA. Translation: AAM14371.1 .
    AK230040 mRNA. Translation: BAF01862.1 .
    Z37275 mRNA. Translation: CAA85537.1 .
    PIRi B85429.
    T04600.
    RefSeqi NP_568001.1. NM_119799.3. [Q9SCV9-1 ]
    NP_849506.1. NM_179175.2. [Q9SCV9-2 ]
    UniGenei At.703.

    3D structure databases

    ProteinModelPortali Q9SCV9.
    SMRi Q9SCV9. Positions 33-735.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9SCV9. 1 interaction.
    STRINGi 3702.AT4G36360.1-P.

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9SCV9.
    PRIDEi Q9SCV9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G36360.1 ; AT4G36360.1 ; AT4G36360 . [Q9SCV9-1 ]
    GeneIDi 829788.
    KEGGi ath:AT4G36360.

    Organism-specific databases

    GeneFarmi 491. 90.
    TAIRi AT4G36360.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000239919.
    InParanoidi Q9SCV9.
    OMAi QTSQMEM.
    PhylomeDBi Q9SCV9.

    Enzyme and pathway databases

    BioCyci ARA:AT4G36360-MONOMER.
    ARA:GQT-587-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SCV9.
    Genevestigatori Q9SCV9.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    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.
    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] (ISOFORM 1).
    2. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
      Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
      , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
      Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. "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.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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 1).
      Strain: cv. Columbia.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-856 (ISOFORM 1).
      Strain: cv. Columbia.
    7. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
      Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-740.
      Strain: cv. Columbia.
      Tissue: Green siliques.
    8. "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: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGAL3_ARATH
    AccessioniPrimary (citable) accession number: Q9SCV9
    Secondary accession number(s): O23243
    , Q0WLZ5, Q42150, Q42317
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 100 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