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Q9M088

- E135_ARATH

UniProt

Q9M088 - E135_ARATH

Protein

Glucan endo-1,3-beta-glucosidase 5

Gene

At4g31140

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei267 – 2671NucleophileBy similarity
    Active sitei328 – 3281Proton donorBy similarity

    GO - Molecular functioni

    1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. defense response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Plant defense

    Enzyme and pathway databases

    BioCyciARA:AT4G31140-MONOMER.

    Protein family/group databases

    CAZyiCBM43. Carbohydrate-Binding Module Family 43.
    GH17. Glycoside Hydrolase Family 17.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan endo-1,3-beta-glucosidase 5 (EC:3.2.1.39)
    Alternative name(s):
    (1->3)-beta-glucan endohydrolase 5
    Short name:
    (1->3)-beta-glucanase 5
    Beta-1,3-endoglucanase 5
    Short name:
    Beta-1,3-glucanase 5
    Gene namesi
    Ordered Locus Names:At4g31140
    ORF Names:F6E21.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G31140.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: TAIR
    2. anchored component of plasma membrane Source: TAIR
    3. plant-type cell wall Source: TAIR
    4. plasma membrane Source: TAIR
    5. plasmodesma Source: TAIR
    6. vacuole Source: TAIR

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 461435Glucan endo-1,3-beta-glucosidase 5PRO_0000011890Add
    BLAST
    Propeptidei462 – 48423Removed in mature formSequence AnalysisPRO_0000011891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi366 ↔ 428By similarity
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
    Lipidationi461 – 4611GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    Contains two additional disulfide bonds.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ9M088.
    PRIDEiQ9M088.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9M088.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M088.
    SMRiQ9M088. Positions 27-346, 362-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG247729.
    HOGENOMiHOG000238221.
    InParanoidiQ9M088.
    OMAiLAKKWCI.
    PhylomeDBiQ9M088.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012946. X8.
    [Graphical view]
    PfamiPF00332. Glyco_hydro_17. 1 hit.
    PF07983. X8. 1 hit.
    [Graphical view]
    SMARTiSM00768. X8. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9M088-1 [UniParc]FASTAAdd to Basket

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    MLFKGVFAVF FVITLLYASL LIEVEGIGVN WGSQARHPLP PATVVRLLRE    50
    NGIQKVKLFE ADSAILKALS RTGIQVMVGI PNDLLAPLAG SVAAAERWVS 100
    QNVSAHVSSN GVDIRYVAVG NEPFLKAFNG TFEGITLPAL QNIQSAIIKA 150
    GLATQVKVTV PLNADVYQSA SNLPSDGDFR PEIRDLMLNI VKFLSDNGAP 200
    FTINIYPFIS LYNDPNFPVE FAFFDGTGTP INDNGRIYDN VLDANYDTLV 250
    WSLQKNGFGN LTIIVGEVGW PTDGDKNANL MYARRYNQGF MNRQKANKGT 300
    PMRPGAMDAY LFGLIDEDAK SIQPGNFERH WGIFYIDGQP KYQLSLGSGN 350
    GLIPAKDVHY LAKKWCILAP NANLQDPQLG PSVSYACDHA DCTSLGYGSS 400
    CGNLNLAQNV SYAFNSYYQV SNQLDSACKF PGLSIVSTRD PSVGSCKFKI 450
    MIKSEDASEA SAMMPITRST AVLLLLSICL YIVL 484
    Length:484
    Mass (Da):52,715
    Last modified:October 1, 2000 - v1
    Checksum:i471AF128AEDCBA2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161578 Genomic DNA. Translation: CAB79832.1.
    CP002687 Genomic DNA. Translation: AEE85864.1.
    AK229398 mRNA. Translation: BAF01260.1.
    PIRiT10668.
    RefSeqiNP_194843.1. NM_119264.4.
    UniGeneiAt.31769.

    Genome annotation databases

    EnsemblPlantsiAT4G31140.1; AT4G31140.1; AT4G31140.
    GeneIDi829242.
    KEGGiath:AT4G31140.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161578 Genomic DNA. Translation: CAB79832.1 .
    CP002687 Genomic DNA. Translation: AEE85864.1 .
    AK229398 mRNA. Translation: BAF01260.1 .
    PIRi T10668.
    RefSeqi NP_194843.1. NM_119264.4.
    UniGenei At.31769.

    3D structure databases

    ProteinModelPortali Q9M088.
    SMRi Q9M088. Positions 27-346, 362-448.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM43. Carbohydrate-Binding Module Family 43.
    GH17. Glycoside Hydrolase Family 17.

    Proteomic databases

    PaxDbi Q9M088.
    PRIDEi Q9M088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G31140.1 ; AT4G31140.1 ; AT4G31140 .
    GeneIDi 829242.
    KEGGi ath:AT4G31140.

    Organism-specific databases

    TAIRi AT4G31140.

    Phylogenomic databases

    eggNOGi NOG247729.
    HOGENOMi HOG000238221.
    InParanoidi Q9M088.
    OMAi LAKKWCI.
    PhylomeDBi Q9M088.

    Enzyme and pathway databases

    BioCyci ARA:AT4G31140-MONOMER.

    Gene expression databases

    Genevestigatori Q9M088.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012946. X8.
    [Graphical view ]
    Pfami PF00332. Glyco_hydro_17. 1 hit.
    PF07983. X8. 1 hit.
    [Graphical view ]
    SMARTi SM00768. X8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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].
      Strain: cv. Columbia.
    4. "Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis."
      Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P.
      Plant Physiol. 132:568-577(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
      Tissue: Callus.
    5. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
      Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
      Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    6. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
      Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
      J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiE135_ARATH
    AccessioniPrimary (citable) accession number: Q9M088
    Secondary accession number(s): Q0WNN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 101 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