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Q8VYE5

- E1312_ARATH

UniProt

Q8VYE5 - E1312_ARATH

Protein

Glucan endo-1,3-beta-glucosidase 12

Gene

At4g29360

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 84 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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 sitei264 – 2641NucleophileBy similarity
    Active sitei327 – 3271NucleophileBy 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

    Cell wall biogenesis/degradation, Plant defense

    Enzyme and pathway databases

    BioCyciARA:AT4G29360-MONOMER.
    ARA:GQT-165-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 12 (EC:3.2.1.39)
    Alternative name(s):
    (1->3)-beta-glucan endohydrolase 12
    Short name:
    (1->3)-beta-glucanase 12
    Beta-1,3-endoglucanase 12
    Short name:
    Beta-1,3-glucanase 12
    Gene namesi
    Ordered Locus Names:At4g29360
    ORF Names:F17A13.180
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29360.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: TAIR
    2. anchored component of plasma membrane Source: TAIR
    3. cell wall Source: UniProtKB-SubCell
    4. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Cell wall, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 507483Glucan endo-1,3-beta-glucosidase 12PRO_0000251271Add
    BLAST
    Propeptidei508 – 53427Removed in mature formSequence AnalysisPRO_0000251272Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi392 ↔ 455By similarity
    Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
    Lipidationi507 – 5071GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    Contains two additional disulfide bonds.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ8VYE5.
    PRIDEiQ8VYE5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VYE5.
    GenevestigatoriQ8VYE5.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G29360.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VYE5.
    SMRiQ8VYE5. Positions 27-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi381 – 3877Poly-Gly

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG322041.
    HOGENOMiHOG000238220.
    InParanoidiQ8VYE5.
    OMAiKWCIASS.
    PhylomeDBiQ8VYE5.

    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]

    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: Q8VYE5-1) [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

    MGQRLNLVFW IFVSILAFLN FGMASKIGIC YGRNADNLPS PNRVSELIQH    50
    LNIKFVRIYD ANIDVLKAFA NTGIELMIGV PNADLLAFAQ FQSNVDTWLS 100
    NNILPYYPST KITSISVGLE VTEAPDNATG LVLPAMRNIH TALKKSGLDK 150
    KIKISSSHSL AILSRSFPPS SASFSKKHSA FLKPMLEFLV ENESPFMIDL 200
    YPYYAYRDST EKVPLEYALF ESSSQVVDPA TGLLYSNMFD AQLDAIYFAL 250
    TAMSFKTVKV MVTESGWPSK GSPKETAATP ENALAYNTNL IRHVIGDPGT 300
    PAKPGEEIDV YLFSLFNENR KPGIESERNW GMFYANGTNV YALDFTGENT 350
    TPVSPTNSTT GTSPSPSSSP IINGNSTVTI GGGGGGGTKK WCIASSQASV 400
    TELQTALDWA CGPGNVDCSA VQPDQPCFEP DTVLSHASYA FNTYYQQSGA 450
    SSIDCSFNGA SVEVDKDPSY GNCLYMIAPA TDGFNRTMAG NITGNITAID 500
    SPLASPSSTN EAFRQMVVAV SVLLPCFVVC SSIW 534
    Length:534
    Mass (Da):57,659
    Last modified:March 1, 2002 - v1
    Checksum:iD76C3E1759D4CA59
    GO
    Isoform 2 (identifier: Q8VYE5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         470-494: YGNCLYMIAPATDGFNRTMAGNITG → KYLYTYTFQNTSIKSNVKP

    Note: May be due to an intron retention. No experimental confirmation available.

    Show »
    Length:528
    Mass (Da):57,303
    Checksum:i05558FC6F457FFD3
    GO

    Sequence cautioni

    The sequence CAB79694.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei470 – 49425YGNCL…GNITG → KYLYTYTFQNTSIKSNVKP in isoform 2. 1 PublicationVSP_020753Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161574 Genomic DNA. Translation: CAB79694.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85622.1.
    AY072133 mRNA. Translation: AAL59955.1.
    AY096465 mRNA. Translation: AAM20105.1.
    AY088354 mRNA. Translation: AAM65893.1.
    PIRiF85342.
    RefSeqiNP_567828.3. NM_119081.5.
    NP_849556.1. NM_179225.3. [Q8VYE5-1]
    UniGeneiAt.31933.

    Genome annotation databases

    EnsemblPlantsiAT4G29360.1; AT4G29360.1; AT4G29360. [Q8VYE5-1]
    GeneIDi829057.
    KEGGiath:AT4G29360.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161574 Genomic DNA. Translation: CAB79694.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85622.1 .
    AY072133 mRNA. Translation: AAL59955.1 .
    AY096465 mRNA. Translation: AAM20105.1 .
    AY088354 mRNA. Translation: AAM65893.1 .
    PIRi F85342.
    RefSeqi NP_567828.3. NM_119081.5.
    NP_849556.1. NM_179225.3. [Q8VYE5-1 ]
    UniGenei At.31933.

    3D structure databases

    ProteinModelPortali Q8VYE5.
    SMRi Q8VYE5. Positions 27-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G29360.1-P.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q8VYE5.
    PRIDEi Q8VYE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G29360.1 ; AT4G29360.1 ; AT4G29360 . [Q8VYE5-1 ]
    GeneIDi 829057.
    KEGGi ath:AT4G29360.

    Organism-specific databases

    TAIRi AT4G29360.

    Phylogenomic databases

    eggNOGi NOG322041.
    HOGENOMi HOG000238220.
    InParanoidi Q8VYE5.
    OMAi KWCIASS.
    PhylomeDBi Q8VYE5.

    Enzyme and pathway databases

    BioCyci ARA:AT4G29360-MONOMER.
    ARA:GQT-165-MONOMER.

    Gene expression databases

    ArrayExpressi Q8VYE5.
    Genevestigatori Q8VYE5.

    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. "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.
    4. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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].

    Entry informationi

    Entry nameiE1312_ARATH
    AccessioniPrimary (citable) accession number: Q8VYE5
    Secondary accession number(s): Q8L9M3, Q9M0E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 84 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