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Q9SE50

- BGL18_ARATH

UniProt

Q9SE50 - BGL18_ARATH

Protein

Beta-D-glucopyranosyl abscisate beta-glucosidase

Gene

BGLU18

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level.2 Publications

    Catalytic activityi

    D-glucopyranosyl abscisate + H2O = D-glucose + abscisate.1 Publication

    Kineticsi

    1. KM=0.41 mM for ABA-beta-D-glucopyranosyl ester1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei58 – 581SubstrateBy similarity
    Binding sitei161 – 1611SubstrateBy similarity
    Binding sitei206 – 2061SubstrateBy similarity
    Active sitei207 – 2071Proton donorCurated
    Binding sitei351 – 3511SubstrateBy similarity
    Active sitei422 – 4221NucleophileBy similarity
    Binding sitei473 – 4731SubstrateBy similarity

    GO - Molecular functioni

    1. abscisic acid glucose ester beta-glucosidase activity Source: TAIR
    2. beta-glucosidase activity Source: UniProtKB
    3. identical protein binding Source: TAIR

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
    2. abscisic acid metabolic process Source: TAIR
    3. carbohydrate metabolic process Source: InterPro
    4. defense response to fungus Source: TAIR
    5. positive regulation of abscisic acid-activated signaling pathway Source: UniProtKB
    6. protein polymerization Source: UniProtKB
    7. regulation of stomatal movement Source: UniProtKB
    8. response to abiotic stimulus Source: UniProtKB
    9. response to abscisic acid Source: UniProtKB
    10. response to insect Source: TAIR
    11. response to salt stress Source: TAIR
    12. response to water deprivation Source: TAIR
    13. water homeostasis Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Abscisic acid signaling pathway

    Enzyme and pathway databases

    BioCyciARA:AT1G52400-MONOMER.
    ARA:GQT-1542-MONOMER.
    ARA:GQT-1543-MONOMER.
    MetaCyc:AT1G52400-MONOMER.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-D-glucopyranosyl abscisate beta-glucosidase (EC:3.2.1.175)
    Alternative name(s):
    Beta-glucosidase 1
    Short name:
    AtBG1
    Beta-glucosidase 18
    Short name:
    AtBGLU18
    Beta-glucosidase homolog 1
    Gene namesi
    Name:BGLU18
    Synonyms:BG1, BGL1
    Ordered Locus Names:At1g52400
    ORF Names:F19K6.15
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G52400.

    Subcellular locationi

    Endoplasmic reticulum lumen 2 PublicationsPROSITE-ProRule annotation
    Note: Located in ER bodies.

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. endoplasmic reticulum Source: TAIR
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. ER body Source: TAIR
    5. nucleus Source: TAIR
    6. peroxisome Source: TAIR
    7. plasmodesma Source: TAIR
    8. vacuole Source: TAIR

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Reduced growth, yellow leaf, defective stomatal closure in the dark, increased transpirational water loss, sensitive response to dehydration, lower germination efficiency and decreased ABA levels.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi207 – 2071E → Q: Loss of activity towards ABA-GE. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 528502Beta-D-glucopyranosyl abscisate beta-glucosidasePRO_0000011766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi226 ↔ 237By similarity
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9SE50.
    PRIDEiQ9SE50.

    2D gel databases

    SWISS-2DPAGEQ9SE50.

    Expressioni

    Tissue specificityi

    Seeds and hydathodes of rosette and cauline leaves.1 Publication

    Inductioni

    By ABA, dehydration, wounding and salt treatment.3 Publications

    Gene expression databases

    ArrayExpressiQ9SE50.
    GenevestigatoriQ9SE50.

    Interactioni

    Protein-protein interaction databases

    BioGridi26895. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SE50.
    SMRiQ9SE50. Positions 40-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni480 – 4812Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi525 – 5284Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SE50.
    KOiK15748.
    OMAiHEIDAEN.
    PhylomeDBiQ9SE50.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 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: Q9SE50-1) [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

    MVRFEKVHLV LGLALVLTLV GAPTKAQGPV CGAGLPDKFS RLNFPEGFIW    50
    GTATAAFQVE GAVNEGCRGP SMWDTFTKKF PHRCENHNAD VAVDFYHRYK 100
    EDIQLMKDLN TDAFRLSIAW PRIFPHGRMS KGISKVGVQF YHDLIDELLK 150
    NNIIPLVTVF HWDTPQDLED EYGGFLSGRI VQDFTEYANF TFHEYGHKVK 200
    HWITFNEPWV FSRAGYDNGK KAPGRCSPYI PGYGQHCQDG RSGYEAYQVS 250
    HNLLLSHAYA VDAFRNCKQC AGGKIGIAHS PAWFEPQDLE HVGGSIERVL 300
    DFILGWHLAP TTYGDYPQSM KDRVGHRLPK FTEAEKKLLK GSTDYVGMNY 350
    YTSVFAKEIS PDPKSPSWTT DSLVDWDSKS VDGYKIGSKP FNGKLDVYSK 400
    GLRYLLKYIK DNYGDPEVII AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ 450
    RHLLSMHDAI CKDKVNVTGY FVWSLMDNFE WQDGYKARFG LYYIDFQNNL 500
    TRHQKVSGKW YSEFLKPQFP TSKLREEL 528
    Length:528
    Mass (Da):60,459
    Last modified:February 5, 2008 - v2
    Checksum:iF148D04C0A6F27B8
    GO
    Isoform 2 (identifier: Q9SE50-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         461-461: C → W
         462-528: Missing.

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:461
    Mass (Da):52,371
    Checksum:iA83D86C9F943776D
    GO

    Sequence cautioni

    The sequence BAD94819.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341S → N in AAF22295. 1 PublicationCurated
    Sequence conflicti210 – 2101V → G in AAN60329. 1 PublicationCurated
    Sequence conflicti214 – 2141A → V in AAN60329. 1 PublicationCurated
    Sequence conflicti253 – 2531L → S in AAN31804. 1 PublicationCurated
    Sequence conflicti266 – 2661N → K in CAC19786. (PubMed:11080278)Curated
    Sequence conflicti266 – 2661N → K in AAN60329. 1 PublicationCurated
    Sequence conflicti365 – 3651S → N in CAC19786. (PubMed:11080278)Curated
    Sequence conflicti431 – 4311E → G in BAD94819. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei461 – 4611C → W in isoform 2. CuratedVSP_041996
    Alternative sequencei462 – 52867Missing in isoform 2. CuratedVSP_041997Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251301 mRNA. Translation: CAC19786.1.
    AF183827 mRNA. Translation: AAF22295.1.
    AC037424 Genomic DNA. Translation: AAG51546.1.
    CP002684 Genomic DNA. Translation: AEE32799.1.
    CP002684 Genomic DNA. Translation: AEE32800.1.
    CP002684 Genomic DNA. Translation: AEE32801.1.
    AY039855 mRNA. Translation: AAK63959.1.
    AY056415 mRNA. Translation: AAL08271.1.
    BT000515 mRNA. Translation: AAN18084.1.
    BT000657 mRNA. Translation: AAN31804.1.
    AF083771 mRNA. Translation: AAN60329.1.
    AK222051 mRNA. Translation: BAD94819.1. Different initiation.
    PIRiC96564.
    RefSeqiNP_001031175.1. NM_001036098.2. [Q9SE50-2]
    NP_001185204.1. NM_001198275.1. [Q9SE50-1]
    NP_175649.1. NM_104118.2. [Q9SE50-1]
    UniGeneiAt.24169.

    Genome annotation databases

    EnsemblPlantsiAT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
    AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
    GeneIDi841670.
    KEGGiath:AT1G52400.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251301 mRNA. Translation: CAC19786.1 .
    AF183827 mRNA. Translation: AAF22295.1 .
    AC037424 Genomic DNA. Translation: AAG51546.1 .
    CP002684 Genomic DNA. Translation: AEE32799.1 .
    CP002684 Genomic DNA. Translation: AEE32800.1 .
    CP002684 Genomic DNA. Translation: AEE32801.1 .
    AY039855 mRNA. Translation: AAK63959.1 .
    AY056415 mRNA. Translation: AAL08271.1 .
    BT000515 mRNA. Translation: AAN18084.1 .
    BT000657 mRNA. Translation: AAN31804.1 .
    AF083771 mRNA. Translation: AAN60329.1 .
    AK222051 mRNA. Translation: BAD94819.1 . Different initiation.
    PIRi C96564.
    RefSeqi NP_001031175.1. NM_001036098.2. [Q9SE50-2 ]
    NP_001185204.1. NM_001198275.1. [Q9SE50-1 ]
    NP_175649.1. NM_104118.2. [Q9SE50-1 ]
    UniGenei At.24169.

    3D structure databases

    ProteinModelPortali Q9SE50.
    SMRi Q9SE50. Positions 40-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 26895. 1 interaction.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    2D gel databases

    SWISS-2DPAGE Q9SE50.

    Proteomic databases

    PaxDbi Q9SE50.
    PRIDEi Q9SE50.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G52400.1 ; AT1G52400.1 ; AT1G52400 . [Q9SE50-1 ]
    AT1G52400.3 ; AT1G52400.3 ; AT1G52400 . [Q9SE50-1 ]
    GeneIDi 841670.
    KEGGi ath:AT1G52400.

    Organism-specific databases

    TAIRi AT1G52400.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    InParanoidi Q9SE50.
    KOi K15748.
    OMAi HEIDAEN.
    PhylomeDBi Q9SE50.

    Enzyme and pathway databases

    BioCyci ARA:AT1G52400-MONOMER.
    ARA:GQT-1542-MONOMER.
    ARA:GQT-1543-MONOMER.
    MetaCyc:AT1G52400-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SE50.
    Genevestigatori Q9SE50.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Induced plant defense responses against chewing insects. Ethylene signaling reduces resistance of Arabidopsis against Egyptian cotton worm but not diamondback moth."
      Stotz H.U., Pittendrigh B.R., Kroymann J., Weniger K., Fritsche J., Bauke A., Mitchell-Olds T.
      Plant Physiol. 124:1007-1018(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: cv. Landsberg erecta.
      Tissue: Rosette leaf.
    2. "A transgenic Arabidopsis plant overexpressing an ER localized b-glucosidase homolog that is transcriptionally suppressed by NaCl is hypersensitive to NaCl stress."
      Piao H.L., Hwang I.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [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. "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
      Stracke R., Palme K.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-308.
    7. "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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-528 (ISOFORM 1).
      Strain: cv. Columbia.
    8. Cited for: GENE FAMILY, NOMENCLATURE.
    9. "Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid."
      Lee K.H., Piao H.L., Kim H.-Y., Choi S.M., Jiang F., Hartung W., Hwang I., Kwak J.M., Lee I.-J., Hwang I.
      Cell 126:1109-1120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-207.
    10. "Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-glucosidase in Arabidopsis thaliana."
      Kato-Noguchi H., Tanaka Y.
      J. Plant Physiol. 165:788-790(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases."
      Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N., Hara-Nishimura I., Nishimura M.
      Plant Cell Physiol. 50:480-488(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    12. "The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific beta-glucosidases."
      Yamada K., Nagano A.J., Ogasawara K., Hara-Nishimura I., Nishimura M.
      Plant Signal. Behav. 4:849-852(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

    Entry informationi

    Entry nameiBGL18_ARATH
    AccessioniPrimary (citable) accession number: Q9SE50
    Secondary accession number(s): F4ICX8
    , Q56WI9, Q8H169, Q8H7A3, Q93V63, Q9FNZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Polymerization into higher molecular weight forms displays diurnal fluctuation, similar to the ABA level.

    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