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Protein

Beta-D-glucopyranosyl abscisate beta-glucosidase

Gene

BGLU18

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    • abscisic acid glucose ester beta-glucosidase activity Source: TAIR
    • beta-glucosidase activity Source: UniProtKB
    • identical protein binding Source: TAIR

    GO - Biological processi

    • abscisic acid-activated signaling pathway Source: UniProtKB-KW
    • abscisic acid metabolic process Source: TAIR
    • carbohydrate metabolic process Source: InterPro
    • defense response to fungus Source: TAIR
    • positive regulation of abscisic acid-activated signaling pathway Source: UniProtKB
    • protein polymerization Source: UniProtKB
    • regulation of stomatal movement Source: UniProtKB
    • response to abiotic stimulus Source: UniProtKB
    • response to abscisic acid Source: UniProtKB
    • response to insect Source: TAIR
    • response to salt stress Source: TAIR
    • response to water deprivation Source: TAIR
    • water homeostasis Source: UniProtKB
    Complete GO annotation...

    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.
    BRENDAi3.2.1.175. 399.

    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 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G52400.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • endoplasmic reticulum Source: TAIR
    • endoplasmic reticulum lumen Source: UniProtKB-SubCell
    • ER body Source: TAIR
    • nucleus Source: TAIR
    • peroxisome Source: TAIR
    • plasmodesma Source: TAIR
    • vacuole Source: TAIR
    Complete GO annotation...

    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

    ExpressionAtlasiQ9SE50. baseline and differential.

    Interactioni

    Protein-protein interaction databases

    BioGridi26895. 1 interaction.
    STRINGi3702.AT1G52400.1.

    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.
    OMAiEQQPNPQ.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MVRFEKVHLV LGLALVLTLV GAPTKAQGPV CGAGLPDKFS RLNFPEGFIW
    60 70 80 90 100
    GTATAAFQVE GAVNEGCRGP SMWDTFTKKF PHRCENHNAD VAVDFYHRYK
    110 120 130 140 150
    EDIQLMKDLN TDAFRLSIAW PRIFPHGRMS KGISKVGVQF YHDLIDELLK
    160 170 180 190 200
    NNIIPLVTVF HWDTPQDLED EYGGFLSGRI VQDFTEYANF TFHEYGHKVK
    210 220 230 240 250
    HWITFNEPWV FSRAGYDNGK KAPGRCSPYI PGYGQHCQDG RSGYEAYQVS
    260 270 280 290 300
    HNLLLSHAYA VDAFRNCKQC AGGKIGIAHS PAWFEPQDLE HVGGSIERVL
    310 320 330 340 350
    DFILGWHLAP TTYGDYPQSM KDRVGHRLPK FTEAEKKLLK GSTDYVGMNY
    360 370 380 390 400
    YTSVFAKEIS PDPKSPSWTT DSLVDWDSKS VDGYKIGSKP FNGKLDVYSK
    410 420 430 440 450
    GLRYLLKYIK DNYGDPEVII AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ
    460 470 480 490 500
    RHLLSMHDAI CKDKVNVTGY FVWSLMDNFE WQDGYKARFG LYYIDFQNNL
    510 520
    TRHQKVSGKW YSEFLKPQFP TSKLREEL
    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. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341S → N in AAF22295 (Ref. 2) Curated
    Sequence conflicti210 – 2101V → G in AAN60329 (Ref. 6) Curated
    Sequence conflicti214 – 2141A → V in AAN60329 (Ref. 6) Curated
    Sequence conflicti253 – 2531L → S in AAN31804 (Ref. 6) Curated
    Sequence conflicti266 – 2661N → K in CAC19786 (PubMed:11080278).Curated
    Sequence conflicti266 – 2661N → K in AAN60329 (Ref. 6) Curated
    Sequence conflicti365 – 3651S → N in CAC19786 (PubMed:11080278).Curated
    Sequence conflicti431 – 4311E → G in BAD94819 (Ref. 7) Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi26895. 1 interaction.
    STRINGi3702.AT1G52400.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    2D gel databases

    SWISS-2DPAGEQ9SE50.

    Proteomic databases

    PaxDbiQ9SE50.
    PRIDEiQ9SE50.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT1G52400.

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SE50.
    KOiK15748.
    OMAiEQQPNPQ.
    PhylomeDBiQ9SE50.

    Enzyme and pathway databases

    BioCyciARA:AT1G52400-MONOMER.
    ARA:GQT-1542-MONOMER.
    ARA:GQT-1543-MONOMER.
    MetaCyc:AT1G52400-MONOMER.
    BRENDAi3.2.1.175. 399.

    Miscellaneous databases

    PROiQ9SE50.

    Gene expression databases

    ExpressionAtlasiQ9SE50. baseline and differential.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 113 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.