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Q9C8Y9

- BGL22_ARATH

UniProt

Q9C8Y9 - BGL22_ARATH

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Protein

Beta-glucosidase 22

Gene

BGLU22

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

Functioni

Beta-D-glucosidase active on scopolin >> esculin >> 4-MU-glucoside. No activity with DIMBOA-glucoside, pNP-glucoside, oNP-glucoside and sinigrin as substrates.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Enzyme regulationi

Activated upon binding to PBP1 or PBP2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551SubstrateBy similarity
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei203 – 2031SubstrateBy similarity
Active sitei204 – 2041Proton donorBy similarity
Binding sitei346 – 3461SubstrateBy similarity
Active sitei418 – 4181NucleophileBy similarity
Binding sitei468 – 4681SubstrateBy similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: TAIR

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cellular response to cold Source: TAIR
  3. cellular response to salt stress Source: TAIR
  4. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT1G66280-MONOMER.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase 22 (EC:3.2.1.21)
Short name:
AtBGLU22
Gene namesi
Name:BGLU22
Ordered Locus Names:At1g66280
ORF Names:T27F4.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G66280.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
  2. membrane Source: TAIR
  3. plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 524500Beta-glucosidase 22PRO_0000389584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi223 ↔ 230By similarity
Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9C8Y9.
PRIDEiQ9C8Y9.

Expressioni

Tissue specificityi

Expressed exclusively in roots.1 Publication

Inductioni

Up-regulated by salt, 2,4-D and methyl jasmonate. Down-regulated by cold and manitol.1 Publication

Gene expression databases

GenevestigatoriQ9C8Y9.

Interactioni

Subunit structurei

Component of the PYK10 complex, at least composed of PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31, JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.1 Publication

Protein-protein interaction databases

IntActiQ9C8Y9. 3 interactions.
STRINGi3702.AT1G66280.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9C8Y9.
SMRiQ9C8Y9. Positions 34-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni475 – 4762Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi521 – 5244Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiQ9C8Y9.
KOiK01188.
OMAiWIPLNEP.
PhylomeDBiQ9C8Y9.

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: Q9C8Y9-1) [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
MALQKFPLLG LLFLITIVVS STIAVDDPVC PTTSKLSRAS FPNGFVFGTA
60 70 80 90 100
TAAFQVEGAI NETCRGPALW DIFCKRNPER CSGHNADVAV DFFHRYKEDI
110 120 130 140 150
QLMKNLNTDA FRLSIAWSRI FPHGRKEKGV SQAGVKFYHD LIDELLKNGI
160 170 180 190 200
IPFVTVFHWD TPQDLEDEYG GFLSENIVKD FREYADYVFT EYGGKVKNWI
210 220 230 240 250
TFNEPWVFAH AGYDVGKKAP GRCSRYLKGC EDRDGRSGYE AYLVSHNLLN
260 270 280 290 300
AHAEAVEVFR QKVKGGKIGI AHSPAWFEPH DLKDSNDVPT VSRVLDFMLG
310 320 330 340 350
WHLDPTTFGD YPQIMKDLLG HRLPKFTSSQ KAKLKDSTDF VGLNYYTSTF
360 370 380 390 400
SNHNEKPDPS TPSWKQDSLV AWEPKNVDHS AIGSQPLTAA LPVYAKGFRS
410 420 430 440 450
LLKYIKDKYA NPEIMIMENG YGDKLKDKDS VEVGTADYNR KYYLQRHLLA
460 470 480 490 500
MNEAICIDKV RVTGYFVWSL LDNFEWQDGY NNRFGLYYVD FKNNLTRYEK
510 520
ESAKYYKDFL GQGVRPSALK KDEL
Length:524
Mass (Da):59,781
Last modified:June 1, 2001 - v1
Checksum:iB05574AECFC56C41
GO
Isoform 2 (identifier: Q9C8Y9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     456-456: C → W
     457-524: Missing.

Note: No experimental confirmation available.

Show »
Length:456
Mass (Da):51,669
Checksum:i88D47178B41A2E9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801H → R in BAH56964. (PubMed:14593172)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei456 – 4561C → W in isoform 2. 1 PublicationVSP_038458
Alternative sequencei457 – 52468Missing in isoform 2. 1 PublicationVSP_038459Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC020665 Genomic DNA. Translation: AAG52159.1.
CP002684 Genomic DNA. Translation: AEE34490.1.
AY074378 mRNA. Translation: AAL67074.1.
AK318849 mRNA. Translation: BAH56964.1.
PIRiH96687.
RefSeqiNP_176802.1. NM_105299.2. [Q9C8Y9-1]
UniGeneiAt.47576.
At.75574.

Genome annotation databases

EnsemblPlantsiAT1G66280.1; AT1G66280.1; AT1G66280. [Q9C8Y9-1]
GeneIDi842945.
KEGGiath:AT1G66280.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC020665 Genomic DNA. Translation: AAG52159.1 .
CP002684 Genomic DNA. Translation: AEE34490.1 .
AY074378 mRNA. Translation: AAL67074.1 .
AK318849 mRNA. Translation: BAH56964.1 .
PIRi H96687.
RefSeqi NP_176802.1. NM_105299.2. [Q9C8Y9-1 ]
UniGenei At.47576.
At.75574.

3D structure databases

ProteinModelPortali Q9C8Y9.
SMRi Q9C8Y9. Positions 34-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9C8Y9. 3 interactions.
STRINGi 3702.AT1G66280.1-P.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbi Q9C8Y9.
PRIDEi Q9C8Y9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G66280.1 ; AT1G66280.1 ; AT1G66280 . [Q9C8Y9-1 ]
GeneIDi 842945.
KEGGi ath:AT1G66280.

Organism-specific databases

TAIRi AT1G66280.

Phylogenomic databases

eggNOGi COG2723.
HOGENOMi HOG000088630.
InParanoidi Q9C8Y9.
KOi K01188.
OMAi WIPLNEP.
PhylomeDBi Q9C8Y9.

Enzyme and pathway databases

BioCyci ARA:AT1G66280-MONOMER.

Gene expression databases

Genevestigatori Q9C8Y9.

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

« Hide 'large scale' publications
  1. "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.
  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. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  5. Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana."
    Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.
    Plant Cell Physiol. 49:969-980(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PYK10 COMPLEX.
  7. "Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis."
    Ahn Y.O., Shimizu B., Sakata K., Gantulga D., Zhou C., Zhou Z., Bevan D.R., Esen A.
    Plant Cell Physiol. 51:132-143(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiBGL22_ARATH
AccessioniPrimary (citable) accession number: Q9C8Y9
Secondary accession number(s): C0Z2N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 91 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