Q9SR37 (BGL23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucosidase 23
Short name=AtBGLU23
EC=3.2.1.21

Alternative name(s):
Protein PHOSPHATE STARVATION-RESPONSE 3.1

Gene names

Name:	BGLU23
Synonyms:	PSR3.1, PYK10
Ordered Locus Names:	At3g09260
ORF Names:	F3L24.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May possess beta-D-glucosidase and beta-D-fucosidase activity. Required for the beneficial interaction with the endophytic fungus P.indica. May participate in the control of root colonization by P.indica by repressing defense responses and modulating other responses required for a mutualistic interaction. Ref.9 Ref.11 Ref.12
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Enzyme regulation	Activated by tissue damage. Ref.11
Subunit structure	Homodimers. Binds to the deubiquitinating enzyme AMSH3. The inactive form interacts with PBP1. Ref.11 Ref.14
Subcellular location	Endoplasmic reticulum lumen. Note: Located in ER bodies. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13
Tissue specificity	Highly expressed in roots. Ref.2
Induction	By wounding and methyl jasmonate (MeJA). Ref.11
Post-translational modification	Forms interchain disulfide bonds.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.
Sequence caution	The sequence AAB38783.1 differs from that shown. Reason: Frameshift at positions 56 and 63. The sequence BAD94012.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER body organization Inferred from mutant phenotype PubMed 19906837. Source: TAIR carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular response to cold Inferred from expression pattern PubMed 19965874. Source: TAIR negative regulation of defense response Inferred from mutant phenotype Ref.12. Source: UniProtKB response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR response to symbiotic fungus Inferred from mutant phenotype Ref.12. Source: TAIR
Cellular_component	ER body Inferred from direct assay Ref.8. Source: TAIR endoplasmic reticulum Inferred from direct assay PubMed 22923678. Source: TAIR endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay PubMed 17432890. Source: TAIR nucleus Inferred from direct assay PubMed 14617066. Source: TAIR peroxisome Inferred from direct assay PubMed 17951448. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	beta-glucosidase activity Inferred from direct assay PubMed 18467340PubMed 19965874. Source: TAIR copper ion binding Inferred from direct assay PubMed 16526091. Source: TAIR fucosidase activity Traceable author statement Ref.11. Source: TAIR protein homodimerization activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Ref.8
	Chain	25 – 524	500	Beta-glucosidase 23		PRO_0000389585
Regions
	Region	475 – 476	2	Substrate binding By similarity
	Motif	521 – 524	4	Prevents secretion from ER Potential
Sites
	Active site	203	1	Proton donor By similarity
	Active site	418	1	Nucleophile By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	346	1	Substrate By similarity
	Binding site	468	1	Substrate By similarity
Amino acid modifications
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
	Glycosylation	494	1	N-linked (GlcNAc...) Potential
	Disulfide bond	222 ↔ 230		By similarity
Experimental info
	Sequence conflict	208	1	S → L in CAB50792. Ref.2
	Sequence conflict	208	1	S → L in CAA61592. Ref.2
	Sequence conflict	222	1	C → S in AAB38783. Ref.1
	Sequence conflict	400	1	S → G in BAD94012. Ref.6
	Sequence conflict	459	1	K → E in BAH20034. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q9SR37 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4758EA7A9B8336E1	FASTA	524	59,721
	10 20 30 40 50 60 MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT AAYQVEGAIN 70 80 90 100 110 120 ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ LMKNLNTDAF RMSIAWPRIF 130 140 150 160 170 180 PHGRKEKGVS QAGVQFYHDL IDELIKNGIT PFVTVFHWDT PQDLEDEYGG FLSERIVKDF 190 200 210 220 230 240 REYADFVFQE YGGKVKHWIT FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY 250 260 270 280 290 300 LVTHNLLISH AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG 310 320 330 340 350 360 WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF SNHLEKPDPS 370 380 390 400 410 420 KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS LLKYIKDKYA NPEIMIMENG 430 440 450 460 470 480 YGEELGASDS VAVGTADHNR KYYLQRHLLS MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY 490 500 510 520 KNRFGLYYVD FKNNLTRYEK ESGKYYKDFL SQGVRPSALK KDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and nucleotide sequences of cDNA clones of phosphate-starvation inducible beta-glucosidase genes of Brassicaceae." Malboobi M.A., Tremblay L., Lefebvre D.D. Plant Gene Register PGR96-114 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Root.
[2]	"Pyk10, a seedling and root specific gene and promoter from Arabidopsis thaliana." Nitz I., Berkefeld H., Puzio P.S., Grundler F.M. Plant Sci. 161:337-346(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Strain: cv. C24.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(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]. Strain: cv. Columbia.
[6]	"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.
[7]	"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]. Strain: cv. Columbia.
[8]	"A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis." Matsushima R., Kondo M., Nishimura M., Hara-Nishimura I. Plant J. 33:493-502(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-41, SUBCELLULAR LOCATION.
[9]	"NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body." Matsushima R., Fukao Y., Nishimura M., Hara-Nishimura I. Plant Cell 16:1536-1549(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1." Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R., Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A. Plant Mol. Biol. 55:343-367(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[11]	"Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana." Nagano A.J., Matsushima R., Hara-Nishimura I. Plant Cell Physiol. 46:1140-1148(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, ENZYME REGULATION, SUBUNIT, DISULFIDE BOND, SUBCELLULAR LOCATION, INTERACTION WITH PBP1. Strain: cv. Columbia.
[12]	"PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and the endophytic fungus Piriformospora indica." Sherameti I., Venus Y., Drzewiecki C., Tripathi S., Dan V.M., Nitz I., Varma A., Grundler F.M., Oelmueller R. Plant J. 54:428-439(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]	"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.
[14]	"The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana." Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C. Plant Cell 22:1826-1837(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AMSH3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U72153 mRNA. Translation: AAB38783.1. Frameshift. X89413 mRNA. Translation: CAA61592.1. AJ243490 Genomic DNA. Translation: CAB50792.1. AC011436 Genomic DNA. Translation: AAF14024.1. CP002686 Genomic DNA. Translation: AEE74744.1. AF386967 mRNA. Translation: AAK62412.1. AY136440 mRNA. Translation: AAM97105.1. AY140060 mRNA. Translation: AAM98201.1. BT000230 mRNA. Translation: AAN15549.1. AK221291 mRNA. Translation: BAD94012.1. Different initiation. AK226844 mRNA. Translation: BAE98937.1. AK230345 mRNA. Translation: BAF02144.1. AK317362 mRNA. Translation: BAH20034.1. AK317443 mRNA. Translation: BAH20110.1.
IPI	IPI00533497.
PIR	S57621.
RefSeq	NP_187537.1. NM_111760.3.
UniGene	At.18035. At.47576. At.71001.
3D structure databases
HSSP	HSSP built from PDB template 1CBG based on UniProtKB P26205.
ProteinModelPortal	Q9SR37.
SMR	Q9SR37. Positions 35-512.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT3G09260.1-P.
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
Proteomic databases
PaxDb	Q9SR37.
PRIDE	Q9SR37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G09260.1; AT3G09260.1; AT3G09260.
GeneID	820082.
KEGG	ath:AT3G09260.
Organism-specific databases
TAIR	At3g09260.
Phylogenomic databases
eggNOG	COG2723.
HOGENOM	HOG000088630.
InParanoid	Q9SR37.
KO	K01188.
OMA	LITWESK.
PhylomeDB	Q9SR37.
ProtClustDB	CLSN2679905.
Gene expression databases
Genevestigator	Q9SR37.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10353. PTHR10353. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00572. GLYCOSYL_HYDROL_F1_1. False negative. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGL23_ARATH

Accession

Primary (citable) accession number: Q9SR37
Secondary accession number(s): B9DH17 , O24433, Q42585, Q56YN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program