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P33157 (E13A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-glucosidase, acidic isoform

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
Beta-1,3-glucanase 2
Pathogenesis-related protein 2
Short name=PR-2
Gene names
Name:BG2
Ordered Locus Names:At3g57260
ORF Names:F28O9.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in the defense of plants against pathogens.

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Subcellular location

Secretedextracellular spaceapoplast. Note: Accumulates in the apoplast before secretion.

Induction

By 2,6-dichloroisonicotinic acid (INA) and salicylic acid (possibly an endogenous signal for acquired resistance). Strongly induced by pathogen infection.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence caution

The sequence AAA32755.1 differs from that shown. Reason: Frameshift at position 62.

The sequence AAA32864.1 differs from that shown. Reason: Frameshift at position 62.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 339309Glucan endo-1,3-beta-glucosidase, acidic isoform
PRO_0000011882

Sites

Active site2631Nucleophile By similarity
Active site3201Proton donor By similarity

Experimental info

Sequence conflict271H → P Ref.2
Sequence conflict271H → P Ref.6
Sequence conflict3321S → P in AAM63339. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P33157 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 3B145DB01733BD22

FASTA33937,339
        10         20         30         40         50         60 
MSESRSLASP PMLMILLSLV IASFFNHTAG QIGVCYGMLG DTLPSPSDVV ALYKQQNIQR 

        70         80         90        100        110        120 
MRLYGPDPGA LAALRGSDIE LILDVPSSDL ERLASSQTEA DKWVQENVQS YRDGVRFRYI 

       130        140        150        160        170        180 
NVGNEVKPSV GGFLLQAMQN IENAVSGAGL EVKVSTAIAT DTTTDTSPPS QGRFRDEYKS 

       190        200        210        220        230        240 
FLEPVIGFLA SKQSPLLVNL YPYFSYMGDT ANIHLDYALF TAQSTVDNDP GYSYQNLFDA 

       250        260        270        280        290        300 
NLDSVYAALE KSGGGSLEIV VSETGWPTEG AVGTSVENAK TYVNNLIQHV KNGSPRRPGK 

       310        320        330 
AIETYIFAMF DENKKEPTYE KFWGLFHPDR QSKYEVNFN 

« Hide

References

« Hide 'large scale' references
[1]"Acquired resistance in Arabidopsis."
Uknes S., Mauch-Mani B., Moyer M., Potter S., Williams S., Dincher S., Chandler D., Slusarenko A., Ward E., Ryals J.
Plant Cell 4:645-656(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Landsberg erecta.
Tissue: Leaf.
[2]"Induction of Arabidopsis defense genes by virulent and avirulent Pseudomonas syringae strains and by a cloned avirulence gene."
Dong X., Mindrinos M., Davis K., Ausubel F.
Plant Cell 3:61-72(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90509 mRNA. Translation: AAA32864.1. Frameshift.
M58462 Genomic DNA. Translation: AAA32755.1. Frameshift.
AL137080 Genomic DNA. Translation: CAB68132.1.
CP002686 Genomic DNA. Translation: AEE79633.1.
AY099668 mRNA. Translation: AAM20519.1.
AY128847 mRNA. Translation: AAM91247.1.
AY086134 mRNA. Translation: AAM63339.1.
PIRJQ1694.
T45804.
RefSeqNP_191285.1. NM_115586.2.
UniGeneAt.22313.

3D structure databases

ProteinModelPortalP33157.
SMRP33157. Positions 31-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP33157. 1 interaction.
STRING3702.AT3G57260.1-P.

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PaxDbP33157.
PRIDEP33157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G57260.1; AT3G57260.1; AT3G57260.
GeneID824893.
KEGGath:AT3G57260.

Organism-specific databases

TAIRAT3G57260.

Phylogenomic databases

eggNOGNOG268889.
HOGENOMHOG000238220.
InParanoidP33157.
OMAFAYSADP.
PhylomeDBP33157.
ProtClustDBCLSN2915357.

Enzyme and pathway databases

BioCycARA:AT3G57260-MONOMER.

Gene expression databases

ArrayExpressP33157.
GenevestigatorP33157.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13A_ARATH
AccessionPrimary (citable) accession number: P33157
Secondary accession number(s): Q8LD94, Q9M2M1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 6, 2002
Last modified: February 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names