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Reviewed, UniProtKB/Swiss-Prot P33157 (E13A_ARATH)

Last modified November 3, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Pathogenesis-related protein 2
      Short name=PR-2
    Beta-1,3-glucanase 2
Gene names
Name: BG2
Ordered Locus Names: At3g57260
ORF Names: F28O9.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

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.5
Sequence conflict3321S → P in AAM63339. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P33157-1 [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: 1392589] [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: 1824335] [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: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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

M90509 mRNA. Translation: AAA32864.1. Frameshift.
M58462 Genomic DNA. Translation: AAA32755.1. Frameshift.
AL137080 Genomic DNA. Translation: CAB68132.1.
AY099668 mRNA. Translation: AAM20519.1.
AY128847 mRNA. Translation: AAM91247.1.
AY086134 mRNA. Translation: AAM63339.1.
IPIIPI00547460.
PIRJQ1694.
T45804.
RefSeqNP_191285.1.
UniGeneAt.22313

3D structure databases

HSSPHSSP built from PDB template 1GHS based on UniProtKB P15737.
ModBaseSearch...

Protein-protein interaction databases

STRINGP33157.

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEP33157.

Genome annotation databases

GeneID824893.
GenomeReviewsGene locus AT3G57260 in contig BA000014_GR.
KEGGath:AT3G57260.
NMPDRfig|3702.1.peg.17058.

Organism-specific databases

TAIRAt3g57260.

Phylogenomic databases

OMANIHAMRI.

Enzyme and pathway databases

BRENDA3.2.1.39. 302.

Gene expression databases

ArrayExpressP33157.
GenevestigatorP33157.
GermOnlineAT3G57260. Arabidopsis thaliana.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
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: November 3, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents