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O65399 (E131_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase 1
Short name=(1->3)-beta-glucanase 1
Beta-1,3-endoglucanase 1
Short name=Beta-1,3-glucanase 1
Gene names
Ordered Locus Names:At1g11820, At1g11830
ORF Names:F12F1.33, F25C20_1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence caution

The sequence AAC17632.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAO42272.1 differs from that shown. Reason: Probable cloning artifact leading to a deletion into the sequence.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O65399-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 485457Glucan endo-1,3-beta-glucosidase 1
PRO_0000011884
Propeptide486 – 51126Removed in mature form Potential
PRO_0000011885

Sites

Active site2841Nucleophile By similarity
Active site3471Proton donor By similarity

Amino acid modifications

Lipidation4851GPI-anchor amidated alanine Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4731N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 16, 2011. Version 3.
Checksum: 1C29693D4F94E8C4

FASTA51155,630
        10         20         30         40         50         60 
MAFTSMVSTV PVLFFFFTLL LISANSSSLS HNIKVQEQDK DPFVGFNIGT DVSNLLSPTE 

        70         80         90        100        110        120 
LVKFLQAQKV NHVRLYDADP ELLKALAKTK VRVIISVPNN QLLAIGSSNS TAASWIGRNV 

       130        140        150        160        170        180 
VAYYPETLIT AISVGDEVLT TVPSSAPLLL PAIESLYNAL VASNLHTQIK VSTPHAASIM 

       190        200        210        220        230        240 
LDTFPPSQAY FNQTWHSIMV PLLQFLSKTG SPLMMNLYPY YVYMQNKGVV PLDNCLFEPL 

       250        260        270        280        290        300 
TPSKEMVDPN TLLHYTNVLD AMVDAAYVSM KNLNVSDVAV LVTESGWPSK GDSKEPYATI 

       310        320        330        340        350        360 
DNADTYNSNL IKHVFDRTGT PLHPEMTSSV YIYELFNEDL RAPPVSEASW GLFYGNSTPV 

       370        380        390        400        410        420 
YLLHVSGSGT FLANDTTNQT YCIAMDGVDA KTLQAALDWA CGPGRSNCSE IQPGESCYQP 

       430        440        450        460        470        480 
NNVKGHASFA FNSYYQKEGR ASGSCDFKGV AMITTTDPSH GSCIFPGSKK VGNRTQTVVN 

       490        500        510 
STEVAAGEAT SRSLSRGFCV TIMILVTFSI L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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.
[4]"Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis."
Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P.
Plant Physiol. 132:568-577(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
Tissue: Callus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC002131 Genomic DNA. Translation: AAC17632.1. Sequence problems.
AC007296 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE28791.1.
BT004271 mRNA. Translation: AAO42272.1. Sequence problems.
PIRE86252.
RefSeqNP_001184967.1. NM_001198038.1.
UniGeneAt.10643.

3D structure databases

ProteinModelPortalO65399.
SMRO65399. Positions 44-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G11820.1-P.

Protein family/group databases

CAZyCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Proteomic databases

PaxDbO65399.
PRIDEO65399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G11820.2; AT1G11820.2; AT1G11820. [O65399-1]
GeneID837730.
KEGGath:AT1G11820.

Organism-specific databases

TAIRAT1G11820.

Phylogenomic databases

eggNOGNOG329755.
HOGENOMHOG000238220.
InParanoidO65399.
OMACYFQGAG.

Enzyme and pathway databases

BioCycARA:AT1G11820-MONOMER.
ARA:GQT-1170-MONOMER.

Gene expression databases

ArrayExpressO65399.
GenevestigatorO65399.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE131_ARATH
AccessionPrimary (citable) accession number: O65399
Secondary accession number(s): F4IAH7, Q84W37
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 94 of the entry and version 3 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