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Reviewed, UniProtKB/Swiss-Prot O65399 (E131_ARATH)

Last modified June 16, 2009. Version 60. 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

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Names and origin

Protein namesRecommended name:
    Putative 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) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor. Ref.3

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: Frameshift at position 33.

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Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete 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 to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 376348Putative glucan endo-1,3-beta-glucosidase 1
PRO_0000011884
Propeptide377 – 40226Removed in mature form Potential
PRO_0000011885

Sites

Active site1751Nucleophile By similarity
Active site2381Proton donor By similarity

Amino acid modifications

Lipidation3761GPI-anchor amidated alanine Potential
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
O65399-1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: 537E19205C2245EC

FASTA40243,767
        10         20         30         40         50         60 
MAFTSMVSTV PVLFFFFTLL LISANSSSLS HNVPSSAPLL LPAIESLYNA LVASNLHTQI 

        70         80         90        100        110        120 
KVSTPHAASI MLDTFPPSQA YFNQTWHSIM VPLLQFLSKT GSPLMMNLYP YYVYMQNKGV 

       130        140        150        160        170        180 
VPLDNCLFEP LTPSKEMVDP NTLLHYTNVL DAMVDAAYVS MKNLNVSDVA VLVTESGWPS 

       190        200        210        220        230        240 
KGDSKEPYAT IDNADTYNSN LIKHVFDRTG TPLHPEMTSS VYIYELFNED LRAPPVSEAS 

       250        260        270        280        290        300 
WGLFYGNSTP VYLLHVSGSG TFLANDTTNQ TYCIAMDGVD AKTLQAALDW ACGPGRSNCS 

       310        320        330        340        350        360 
EIQPGESCYQ PNNVKGHASF AFNSYYQKEG RASGSCDFKG VAMITTTDPS HGSCIFPGSK 

       370        380        390        400 
KVGNRTQTVV NSTEVAAGEA TSRSLSRGFC VTIMILVTFS IL

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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: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"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: 12805588] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
Tissue: Callus.

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Cross-references

Sequence databases

AC002131 Genomic DNA. Translation: AAC17632.1. Sequence problems.
AC007296 Genomic DNA. No translation available.
BT004271 mRNA. Translation: AAO42272.1. Frameshift.
IPIIPI00548319.
PIRE86252.

3D structure databases

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

Protein family/group databases

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

Proteomic databases

PRIDEO65399.

Genome annotation databases

GenomeReviewsGene locus AT1G11820 in contig CT485782_GR.

Organism-specific databases

TAIRAt1g11820.

Enzyme and pathway databases

BRENDA3.2.1.39. 302.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sg_catalytic.
IPR012946. X8.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameE131_ARATH
AccessionPrimary (citable) accession number: O65399
Secondary accession number(s): Q84W37
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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