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Reviewed, UniProtKB/Swiss-Prot Q93Z08 (E136_ARATH)

Last modified February 9, 2010. Version 68. 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 6
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 6
      Short name=(1->3)-beta-glucanase 6
    Beta-1,3-endoglucanase 6
      Short name=Beta-1,3-glucanase 6
Gene names
Ordered Locus Names: At5g58090
ORF Names: K21L19.12, K21L19_70
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length477 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 Ref.3 Ref.4.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

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 plasma membrane Ref.3

Inferred from direct assay. Source: TAIR

   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 455434Glucan endo-1,3-beta-glucosidase 6
PRO_0000011892
Propeptide456 – 47722Removed in mature form Potential
PRO_0000011893

Sites

Active site2621Nucleophile By similarity
Active site3231Proton donor By similarity

Amino acid modifications

Lipidation4551GPI-anchor amidated glycine Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2191F → L in AAL24251. Ref.2
Sequence conflict2191F → L in AAN18179. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q93Z08-1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: B8FE6F29218DF57C

FASTA47752,211
        10         20         30         40         50         60 
MGWGSVLLLL AVALLCQRAS SIGANWGTQA SHPLPPDIVV RMLRENGIQK VKLFDAEYDT 

        70         80         90        100        110        120 
LRALGKSGIE VMVGIPNEML ATLASSLKAA EKWVAKNVST HISTDNVNIR YVAVGNEPFL 

       130        140        150        160        170        180 
STYNGSYLST TFPALRNIQI AIIKAGLQNQ VKVTCPLNAD VYDSSTTFPS GGDFRANIRD 

       190        200        210        220        230        240 
LMITIVKFLS ENGGPFTVNI YPYISLYTNP DFPVDYAFFD GNAQPLNDGG TFYYNMFDAN 

       250        260        270        280        290        300 
YDTLVHALEK NGFGNMPIII GEIGWPTDGD SNANLDYAKK FNQGFMAHIS GGKGTPRRPG 

       310        320        330        340        350        360 
PIDAYLFSLI DEDAKSVQPG YFERHWGIFT FDGLPKYALN LGTTNTGALI QAKGVRYLER 

       370        380        390        400        410        420 
KWCVMKPNVR LDDPQVAPAV SYACSLGDCT SLGVGTSCAN LDGKQNISYA FNSYYQIQDQ 

       430        440        450        460        470 
LDTACKFPNI SEVTKTDPST GTCRFPIMIE PYYGGAAREH GFFFPLLMVA AIAVSIF 

« Hide

References

[1]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed: 10718197] [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.
[4]"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB024029 Genomic DNA. Translation: BAB11001.1.
AY058864 mRNA. Translation: AAL24251.1.
BT000612 mRNA. Translation: AAN18179.1.
IPIIPI00518292.
RefSeqNP_200617.2.
UniGeneAt.9709

3D structure databases

SMRQ93Z08. Positions 22-341, 355-447.
ModBaseSearch...

Protein-protein interaction databases

IntActQ93Z08. 1 interaction.

Protein family/group databases

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

Proteomic databases

PRIDEQ93Z08.

Genome annotation databases

GeneID835921.
GenomeReviewsGene locus AT5G58090 in contig BA000015_GR.
KEGGath:AT5G58090.
NMPDRfig|3702.1.peg.27776.

Organism-specific databases

TAIRAt5g58090.

Phylogenomic databases

HOGENOMHBG605194.
InParanoidQ93Z08.
OMADLMLTIV.

Enzyme and pathway databases

BRENDA3.2.1.39. 302.

Gene expression databases

ArrayExpressQ93Z08.
GenevestigatorQ93Z08.
GermOnlineAT5G58090. Arabidopsis thaliana.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR017853. Glyco_hydro_catalytic_core.
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...

Entry information

Entry nameE136_ARATH
AccessionPrimary (citable) accession number: Q93Z08
Secondary accession number(s): Q9FGT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: February 9, 2010
This is version 68 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