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Reviewed, UniProtKB/Swiss-Prot Q94CD8 (E134_ARATH)

Last modified November 25, 2008. Version 51. 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 4
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 4
      Short name=(1->3)-beta-glucanase 4
    Beta-1,3-endoglucanase 4
      Short name=Beta-1,3-glucanase 4
Gene names
Ordered Locus Names: At3g13560
ORF Names: MRP15.22
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 length505 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.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence caution

The sequence BAB01763.1 differs from that shown. Reason: Erroneous gene model prediction.

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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-KW

   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 – 2323 Potential
Chain24 – 474451Putative glucan endo-1,3-beta-glucosidase 4
PRO_0000011888
Propeptide475 – 50531Removed in mature form Potential
PRO_0000011889

Sites

Active site2661Nucleophile By similarity
Active site3291Proton donor By similarity

Amino acid modifications

Lipidation4741GPI-anchor amidated alanine Potential
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q94CD8-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4C6CA8CA9952B671

FASTA50554,416
        10         20         30         40         50         60 
MLLPRWFAEA LLLLLSILAC SNAAFIGVNI GTDLTNMPPP SDIVTLLKSQ QITHVRLYDA 

        70         80         90        100        110        120 
NSHMLKAFAN TSIEVMVGVT NEEILKIGRF PSAAAAWVNK NVAAYIPSTN ITAIAVGSEV 

       130        140        150        160        170        180 
LTTIPHVAPI LASALNNIHK ALVASNLNFK VKVSSPMSMD IMPKPFPPST STFSPSWNTT 

       190        200        210        220        230        240 
VYQLLQFLKN TGSFFMLNAY PYYGYTTANG IFPLDYALFK QLSPVKQIVD PNTLLHYNSM 

       250        260        270        280        290        300 
FDAMVDAAYY SMEALNFSKI PVVVTETGWP SSGGSDEAAA TVANAETFNT NLIKRVLNNS 

       310        320        330        340        350        360 
GPPSQPDIPI NTYIYELYNE DKRSGPVSER NWGILFPNGT SVYPLSLSGG SSSAALNGSS 

       370        380        390        400        410        420 
MFCVAKADAD DDKLVDGLNW ACGQGRANCA AIQPGQPCYL PNDVKSHASF AFNDYYQKMK 

       430        440        450        460        470        480 
SAGGTCDFDG TAITTTRDPS YRTCAYTGSL NANATNGNFP PDALGPASPL GGNANARIIF 

       490        500 
SYHLPILAPL ALTLLQLLLQ HDRLL

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References

[1]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(2000) [PubMed: 10907853] [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.
[5]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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Cross-references

Sequence databases

AP000603 Genomic DNA. Translation: BAB01763.1. Sequence problems.
AY034940 mRNA. Translation: AAK59446.1.
AY063117 mRNA. Translation: AAL34291.1.
RefSeqNP_187965.1.
NP_974302.1.
NP_974303.1.
UniGeneAt.8269

3D structure databases

HSSPHSSP built from PDB template 1AQ0 based on UniProtKB P12257.
ModBaseSearch...

Genome annotation databases

GeneID820558.
GenomeReviewsGene locus AT3G13560 in contig BA000014_GR.
NMPDRfig|3702.1.peg.13463.

Organism-specific databases

TAIRAt3g13560.

Gene expression databases

ArrayExpressQ94CD8.
GermOnlineAT3G13560. Arabidopsis thaliana.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sub_cat.
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 nameE134_ARATH
AccessionPrimary (citable) accession number: Q94CD8
Secondary accession number(s): Q9LJD6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: December 1, 2001
Last modified: November 25, 2008
This is version 51 of the entry and version 1 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