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Q9C7U5 (E132_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 78. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-glucosidase 2

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase 2
Short name=(1->3)-beta-glucanase 2
Beta-1,3-endoglucanase 2
Short name=Beta-1,3-glucanase 2
Gene names
Ordered Locus Names:At1g66250
ORF Names:T6J19.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length505 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 AAG51762.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   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 plasma membrane

Inferred from direct assay Ref.4. Source: TAIR

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

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 477457Glucan endo-1,3-beta-glucosidase 2
PRO_0000252330
Propeptide478 – 50528Removed in mature form Potential
PRO_0000252331

Sites

Active site2721Nucleophile By similarity
Active site3341Proton donor By similarity

Amino acid modifications

Lipidation4771GPI-anchor amidated serine Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4731N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9C7U5 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 1A1CC342B307F29F

FASTA50554,206
        10         20         30         40         50         60 
MASLLHLLLL SLSLLVLASA SPSPPADEGS YIGVNIGTDL SDMPHPTQVV ALLKAQEIRH 

        70         80         90        100        110        120 
IRLYNADPGL LIALANTGIK VIISIPNDQL LGIGQSNSTA ANWVKRNVIA HYPATMITAV 

       130        140        150        160        170        180 
SVGSEVLTSL SNAAPVLVSA IKNVHAALLS ANLDKLIKVS TPLSTSLILD PFPPSQAFFN 

       190        200        210        220        230        240 
RSLNAVIVPL LSFLQSTNSY LMVNVYPYID YMQSNGVIPL DYALFKPIPP NKEAVDANTL 

       250        260        270        280        290        300 
VRYSNAFDAM VDATYFAMAF LNFTNIPVLV TESGWPSKGE TNEPDATLDN ANTYNSNLIR 

       310        320        330        340        350        360 
HVLNKTGTPK RPGIAVSTYI YELYNEDTKA GLSEKNWGLF NANGEPVYVL RLTNSGSVLA 

       370        380        390        400        410        420 
NDTTNQTYCT AREGADTKML QAALDWACGP GKIDCSPIKQ GETCYEPDNV VAHANYAFDT 

       430        440        450        460        470        480 
YYHQTGNNPD ACNFNGVASI TTTDPSHGTC VFAGSRGNGR NGTSVNITAP SANSTTSSGI 

       490        500 
RSDLYYSRGI WSILTVMILN VANIL 

« 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]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [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
AC066691 Genomic DNA. Translation: AAG51762.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34485.1.
BX814184 mRNA. No translation available.
PIRE96687.
RefSeqNP_176799.2. NM_105296.2.
UniGeneAt.49486.

3D structure databases

ProteinModelPortalQ9C7U5.
SMRQ9C7U5. Positions 32-348, 367-452.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Proteomic databases

PaxDbQ9C7U5.
PRIDEQ9C7U5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G66250.1; AT1G66250.1; AT1G66250.
GeneID842942.
KEGGath:AT1G66250.

Organism-specific databases

TAIRAT1G66250.

Phylogenomic databases

eggNOGNOG290245.
HOGENOMHOG000238220.
InParanoidQ9C7U5.
OMASHGTCVF.
PhylomeDBQ9C7U5.
ProtClustDBCLSN2918516.

Enzyme and pathway databases

BioCycARA:AT1G66250-MONOMER.

Gene expression databases

ArrayExpressQ9C7U5.
GenevestigatorQ9C7U5.

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 nameE132_ARATH
AccessionPrimary (citable) accession number: Q9C7U5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: March 19, 2014
This is version 78 of the entry and version 2 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