Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6NKW9 (E138_ARATH)

Last modified February 9, 2010. Version 46. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Glucan endo-1,3-beta-glucosidase 8
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 8
      Short name=(1->3)-beta-glucanase 8
    Beta-1,3-endoglucanase 8
      Short name=Beta-1,3-glucanase 8
Gene names
Ordered Locus Names: At1g64760
ORF Names: F13O11.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Hide | Top

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Subcellular location

Secreted › cell wall Potential. Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side Ref.4 Ref.5.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 455422Glucan endo-1,3-beta-glucosidase 8
PRO_0000251255
Propeptide456 – 48126Removed in mature form Potential
PRO_0000251256

Sites

Active site2651Nucleophile By similarity
Active site3261Nucleophile By similarity

Amino acid modifications

Lipidation4551GPI-anchor amidated serine Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict951W → L in AAS99718. Ref.2
Sequence conflict951W → L in BAD95084. Ref.3
Sequence conflict3581N → H in AAS99718. Ref.2
Sequence conflict3581N → H in BAD95084. Ref.3

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q6NKW9-1 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 01A7938FBF3C65F0

FASTA48152,281
        10         20         30         40         50         60 
MSNLLALVVG FVIVIGHLGI LVNGLGVNWG TMATHKLPPK TVVQMLKDNN INKVKLFDAD 

        70         80         90        100        110        120 
ETTMGALAGS GLEVMVAIPN DQLKVMTSYD RAKDWVRKNV TRYNFDGGVN ITFVAVGNEP 

       130        140        150        160        170        180 
FLKSYNGSFI NLTFPALANI QNALNEAGLG NSVKATVPLN ADVYDSPASN PVPSAGRFRP 

       190        200        210        220        230        240 
DIIGQMTQIV DFLGKNNAPI TINIYPFLSL YGNDDFPLNY AFFDGAEPIN DNGIDYTNVF 

       250        260        270        280        290        300 
DANFDTLVSS LKAVGHGDMP IIVGEVGWPT EGDKHANAGS AYRFYNGLLP RLGTNKGTPL 

       310        320        330        340        350        360 
RPTYIEVYLF GLLDEDAKSI APGPFERHWG IFKFDGQPKF PIDLSGQGQS KFLIGAQNVP 

       370        380        390        400        410        420 
YLPNKWCTFN PEAKDLTKLA ANIDYACTFS DCTALGYGSS CNTLDANGNA SYAFNMFFQV 

       430        440        450        460        470        480 
KNQDESACYF QGLATITTQN ISQGQCNFPI QIVASSASSF SCSSYSLVVL IVWFLLSGMM 


F

« Hide

Hide | Top

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: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M., Shinozaki K., Ecker J.R.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[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.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC006193 Genomic DNA. Translation: AAD38251.1. Different initiation.
BT012574 mRNA. Translation: AAS99718.1.
AK220635 mRNA. Translation: BAD95084.1.
AK176856 mRNA. Translation: BAD44619.1.
AK175510 mRNA. Translation: BAD43273.1.
IPIIPI00535099.
PIRG96670.
RefSeqNP_001031232.1.
NP_176656.1.
UniGeneAt.50002

3D structure databases

HSSPHSSP built from PDB template 2CYG based on UniProtKB O22317.
SMRQ6NKW9. Positions 359-450.
ModBaseSearch...

Protein family/group databases

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

Proteomic databases

PRIDEQ6NKW9.

Genome annotation databases

GeneID842784.
GenomeReviewsGene locus AT1G64760 in contig CT485782_GR.
KEGGath:AT1G64760.
NMPDRfig|3702.1.peg.5894.

Organism-specific databases

TAIRAt1g64760.

Phylogenomic databases

HOGENOMHBG605194.
InParanoidQ6NKW9.
OMAIVQFLNQ.

Enzyme and pathway databases

BRENDA3.2.1.39. 302.

Gene expression databases

GenevestigatorQ6NKW9.
GermOnlineAT1G64760. 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...

Hide | Top

Entry information

Entry nameE138_ARATH
AccessionPrimary (citable) accession number: Q6NKW9
Secondary accession number(s): Q67XG3, Q9XIR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: February 9, 2010
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

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