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Q9FGH4 (E139_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. 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 9

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase 9
Short name=(1->3)-beta-glucanase 9
Beta-1,3-endoglucanase 9
Short name=Beta-1,3-glucanase 9
Gene names
Ordered Locus Names:At5g58480
ORF Names:MQJ2.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length476 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

Secretedcell wall Potential. Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 453428Glucan endo-1,3-beta-glucosidase 9
PRO_0000251265
Propeptide454 – 47623Removed in mature form Potential
PRO_0000251266

Sites

Active site3271Nucleophile By similarity

Amino acid modifications

Lipidation4531GPI-anchor amidated serine Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9FGH4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 00CC6739B10CBB20

FASTA47652,370
        10         20         30         40         50         60 
MARRLFLLLL AVTAGLSLTG TTVRAVGINW GTEASHPLPP SKVVELLKSN GIVKVKLFDA 

        70         80         90        100        110        120 
DPKVLRALSG SNIGVTIGIQ NSMLKSLNAS VKVAESWVHD NVTRYFNGGN RVRIEYVAVG 

       130        140        150        160        170        180 
EEPFLQSYGN QYKPFVIGAA MNIQNALVKA NLANEVKVVV PSSFDSFLSE SGRPSSGHFR 

       190        200        210        220        230        240 
ADLNKTMIEL LSFLTKHHSP FFVTISPFLS FHQNKNISLD FSLFKETAKA HKDGRKTYRN 

       250        260        270        280        290        300 
SFDLSYDTLV SALFTIGFSE VDIVVSKIGW PTDGAENATS LTAEAFFKGL IVHLEKKTAS 

       310        320        330        340        350        360 
LPRPPVETYI ESLLDEDQRN LSAGNFERHW GVFTFDGQAK YNFSFNHKNQ VNAQNVQYLP 

       370        380        390        400        410        420 
PKWCVVNNNK DLSNASARAL EACAVADCTS ILPGGSCSGI RWPGNVSYAF NSLYQQNDHS 

       430        440        450        460        470 
AESCNFGGLG LITTVDPSED NCRFSIQLDT SHSSSQTPNF FQSWPLLLLF LLSGLF 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
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]"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] [Europe PMC] [Abstract]
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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025632 Genomic DNA. Translation: BAB10263.1.
CP002688 Genomic DNA. Translation: AED97058.1.
BT005117 mRNA. Translation: AAO50650.1.
BT003904 mRNA. Translation: AAO41952.1.
RefSeqNP_200656.2. NM_125234.3.
UniGeneAt.29278.

3D structure databases

ProteinModelPortalQ9FGH4.
SMRQ9FGH4. Positions 26-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G58480.1-P.

Protein family/group databases

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

Proteomic databases

PaxDbQ9FGH4.
PRIDEQ9FGH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G58480.1; AT5G58480.1; AT5G58480.
GeneID835961.
KEGGath:AT5G58480.

Organism-specific databases

TAIRAT5G58480.

Phylogenomic databases

eggNOGNOG266375.
HOGENOMHOG000238221.
InParanoidQ9FGH4.
OMALPNSVPR.
PhylomeDBQ9FGH4.

Enzyme and pathway databases

BioCycARA:AT5G58480-MONOMER.

Gene expression databases

GenevestigatorQ9FGH4.

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.
ProtoNetSearch...

Entry information

Entry nameE139_ARATH
AccessionPrimary (citable) accession number: Q9FGH4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 93 of the entry and version 1 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