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Q9M069 (E137_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. 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 7

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase 7
Short name=(1->3)-beta-glucanase 7
Beta-1,3-endoglucanase 7
Short name=Beta-1,3-glucanase 7
Gene names
Ordered Locus Names:At4g34480
ORF Names:T4L20.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length504 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

Secreted. Secretedcell wall Ref.3.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence caution

The sequence CAA18827.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80165.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2222 Ref.3
Chain23 – 504482Glucan endo-1,3-beta-glucosidase 7
PRO_0000042684

Regions

Compositional bias449 – 46012Gly-rich

Sites

Active site2641Nucleophile By similarity UniProtKB P15737
Active site3271Proton donor By similarity UniProtKB P15737

Sequences

Sequence LengthMass (Da)Tools
Q9M069 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 77FF26A6AF36C167

FASTA50453,121
        10         20         30         40         50         60 
MALSISIYFL LIFLSHFPSS HAEPFIGVNY GQVADNLPPP SETVKLLQST SIQKVRLYGA 

        70         80         90        100        110        120 
DPAIIKALAG TGVGIVIGAA NGDVPSLASD PNAATQWINS NVLPFYPASK IMLITVGNEI 

       130        140        150        160        170        180 
LMSNDPNLVN QLLPAMQNVQ KALEAVSLGG KIKVSTVNSM TVLGSSDPPS SGSFAAGYQT 

       190        200        210        220        230        240 
GLKGILQFLS DTGSPFAINP YPFFAYQSDP RPETLAFCLF EPNAGRVDSK TGIKYTNMFD 

       250        260        270        280        290        300 
AQVDAVHSAL KSMGFEKVEI VVAETGWASR GDANEVGASV DNAKAYNGNL IAHLRSMVGT 

       310        320        330        340        350        360 
PLMPGKPVDT YIFALYDENL KPGPSSERAF GLFKTDLSMV YDVGLAKSSS SSQTPSGKVT 

       370        380        390        400        410        420 
SSGWCVPKKG ATNEELQASL DWACGHGIDC GAIQPGGACF EPNNVVSHAA YAMNMYFQKS 

       430        440        450        460        470        480 
PKQPTDCDFS KTATVTSQNP SYNNCVYPGG GGGGGGGGGG SKAVMNKYVS SDKVEKKNGA 

       490        500 
TEPKVSSSLS FLLIFLSLIF HVYM 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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]"Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants."
Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P., Slabas A.R.
J. Biol. Chem. 272:15841-15848(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-38, SUBCELLULAR LOCATION.
Strain: cv. Landsberg erecta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL023094 Genomic DNA. Translation: CAA18827.1. Sequence problems.
AL161585 Genomic DNA. Translation: CAB80165.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86384.1.
PIRD85406.
T05268.
RefSeqNP_195174.6. NM_119613.7.
UniGeneAt.48072.

3D structure databases

ProteinModelPortalQ9M069.
SMRQ9M069. Positions 26-345, 351-450.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PaxDbQ9M069.
PRIDEQ9M069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34480.1; AT4G34480.1; AT4G34480.
GeneID829599.
KEGGath:AT4G34480.

Organism-specific databases

TAIRAT4G34480.

Phylogenomic databases

eggNOGNOG309748.
HOGENOMHOG000238220.
InParanoidQ9M069.
OMAWLAANVL.
PhylomeDBQ9M069.

Enzyme and pathway databases

BioCycARA:AT4G34480-MONOMER.

Gene expression databases

GenevestigatorQ9M069.

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 nameE137_ARATH
AccessionPrimary (citable) accession number: Q9M069
Secondary accession number(s): O65675, P80829
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: September 22, 2009
Last modified: May 14, 2014
This is version 89 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