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Q9SZ90 (GUN18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:
Endoglucanase 18

EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 18
Gene names
Ordered Locus Names:At4g09740
ORF Names:F17A8.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Sequence caution

The sequence CAB39641.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB78097.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 478457Endoglucanase 18
PRO_0000249270

Sites

Active site3981 By similarity
Active site4491 By similarity
Active site4581 By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation4421N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SZ90 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 594B26EAD9E82FD3

FASTA47852,514
        10         20         30         40         50         60 
MGKLLVVMLI GMFLAFESLE ALDYGDALNK SILFFEGQRS GKLPTNQRVK WRADSGLSDG 

        70         80         90        100        110        120 
ASANVNLIGG YYDAGDNVKF VWPMSFTTTL LSWAALEYQN EITFVNQLGY LRSTIKWGTN 

       130        140        150        160        170        180 
FILRAHTSTN MLYTQVGDGN SDHSCWERPE DMDTPRTLYS ISSSSPGSEA AGEAAAALAA 

       190        200        210        220        230        240 
ASLVFKLVDS TYSSKLLNNA KSLFEFADKY RGSYQASCPF YCSHSGYQDE LLWAAAWLYK 

       250        260        270        280        290        300 
ATGEKSYLNY VISNKDWSKA INEFSWDNKF AGVQALLASE FYNGANDLEK FKTDVESFVC 

       310        320        330        340        350        360 
ALMPGSSSQQ IKPTPGGILF IRDSSNLQYV TTATTILFYY SKTLTKAGVG SIQCGSTQFT 

       370        380        390        400        410        420 
VSQIRNFAKS QVDYILGNNP LKMSYMVGFG TKYPTQPHHR GSSLPSIQSK PEKIDCNGGF 

       430        440        450        460        470 
SYYNFDTPNP NVHTGAIVGG PNSSDQYSDK RTDYSHAEPT TYINAAFIGS VAALISSS 

« 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]"Phylogenetic analysis of the plant endo-beta-1,4-glucanase gene family."
Libertini E., Li Y., McQueen-Mason S.J.
J. Mol. Evol. 58:506-515(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049482 Genomic DNA. Translation: CAB39641.1. Sequence problems.
AL161515 Genomic DNA. Translation: CAB78097.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82789.1.
PIRT04021.
RefSeqNP_849349.1. NM_179018.1.
UniGeneAt.54238.

3D structure databases

ProteinModelPortalQ9SZ90.
SMRQ9SZ90. Positions 21-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G09740.1-P.

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PaxDbQ9SZ90.
PRIDEQ9SZ90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G09740.1; AT4G09740.1; AT4G09740.
GeneID826560.
KEGGath:AT4G09740.

Organism-specific databases

TAIRAT4G09740.

Phylogenomic databases

eggNOGNOG275252.
HOGENOMHOG000021033.
InParanoidQ9SZ90.
OMANFILRAH.

Enzyme and pathway databases

BioCycARA:AT4G09740-MONOMER.

Gene expression databases

GenevestigatorQ9SZ90.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN18_ARATH
AccessionPrimary (citable) accession number: Q9SZ90
Secondary accession number(s): F4JKS2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: January 25, 2012
Last modified: May 14, 2014
This is version 84 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