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Q9SUS0 (GUN20_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 67. 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
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 20
EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 20
Gene names
Ordered Locus Names:At4g23560
ORF Names:F9D16.30
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

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 processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

cellulose 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 479458Endoglucanase 20
PRO_0000249272

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
Q9SUS0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 058C98C096A0A07F

FASTA47952,450
        10         20         30         40         50         60 
MGKLLVLMLV GMFLAFESLE ALEYGDALNK SILFFEGQRS GKLPTNQRVK WRADSALSDG 

        70         80         90        100        110        120 
SLANVNLIGG YYDAGDNVKF VWPMSFTTTL LSWAAIEYQN EISSVNQLGY LRSTIKWGTD 

       130        140        150        160        170        180 
FILRAHTSPN MLYTQVGDGN SDHSCWERPE DMDTSRTLYS ISSSSPGSEA AGEAAAALAA 

       190        200        210        220        230        240 
ASLVFKSVDS TYSSTLLNHA KTLFEFADKY RGSYQASCPF YCSYSGYQDE LLWAAAWLYK 

       250        260        270        280        290        300 
ATGDKIYINY VISNKDWSQA VNEFSWDNKF VGAQALLVSE FYNGANDLAK FKSDVESFVC 

       310        320        330        340        350        360 
AMMPGSSSQQ IKPTPGGLLF IRDSSNLQYV TTATTVLFHY SKTLTKAGVG SIQCGSTKFT 

       370        380        390        400        410        420 
VSQIRNFAKS QVDYILGNNP MKMSYMVGFG TKYPTQPHHR GSSLPSIQSK PEKIDCNGGY 

       430        440        450        460        470 
SYYNSDTPNP NVHIGAIVGG PNSSDQYSDK KSDYSHAEPT TYINAAFIGP VAALISSSG

« 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: 10617198] [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: 15170254] [Abstract]
Cited for: GENE FAMILY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL035394 Genomic DNA. Translation: CAA23022.1.
AL161559 Genomic DNA. Translation: CAB79311.1.
CP002687 Genomic DNA. Translation: AEE84775.1.
IPIIPI00530947.
PIRT05588.
RefSeqNP_194087.1. NM_118487.3.
UniGeneAt.23383.
At.5403.

3D structure databases

HSSPHSSP built from PDB template 1TF4 based on UniProtKB P26221.
ProteinModelPortalQ9SUS0.
SMRQ9SUS0. Positions 20-477.
ModBaseSearch...

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEQ9SUS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G23560.1; AT4G23560.1; AT4G23560.
GeneID828456.
GenomeReviewsGene locus AT4G23560 in contig CT486007_GR.
KEGGath:AT4G23560.
NMPDRfig|3702.1.peg.20231.

Organism-specific databases

TAIRAt4g23560.

Phylogenomic databases

GeneTreeEPGT00070000030791.
HOGENOMHBG746347.
InParanoidQ9SUS0.
OMAEYQNEIS.
PhylomeDBQ9SUS0.
ProtClustDBPLN02613.

Gene expression databases

GenevestigatorQ9SUS0.
GermOnlineAT4G23560. Arabidopsis thaliana.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PfamPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN20_ARATH
AccessionPrimary (citable) accession number: Q9SUS0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents