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Reviewed, UniProtKB/Swiss-Prot Q9SVJ4 (GUN22_ARATH)

Last modified October 13, 2009. Version 45. 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

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Names and origin

Protein namesRecommended name:
    Endoglucanase 22
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta glucanase 22
Gene names
Ordered Locus Names: At4g38990
ORF Names: F19H22.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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.

Caution

The conserved 'Asp-464' active site is replaced by a Gly residue.

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Ontologies

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 494473Endoglucanase 22
PRO_0000249274

Sites

Active site4131 By similarity
Active site4731 By similarity

Amino acid modifications

Glycosylation4681N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9SVJ4-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FF242EA53A8070A4

FASTA49455,019
        10         20         30         40         50         60 
MKPLVCSFIV ILLILLPTTI SHDYSDALTK SILFFEGQRS GYLPREQRMT WRHNSALNDG 

        70         80         90        100        110        120 
KNLNVDLVGG YYDAGDNIKF HFPMAFTTTM LAWSAIDFGS YMSPADLRDN LVALRWGSNY 

       130        140        150        160        170        180 
LLKTVSQLPN RIFVQVGEPT PDHQCWERPE DMDTPRTAYA LEAPKPASDL AGEIAAALAA 

       190        200        210        220        230        240 
ASIAFKRFDP RYSKLLLDNA LRTFEYADSH RGSYTNNPET KLAVCPFYCS VNGYEDELLW 

       250        260        270        280        290        300 
GAAWLRRATG KDSYIKYLVE NRQSFGSDSN YFEFGWDNKV GGVNVLVAKE VFEKNVAAIA 

       310        320        330        340        350        360 
PYKDTAEKLM CSFFLETPGA HMSYSPGGLL YKPGSSQLQN TVALSFLLLT YANYLSKSSQ 

       370        380        390        400        410        420 
QPLQILSTTP LWYLTQRIAN IVGFEKVDYI LGDNPMKMSY MIGYGNRYPR QIHHRGASSP 

       430        440        450        460        470        480 
SITTHPTPVK CSEGWNSFSS PNPDPNVLVG AVIGGPNIDD KFVGGRTNAS ETEPTTYINA 

       490 
PFVGLLAYFK ANPV

« Hide

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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]"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.

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Cross-references

Sequence databases

AL035679 Genomic DNA. Translation: CAB38819.1.
AL161594 Genomic DNA. Translation: CAB80562.1.
IPIIPI00536910.
PIRT06059.

3D structure databases

HSSPHSSP built from PDB template 1KS8 based on UniProtKB O77044.
ModBaseSearch...

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Organism-specific databases

TAIRAt4g38990.

Enzyme and pathway databases

BRENDA3.2.1.4. 302.

Gene expression databases

ArrayExpressQ9SVJ4.
GenevestigatorQ9SVJ4.
GermOnlineAT4G38990. Arabidopsis thaliana.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PANTHERPTHR22298:SF3. Glyco_hydro_9. 1 hit.
PfamPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. False negative.
PS00698. GLYCOSYL_HYDROL_F9_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGUN22_ARATH
AccessionPrimary (citable) accession number: Q9SVJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: October 13, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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