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Q93YQ7 (GUN24_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:
Endoglucanase 24

EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 24
Gene names
Ordered Locus Names:At4g39010
ORF Names:F19H22.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length497 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.

Sequence caution

The sequence CAB38821.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB80564.1 differs from that shown. Reason: Erroneous initiation.

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 – 2424 Potential
Chain25 – 497473Endoglucanase 24
PRO_0000249276

Sites

Active site4141 By similarity
Active site4651 By similarity
Active site4741 By similarity

Amino acid modifications

Glycosylation4401N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q93YQ7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1F3EC2493D36BDDD

FASTA49755,495
        10         20         30         40         50         60 
MKLHLHPLSL VFFFFFFFFR PTMSSNQHDY SDALSKSILF FEGQRSGYLP NDQRMTWRRN 

        70         80         90        100        110        120 
SGLSDGWTHN IDLTGGYYDA GDNVKFNFPM AFTTTMLAWS VIEFGEFMPS SELRNSLVAL 

       130        140        150        160        170        180 
RWSSNYLLKS VSQLPNRIFV QVGDPIADHN CWERPEDMDT PRTAYAVNAP NPASEVAGET 

       190        200        210        220        230        240 
TAALSAASIA FRSSDPGYSQ TLLQNAVKTF QFADMYRGAY SSNDDIKNDV CPFYCDFNGF 

       250        260        270        280        290        300 
QDELLWGAAW LRKATGDESY LNYIESNREP FGANDNVDEF GWDNKVGGLN VLVSKEVIEG 

       310        320        330        340        350        360 
NMYNLEAYKA SAESFMCSLV PESSGPHVEY TSAGLLYKPG GSQLQHATTI SFLLLVYAQY 

       370        380        390        400        410        420 
LSRSSLSLNC GTLTVPPDYL RRLAKKQVDY ILGNNPMGLS YMVGYGERYP KRIHHRGSSL 

       430        440        450        460        470        480 
PSIVDHPEAI RCKDGSVYFN STEPNPNVLI GAVVGGPGED DMYDDDRSDF RKSEPTTYIN 

       490 
APFVGVLAYF AANPGSS 

« 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]"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]"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
AL035679 Genomic DNA. Translation: CAB38821.1. Different initiation.
AL161594 Genomic DNA. Translation: CAB80564.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE87007.1.
AY059825 mRNA. Translation: AAL24307.1.
BT002204 mRNA. Translation: AAN72215.1.
PIRT06061.
RefSeqNP_568050.1. NM_120061.1.
UniGeneAt.26609.
At.67360.

3D structure databases

ProteinModelPortalQ93YQ7.
SMRQ93YQ7. Positions 29-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G39010.1-P.

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PaxDbQ93YQ7.
PRIDEQ93YQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39010.1; AT4G39010.1; AT4G39010.
GeneID830056.
KEGGath:AT4G39010.

Organism-specific databases

TAIRAT4G39010.

Phylogenomic databases

eggNOGNOG280562.
HOGENOMHOG000021033.
InParanoidQ93YQ7.
KOK01179.
OMADRYPQRI.
PhylomeDBQ93YQ7.

Enzyme and pathway databases

BioCycARA:AT4G39010-MONOMER.

Gene expression databases

GenevestigatorQ93YQ7.

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 nameGUN24_ARATH
AccessionPrimary (citable) accession number: Q93YQ7
Secondary accession number(s): Q9SVJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 89 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