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Q9STW8 (GUN21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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 21

EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 21
Gene names
Name:KOR3
Ordered Locus Names:At4g24260
ORF Names:T22A6.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
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

Cell membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Expressed in conductive tissues of young roots, cotyledons, rosette leaves, cauline leaves and sepals. Expressed in the leaf trichome support cells. Ref.3

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Endoglucanase 21
PRO_0000249273

Regions

Topological domain1 – 7070Cytoplasmic Potential
Transmembrane71 – 9121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain92 – 620529Extracellular Potential

Sites

Active site5141 By similarity
Active site5611 By similarity
Active site5701 By similarity

Amino acid modifications

Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9STW8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7BCF07C806B0BBD0

FASTA62069,585
        10         20         30         40         50         60 
MYGRDPWGGP LEINAADSMT DDDRSRNLQD LDRATPSRPL DETQQSWLLG PKVLKKKKYV 

        70         80         90        100        110        120 
DLGCILVSRK IFLWTLGTIV VTALLSGFIT LIVKTLPHHH HKEPPPDNYT IALRTALKFF 

       130        140        150        160        170        180 
NAQQSGKLPK NIYNVSWRHD SCLQDGKGDP GQCYKDLVGG YYDAGDSIKF NFPMSYAMTM 

       190        200        210        220        230        240 
LSWSVIEYSA KYQAAGELEH VKELIKWGTD YFLKTFNSSA DNIYVMVEQV GSGVSGRGSE 

       250        260        270        280        290        300 
LHNDHYCWMR PEDIHYKRTV SQCYSSCSDL AAEMAAALAS ASIVFKDNRL YSKNLVHGAK 

       310        320        330        340        350        360 
TLYRFATTSR NRYSQNGKES SKFYNSSMFE DELLWGGAWL YYATGNVTYL ERVTSHHMAE 

       370        380        390        400        410        420 
KAGAFGNSPY YGVFSWDNKL PGAQLLLTRM RLFLSPGYPY EDMLSEFHNQ TGRVMCSYLP 

       430        440        450        460        470        480 
YYKKFNRTNG GLIQLNHGAP QPLQYVANAA FLAALFSDYL EAADTPGWYC GPNFYTTEFL 

       490        500        510        520        530        540 
RNFSRSQIDY ILGKNPRKMS YVVGYGQRYP KQVHHRGASI PKNMKETCTG GFKWKKSKKN 

       550        560        570        580        590        600 
NPNAINGAMV AGPDKHDGFH DIRTNYNYTE PTLAGNAGLV AALVALSGEK AVGGIDKNTM 

       610        620 
FSAVPPLVMA TPPPPAPWTP 

« 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]"Two Arabidopsis thaliana genes, KOR2 and KOR3, which encode membrane-anchored endo-1,4-beta-D-glucanases, are differentially expressed in developing leaf trichomes and their support cells."
Moelhoej M., Joergensen B., Ulvskov P., Borkhardt B.
Plant Mol. Biol. 46:263-275(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[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
AL078637 Genomic DNA. Translation: CAB45061.1.
AL161561 Genomic DNA. Translation: CAB79336.1.
CP002687 Genomic DNA. Translation: AEE84879.1.
PIRT09889.
RefSeqNP_194157.1. NM_118559.1.
UniGeneAt.54499.

3D structure databases

ProteinModelPortalQ9STW8.
SMRQ9STW8. Positions 108-586.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PaxDbQ9STW8.
PRIDEQ9STW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G24260.1; AT4G24260.1; AT4G24260.
GeneID828527.
KEGGath:AT4G24260.

Organism-specific databases

TAIRAT4G24260.

Phylogenomic databases

eggNOGNOG238365.
HOGENOMHOG000021033.
InParanoidQ9STW8.
OMAPEDIHYK.
PhylomeDBQ9STW8.

Enzyme and pathway databases

BioCycARA:AT4G24260-MONOMER.

Gene expression databases

GenevestigatorQ9STW8.

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 nameGUN21_ARATH
AccessionPrimary (citable) accession number: Q9STW8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 85 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