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Protein

Endoglucanase 23

Gene

At4g39000

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei410 – 4101By similarity
Active sitei470 – 4701By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciARA:AT4G39000-MONOMER.

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 23 (EC:3.2.1.4)
Alternative name(s):
Endo-1,4-beta glucanase 23
Gene namesi
Ordered Locus Names:At4g39000
ORF Names:F19H22.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G39000.

Subcellular locationi

  1. Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 493470Endoglucanase 23PRO_0000249275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ8GY58.

Expressioni

Gene expression databases

ExpressionAtlasiQ8GY58. differential.
GenevestigatoriQ8GY58.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G39000.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8GY58.
SMRiQ8GY58. Positions 25-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG322234.
InParanoidiQ8GY58.
KOiK01179.
OMAiFQYADSH.
PhylomeDBiQ8GY58.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
[Graphical view]
PfamiPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8GY58-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKASIYLVTV FILLLLLLPT AIPHDYSDAL RKSILFFEGQ RSGRLPKQQR
60 70 80 90 100
MAWRRNSALN DGKNLKTDLV GGYYDAGDNV KFHFPMAFTA TMLAWSSVDF
110 120 130 140 150
GRYMSQHDFR HNLVAVKWAT DYLLKTVSQL PNRIFVHVGE VQPDHDCWER
160 170 180 190 200
PEDMDTPRTA FALDAPYPAS DLAGEIAAAL AAASIAFKQA NPKYSAILLN
210 220 230 240 250
KAVQTFQYAD SHRGSYTDNP GIKQAVCPFY CSVNGYKDEL LWGAAWLRRA
260 270 280 290 300
TGEDSYLRYL VDNGQAFGES SNYFEFGWDN KVGGVNVLVA KEVLQNNVTA
310 320 330 340 350
IAAYKDTAEK MMCSFLPETN GPHMSYTPGG LIYKPGSTQL QNTAALSFLL
360 370 380 390 400
LTYADYLSTS SQQLNCGNLK FQPDSLRRIV KRQVDYVLGD NPMKLSYMIG
410 420 430 440 450
YGERYPGLIH HRGSSIPSVT VHPAAFGCIA GWNIFSSPNP NPNILIGAVI
460 470 480 490
GGPDVDDRFI GGRTNASETE PTTYINAPFV GVFAYFKSNP NFS
Length:493
Mass (Da):54,692
Last modified:September 5, 2006 - v2
Checksum:iB999CEC76F5FDFC3
GO
Isoform 2 (identifier: Q8GY58-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     292-310: EVLQNNVTAIAAYKDTAEK → VWSNFQNQTDVYIYDKCDR
     311-493: Missing.

Note: No experimental confirmation available.

Show »
Length:310
Mass (Da):35,065
Checksum:iBDC4CF88CD8C2535
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971Missing in BAC42491 (PubMed:11910074).Curated
Sequence conflicti215 – 2151S → T in BAC42491 (PubMed:11910074).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei292 – 31019EVLQN…DTAEK → VWSNFQNQTDVYIYDKCDR in isoform 2. 1 PublicationVSP_020387Add
BLAST
Alternative sequencei311 – 493183Missing in isoform 2. 1 PublicationVSP_020388Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035679 Genomic DNA. Translation: CAB38820.1.
AL161594 Genomic DNA. Translation: CAB80563.1.
CP002687 Genomic DNA. Translation: AEE87006.1.
AK117850 mRNA. Translation: BAC42491.1.
DQ446906 mRNA. Translation: ABE66120.1.
PIRiT06060.
RefSeqiNP_195611.1. NM_120060.1. [Q8GY58-1]
UniGeneiAt.31125.

Genome annotation databases

EnsemblPlantsiAT4G39000.1; AT4G39000.1; AT4G39000. [Q8GY58-1]
GeneIDi830055.
KEGGiath:AT4G39000.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035679 Genomic DNA. Translation: CAB38820.1.
AL161594 Genomic DNA. Translation: CAB80563.1.
CP002687 Genomic DNA. Translation: AEE87006.1.
AK117850 mRNA. Translation: BAC42491.1.
DQ446906 mRNA. Translation: ABE66120.1.
PIRiT06060.
RefSeqiNP_195611.1. NM_120060.1. [Q8GY58-1]
UniGeneiAt.31125.

3D structure databases

ProteinModelPortaliQ8GY58.
SMRiQ8GY58. Positions 25-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G39000.1-P.

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEiQ8GY58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G39000.1; AT4G39000.1; AT4G39000. [Q8GY58-1]
GeneIDi830055.
KEGGiath:AT4G39000.

Organism-specific databases

TAIRiAT4G39000.

Phylogenomic databases

eggNOGiNOG322234.
InParanoidiQ8GY58.
KOiK01179.
OMAiFQYADSH.
PhylomeDBiQ8GY58.

Enzyme and pathway databases

BioCyciARA:AT4G39000-MONOMER.

Miscellaneous databases

PROiQ8GY58.

Gene expression databases

ExpressionAtlasiQ8GY58. differential.
GenevestigatoriQ8GY58.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
[Graphical view]
PfamiPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  4. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  5. "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.

Entry informationi

Entry nameiGUN23_ARATH
AccessioniPrimary (citable) accession number: Q8GY58
Secondary accession number(s): Q9SVJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: April 29, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The conserved 'Asp-461' active site is replaced by a Gly residue.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.