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Reviewed, UniProtKB/Swiss-Prot Q8L7I0 (GUN19_ARATH)

Last modified June 16, 2009. Version 46. 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 19
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta glucanase 19
Gene names
Ordered Locus Names: At4g11050
ORF Names: F2P3.1, T22B4.30
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 length626 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.

Sequence caution

The sequence AAC35539.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB43040.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB81206.1 differs from that shown. Reason: Erroneous gene model prediction.

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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 functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cellulase 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 – 2323 Potential
Chain24 – 626603Endoglucanase 19
PRO_0000249271

Sites

Active site4121 By similarity
Active site4641 By similarity
Active site4731 By similarity

Amino acid modifications

Glycosylation5601N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8L7I0-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6F7457C97EEF655F

FASTA62669,345
        10         20         30         40         50         60 
MGSRTTISIL VVLLLGLVQL AISGHDYKQA LSKSILFFEA QRSGHLPPNQ RVSWRSHSGL 

        70         80         90        100        110        120 
YDGKSSGVDL VGGYYDAGDN VKFGLPMAFT VTTMCWSIIE YGGQLESNGE LGHAIDAVKW 

       130        140        150        160        170        180 
GTDYFIKAHP EPNVLYGEVG DGKSDHYCWQ RPEEMTTDRR AYKIDRNNPG SDLAGETAAA 

       190        200        210        220        230        240 
MAAASIVFRR SDPSYSAELL RHAHQLFEFA DKYRGKYDSS ITVAQKYYRS VSGYNDELLW 

       250        260        270        280        290        300 
AAAWLYQATN DKYYLDYLGK NGDSMGGTGW SMTEFGWDVK YAGVQTLVAK VLMQGKGGEH 

       310        320        330        340        350        360 
TAVFERYQQK AEQFMCSLLG KSTKNIKKTP GGLIFRQSWN NMQFVTSASF LATVYSDYLS 

       370        380        390        400        410        420 
YSKRDLLCSQ GNISPSQLLE FSKSQVDYIL GDNPRATSYM VGYGENYPRQ VHHRGSSIVS 

       430        440        450        460        470        480 
FNVDQKFVTC RGGYATWFSR KGSDPNVLTG ALVGGPDAYD NFADQRDNYE QTEPATYNNA 

       490        500        510        520        530        540 
PLLGVLARLI SGSTGFDQLL PGVSPTPSPV IIKPAPVPQR KPTKPPAASS PSPITISQKM 

       550        560        570        580        590        600 
TNSWKNEGKV YYRYSTILTN RSTKTLKILK ISITKLYGPI WGVTKTGNSF SFPSWMQSLP 

       610        620 
SGKSMEFVYI HSASPADVLV SNYSLE

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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].
[2]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.

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Cross-references

Sequence databases

AF080120 Genomic DNA. Translation: AAC35539.1. Sequence problems.
AL049876 Genomic DNA. Translation: CAB43040.1. Sequence problems.
AL161518 Genomic DNA. Translation: CAB81206.1. Sequence problems.
AY133685 mRNA. Translation: AAM91619.1.
IPIIPI00523137.
PIRT01929.
RefSeqNP_192843.2.
UniGeneAt.33589

3D structure databases

HSSPHSSP built from PDB template 1IA6 based on UniProtKB Q9EYQ2.
ModBaseSearch...

Protein family/group databases

CAZyCBM49. Carbohydrate-Binding Module Family 49.
GH9. Glycoside Hydrolase Family 9.

Genome annotation databases

GeneID826706.
GenomeReviewsGene locus AT4G11050 in contig CT486007_GR.
KEGGath:AT4G11050.
NMPDRfig|3702.1.peg.18770.

Organism-specific databases

TAIRAt4g11050.

Phylogenomic databases

OMAQ8L7I0. YSANMAM.

Enzyme and pathway databases

BRENDA3.2.1.4. 302.

Gene expression databases

GermOnlineAT4G11050. Arabidopsis thaliana.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR019028. CBM_49.
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.
PfamPF09478. CBM49. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGUN19_ARATH
AccessionPrimary (citable) accession number: Q8L7I0
Secondary accession number(s): O82513
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 46 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