Reviewed, UniProtKB/Swiss-Prot Q9M069 (E137_ARATH)

Names and origin

Protein names

Recommended name:
    Glucan endo-1,3-beta-glucosidase 7
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 7
      Short name=(1->3)-beta-glucanase 7
    Beta-1,3-endoglucanase 7
      Short name=Beta-1,3-glucanase 7

Gene names

Ordered Locus Names:	At4g34480
ORF Names:	T4L20.60

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subcellular location	Secreted. Secreted › cell wall. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.
Sequence caution	The sequence CAA18827.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80165.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.2
	Chain	23 – 504	482	Glucan endo-1,3-beta-glucosidase 7		PRO_0000042684
Regions
	Compositional bias	449 – 460	12	Gly-rich
Sites
	Active site	264	1	Nucleophile By similarity UniProtKB P15737
	Active site	327	1	Proton donor By similarity UniProtKB P15737

Sequences

	Sequence		Length	Mass (Da)
	Q9M069-1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 77FF26A6AF36C167	FASTA	504	53,121
	10 20 30 40 50 60 MALSISIYFL LIFLSHFPSS HAEPFIGVNY GQVADNLPPP SETVKLLQST SIQKVRLYGA 70 80 90 100 110 120 DPAIIKALAG TGVGIVIGAA NGDVPSLASD PNAATQWINS NVLPFYPASK IMLITVGNEI 130 140 150 160 170 180 LMSNDPNLVN QLLPAMQNVQ KALEAVSLGG KIKVSTVNSM TVLGSSDPPS SGSFAAGYQT 190 200 210 220 230 240 GLKGILQFLS DTGSPFAINP YPFFAYQSDP RPETLAFCLF EPNAGRVDSK TGIKYTNMFD 250 260 270 280 290 300 AQVDAVHSAL KSMGFEKVEI VVAETGWASR GDANEVGASV DNAKAYNGNL IAHLRSMVGT 310 320 330 340 350 360 PLMPGKPVDT YIFALYDENL KPGPSSERAF GLFKTDLSMV YDVGLAKSSS SSQTPSGKVT 370 380 390 400 410 420 SSGWCVPKKG ATNEELQASL DWACGHGIDC GAIQPGGACF EPNNVVSHAA YAMNMYFQKS 430 440 450 460 470 480 PKQPTDCDFS KTATVTSQNP SYNNCVYPGG GGGGGGGGGG SKAVMNKYVS SDKVEKKNGA 490 500 TEPKVSSSLS FLLIFLSLIF HVYM

References

	« Hide 'large scale' referencesShow '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. , 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]	"Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants." Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P., Slabas A.R. J. Biol. Chem. 272:15841-15848(1997) [PubMed: 9188482] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-38, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL023094 Genomic DNA. Translation: CAA18827.1. Sequence problems. AL161585 Genomic DNA. Translation: CAB80165.1. Sequence problems.
IPI	IPI00536895.
PIR	D85406. T05268.
RefSeq	NP_195174.6.
UniGene	At.54602
3D structure databases
HSSP	HSSP built from PDB template 1GHS based on UniProtKB P15737.
ModBase	Search...
Protein family/group databases
CAZy	GH17. Glycoside Hydrolase Family 17.
Proteomic databases
PRIDE	Q9M069.
Genome annotation databases
GeneID	829599.
GenomeReviews	Gene locus AT4G34480 in contig CT486007_GR.
KEGG	ath:AT4G34480.
NMPDR	fig|3702.1.peg.21520.
Organism-specific databases
TAIR	At4g34480.
Phylogenomic databases
OMA	MAYDAGL.
Enzyme and pathway databases
BRENDA	3.2.1.39. 302.
Gene expression databases
ArrayExpress	Q9M069.
Genevestigator	Q9M069.
GermOnline	AT4G34480. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000490. Glyco_hydro_17. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00332. Glyco_hydro_17. 1 hit. [Graphical view]
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E137_ARATH

Accession

Primary (citable) accession number: Q9M069
Secondary accession number(s): O65675, P80829

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	September 22, 2009
Last modified:	November 3, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)