Q9C7U5 (E132_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucan endo-1,3-beta-glucosidase 2
EC=3.2.1.39

Alternative name(s):
(1->3)-beta-glucan endohydrolase 2
Short name=(1->3)-beta-glucanase 2
Beta-1,3-endoglucanase 2
Short name=Beta-1,3-glucanase 2

Gene names

Ordered Locus Names:	At1g66250
ORF Names:	T6J19.7

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	505 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	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.
Sequence caution	The sequence AAG51762.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to plasma membrane Inferred from direct assay Ref.4. Source: TAIR
Molecular_function	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 – 20	20	Potential
	Chain	21 – 477	457	Glucan endo-1,3-beta-glucosidase 2		PRO_0000252330
	Propeptide	478 – 505	28	Removed in mature form Potential		PRO_0000252331
Sites
	Active site	272	1	Nucleophile By similarity
	Active site	334	1	Proton donor By similarity
Amino acid modifications
	Lipidation	477	1	GPI-anchor amidated serine Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	180	1	N-linked (GlcNAc...) Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Glycosylation	304	1	N-linked (GlcNAc...) Potential
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
	Glycosylation	365	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
	Glycosylation	466	1	N-linked (GlcNAc...) Potential
	Glycosylation	473	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9C7U5 [UniParc]. Last modified October 3, 2006. Version 2. Checksum: 1A1CC342B307F29F	FASTA	505	54,206
	10 20 30 40 50 60 MASLLHLLLL SLSLLVLASA SPSPPADEGS YIGVNIGTDL SDMPHPTQVV ALLKAQEIRH 70 80 90 100 110 120 IRLYNADPGL LIALANTGIK VIISIPNDQL LGIGQSNSTA ANWVKRNVIA HYPATMITAV 130 140 150 160 170 180 SVGSEVLTSL SNAAPVLVSA IKNVHAALLS ANLDKLIKVS TPLSTSLILD PFPPSQAFFN 190 200 210 220 230 240 RSLNAVIVPL LSFLQSTNSY LMVNVYPYID YMQSNGVIPL DYALFKPIPP NKEAVDANTL 250 260 270 280 290 300 VRYSNAFDAM VDATYFAMAF LNFTNIPVLV TESGWPSKGE TNEPDATLDN ANTYNSNLIR 310 320 330 340 350 360 HVLNKTGTPK RPGIAVSTYI YELYNEDTKA GLSEKNWGLF NANGEPVYVL RLTNSGSVLA 370 380 390 400 410 420 NDTTNQTYCT AREGADTKML QAALDWACGP GKIDCSPIKQ GETCYEPDNV VAHANYAFDT 430 440 450 460 470 480 YYHQTGNNPD ACNFNGVASI TTTDPSHGTC VFAGSRGNGR NGTSVNITAP SANSTTSSGI 490 500 RSDLYYSRGI WSILTVMILN VANIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [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]	"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation." Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M. Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis." Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P. Plant Physiol. 132:568-577(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Callus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC066691 Genomic DNA. Translation: AAG51762.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE34485.1. BX814184 mRNA. No translation available.
IPI	IPI00525275.
PIR	E96687.
RefSeq	NP_176799.2. NM_105296.2.
UniGene	At.49486.
3D structure databases
HSSP	HSSP built from PDB template 1GHS based on UniProtKB P15737.
ProteinModelPortal	Q9C7U5.
SMR	Q9C7U5. Positions 32-348, 367-452.
ModBase	Search...
Protein family/group databases
CAZy	CBM43. Carbohydrate-Binding Module Family 43. GH17. Glycoside Hydrolase Family 17.
Proteomic databases
PaxDb	Q9C7U5.
PRIDE	Q9C7U5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G66250.1; AT1G66250.1; AT1G66250.
GeneID	842942.
KEGG	ath:AT1G66250.
Organism-specific databases
TAIR	At1g66250.
Phylogenomic databases
eggNOG	NOG290245.
HOGENOM	HOG000238220.
InParanoid	Q9C7U5.
OMA	SHGTCVF.
PhylomeDB	Q9C7U5.
ProtClustDB	CLSN2918516.
Gene expression databases
ArrayExpress	Q9C7U5.
Genevestigator	Q9C7U5.
GermOnline	AT1G66250. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR000490. Glyco_hydro_17. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. IPR012946. X8. [Graphical view]
Pfam	PF00332. Glyco_hydro_17. 1 hit. PF07983. X8. 1 hit. [Graphical view]
SMART	SM00768. X8. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E132_ARATH

Accession

Primary (citable) accession number: Q9C7U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program