Reviewed, UniProtKB/Swiss-Prot Q8L868 (E1311_ARATH)

Names and origin

Protein names

Recommended name:
    Glucan endo-1,3-beta-glucosidase 11
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 11
      Short name=(1->3)-beta-glucanase 11
    Beta-1,3-endoglucanase 11
      Short name=Beta-1,3-glucanase 11

Gene names

Ordered Locus Names:	At1g32860
ORF Names:	F9L11.6

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	426 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 › cell wall Potential. Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.
Sequence caution	The sequence AAF31288.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Plant defense
Cellular component	Cell membrane Cell wall Membrane Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to plasma membrane Ref.3 Inferred from direct assay. Source: TAIR cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell external side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
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 – 30	30	Potential
	Chain	31 – 398	368	Glucan endo-1,3-beta-glucosidase 11		PRO_0000251269
	Propeptide	399 – 426	28	Removed in mature form Potential		PRO_0000251270
Sites
	Active site	266	1	Nucleophile By similarity
	Active site	331	1	Nucleophile By similarity
Amino acid modifications
	Lipidation	398	1	GPI-anchor amidated serine Potential
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
	Glycosylation	367	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8L868-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E40288A0C0543540	FASTA	426	45,421
	10 20 30 40 50 60 MELTSFHRSS LLFLISLTLI ILPTTTTSIG VNYGQIGDNL PSPTDVIPLI KSIGATKVKL 70 80 90 100 110 120 YDANPQILKA FSNTGIEFII GLGNEYLSKM KDPSKALTWI KQNVTPFLPA TNITCITIGN 130 140 150 160 170 180 EILALNDSSL TTNLLPAMQG VHSALITAGL SDQISVTTAH SLSILKSSFP PSAGEFQPDL 190 200 210 220 230 240 LDSLTPILEF HRKTDSPFLI NAYPFFAYKG NPKEVPLDFV LFQPNQGIVD PATGFHYDNM 250 260 270 280 290 300 LFAQIDAVYS ALAAAGFKSL RVEISETGWP SKGDDDEVGA TPENAKRYNG NLIKMMMSGK 310 320 330 340 350 360 KTKTPLKPNN DLSIYVFALF NENLKPGPTS ERNYGLFKPD GTQAYSLGFA LNDVVRGASG 370 380 390 400 410 420 GGTGGGNSSS GGGRDKSPVF PVSPVAPDSA STGYLAISAS PVTGKRKGKG AILSLVVSML LARHLL

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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[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. , 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]	"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins." Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N. Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]	"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment." Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N. J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC006424 Genomic DNA. Translation: AAF31288.1. Sequence problems. AY120710 mRNA. Translation: AAM53268.1. BT000048 mRNA. Translation: AAN15367.1.
IPI	IPI00538729.
PIR	D86453.
RefSeq	NP_174563.2.
UniGene	At.40046
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.
Genome annotation databases
GeneID	840180.
GenomeReviews	Gene locus AT1G32860 in contig CT485782_GR.
KEGG	ath:AT1G32860.
NMPDR	fig|3702.1.peg.3642.
Organism-specific databases
TAIR	At1g32860.
Phylogenomic databases
OMA	TNITCIT.
Enzyme and pathway databases
BRENDA	3.2.1.39. 302.
Gene expression databases
ArrayExpress	Q8L868.
Genevestigator	Q8L868.
GermOnline	AT1G32860. 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

E1311_ARATH

Accession

Primary (citable) accession number: Q8L868
Secondary accession number(s): Q9MAQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 1, 2002
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)