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Protein

Glucan endo-1,3-beta-glucosidase 2

Gene

At1g66250

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei272 – 2721NucleophileBy similarity
Active sitei334 – 3341Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

BioCyciARA:AT1G66250-MONOMER.

Protein family/group databases

CAZyiCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
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 namesi
Ordered Locus Names:At1g66250
ORF Names:T6J19.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G66250.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: TAIR
  • anchored component of plasma membrane Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 477457Glucan endo-1,3-beta-glucosidase 2PRO_0000252330Add
BLAST
Propeptidei478 – 50528Removed in mature formSequence AnalysisPRO_0000252331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi369 ↔ 432By similarity
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis
Lipidationi477 – 4771GPI-anchor amidated serineSequence Analysis

Post-translational modificationi

Contains two additional disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9C7U5.
PRIDEiQ9C7U5.

Structurei

3D structure databases

ProteinModelPortaliQ9C7U5.
SMRiQ9C7U5. Positions 32-348, 367-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290245.
HOGENOMiHOG000238220.
InParanoidiQ9C7U5.
OMAiYCTAREG.
PhylomeDBiQ9C7U5.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTiSM00768. X8. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9C7U5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLLHLLLL SLSLLVLASA SPSPPADEGS YIGVNIGTDL SDMPHPTQVV
60 70 80 90 100
ALLKAQEIRH IRLYNADPGL LIALANTGIK VIISIPNDQL LGIGQSNSTA
110 120 130 140 150
ANWVKRNVIA HYPATMITAV SVGSEVLTSL SNAAPVLVSA IKNVHAALLS
160 170 180 190 200
ANLDKLIKVS TPLSTSLILD PFPPSQAFFN RSLNAVIVPL LSFLQSTNSY
210 220 230 240 250
LMVNVYPYID YMQSNGVIPL DYALFKPIPP NKEAVDANTL VRYSNAFDAM
260 270 280 290 300
VDATYFAMAF LNFTNIPVLV TESGWPSKGE TNEPDATLDN ANTYNSNLIR
310 320 330 340 350
HVLNKTGTPK RPGIAVSTYI YELYNEDTKA GLSEKNWGLF NANGEPVYVL
360 370 380 390 400
RLTNSGSVLA NDTTNQTYCT AREGADTKML QAALDWACGP GKIDCSPIKQ
410 420 430 440 450
GETCYEPDNV VAHANYAFDT YYHQTGNNPD ACNFNGVASI TTTDPSHGTC
460 470 480 490 500
VFAGSRGNGR NGTSVNITAP SANSTTSSGI RSDLYYSRGI WSILTVMILN

VANIL
Length:505
Mass (Da):54,206
Last modified:October 3, 2006 - v2
Checksum:i1A1CC342B307F29F
GO

Sequence cautioni

The sequence AAG51762.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC066691 Genomic DNA. Translation: AAG51762.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34485.1.
BX814184 mRNA. No translation available.
PIRiE96687.
RefSeqiNP_176799.2. NM_105296.2.
UniGeneiAt.49486.

Genome annotation databases

EnsemblPlantsiAT1G66250.1; AT1G66250.1; AT1G66250.
GeneIDi842942.
KEGGiath:AT1G66250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC066691 Genomic DNA. Translation: AAG51762.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34485.1.
BX814184 mRNA. No translation available.
PIRiE96687.
RefSeqiNP_176799.2. NM_105296.2.
UniGeneiAt.49486.

3D structure databases

ProteinModelPortaliQ9C7U5.
SMRiQ9C7U5. Positions 32-348, 367-452.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Proteomic databases

PaxDbiQ9C7U5.
PRIDEiQ9C7U5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G66250.1; AT1G66250.1; AT1G66250.
GeneIDi842942.
KEGGiath:AT1G66250.

Organism-specific databases

TAIRiAT1G66250.

Phylogenomic databases

eggNOGiNOG290245.
HOGENOMiHOG000238220.
InParanoidiQ9C7U5.
OMAiYCTAREG.
PhylomeDBiQ9C7U5.

Enzyme and pathway databases

BioCyciARA:AT1G66250-MONOMER.

Miscellaneous databases

PROiQ9C7U5.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTiSM00768. X8. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Strain: cv. Columbia.
    Tissue: Callus.

Entry informationi

Entry nameiE132_ARATH
AccessioniPrimary (citable) accession number: Q9C7U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 22, 2015
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.