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Q8VYE5 (E1312_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-glucosidase 12
EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase 12
Short name=(1->3)-beta-glucanase 12
Beta-1,3-endoglucanase 12
Short name=Beta-1,3-glucanase 12
Gene names
Ordered Locus Names:At4g29360
ORF Names:F17A13.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 CAB79694.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VYE5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VYE5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-494: YGNCLYMIAPATDGFNRTMAGNITG → KYLYTYTFQNTSIKSNVKP
Note: May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 507483Glucan endo-1,3-beta-glucosidase 12
PRO_0000251271
Propeptide508 – 53427Removed in mature form Potential
PRO_0000251272

Regions

Compositional bias381 – 3877Poly-Gly

Sites

Active site2641Nucleophile By similarity
Active site3271Nucleophile By similarity

Amino acid modifications

Lipidation5071GPI-anchor amidated serine Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation4951N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence470 – 49425YGNCL…GNITG → KYLYTYTFQNTSIKSNVKP in isoform 2.
VSP_020753

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D76C3E1759D4CA59

FASTA53457,659
        10         20         30         40         50         60 
MGQRLNLVFW IFVSILAFLN FGMASKIGIC YGRNADNLPS PNRVSELIQH LNIKFVRIYD 

        70         80         90        100        110        120 
ANIDVLKAFA NTGIELMIGV PNADLLAFAQ FQSNVDTWLS NNILPYYPST KITSISVGLE 

       130        140        150        160        170        180 
VTEAPDNATG LVLPAMRNIH TALKKSGLDK KIKISSSHSL AILSRSFPPS SASFSKKHSA 

       190        200        210        220        230        240 
FLKPMLEFLV ENESPFMIDL YPYYAYRDST EKVPLEYALF ESSSQVVDPA TGLLYSNMFD 

       250        260        270        280        290        300 
AQLDAIYFAL TAMSFKTVKV MVTESGWPSK GSPKETAATP ENALAYNTNL IRHVIGDPGT 

       310        320        330        340        350        360 
PAKPGEEIDV YLFSLFNENR KPGIESERNW GMFYANGTNV YALDFTGENT TPVSPTNSTT 

       370        380        390        400        410        420 
GTSPSPSSSP IINGNSTVTI GGGGGGGTKK WCIASSQASV TELQTALDWA CGPGNVDCSA 

       430        440        450        460        470        480 
VQPDQPCFEP DTVLSHASYA FNTYYQQSGA SSIDCSFNGA SVEVDKDPSY GNCLYMIAPA 

       490        500        510        520        530 
TDGFNRTMAG NITGNITAID SPLASPSSTN EAFRQMVVAV SVLLPCFVVC SSIW

« Hide

Isoform 2 [UniParc].

Checksum: 05558FC6F457FFD3
Show »

FASTA52857,303

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] [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]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL161574 Genomic DNA. Translation: CAB79694.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85622.1.
AY072133 mRNA. Translation: AAL59955.1.
AY096465 mRNA. Translation: AAM20105.1.
AY088354 mRNA. Translation: AAM65893.1.
IPIIPI00528724.
IPI00541859.
PIRF85342.
RefSeqNP_567828.3. NM_119081.5.
NP_849556.1. NM_179225.3.
UniGeneAt.31933.

3D structure databases

HSSPHSSP built from PDB template 2CYG based on UniProtKB O22317.
ProteinModelPortalQ8VYE5.
SMRQ8VYE5. Positions 27-345.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G29360.1-P.

Protein family/group databases

CAZyCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Proteomic databases

PaxDbQ8VYE5.
PRIDEQ8VYE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G29360.1; AT4G29360.1; AT4G29360.
GeneID829057.
KEGGath:AT4G29360.

Organism-specific databases

TAIRAt4g29360.

Phylogenomic databases

eggNOGNOG322041.
HOGENOMHOG000238220.
InParanoidQ8VYE5.
OMARIYDANI.
PhylomeDBQ8VYE5.
ProtClustDBCLSN2687189.

Gene expression databases

ArrayExpressQ8VYE5.
GenevestigatorQ8VYE5.
GermOnlineAT4G29360. Arabidopsis thaliana.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE1312_ARATH
AccessionPrimary (citable) accession number: Q8VYE5
Secondary accession number(s): Q8L9M3, Q9M0E7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents