Reviewed, UniProtKB/Swiss-Prot Q8VYE5 (E1312_ARATH)

Names and origin

Protein names

Recommended name:
    Putative 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

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	534 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 CAB79694.1 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
Coding sequence diversity	Alternative splicing
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.4 Inferred from direct assay. Source: TAIR 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...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 507	483	Putative glucan endo-1,3-beta-glucosidase 12		PRO_0000251271
	Propeptide	508 – 534	27	Removed in mature form Potential		PRO_0000251272
Regions
	Compositional bias	381 – 387	7	Poly-Gly
Amino acid modifications
	Lipidation	507	1	GPI-anchor amidated serine Potential
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	336	1	N-linked (GlcNAc...) Potential
	Glycosylation	357	1	N-linked (GlcNAc...) Potential
	Glycosylation	375	1	N-linked (GlcNAc...) Potential
	Glycosylation	485	1	N-linked (GlcNAc...) Potential
	Glycosylation	491	1	N-linked (GlcNAc...) Potential
	Glycosylation	495	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	470 – 494	25	YGNCL…GNITG → KYLYTYTFQNTSIKSNVKP in isoform 2.		VSP_020753

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: D76C3E1759D4CA59	FASTA	534	57,659
	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
	Isoform 2. Checksum: 05558FC6F457FFD3	FASTA	528	57,303
	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 SVEVDKDPSK YLYTYTFQNT 490 500 510 520 SIKSNVKPNI TAIDSPLASP SSTNEAFRQM VVAVSVLLPC FVVCSSIW

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]	"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] (ISOFORM 1). Strain: cv. Columbia.
[3]	"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).
[4]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL161574 Genomic DNA. Translation: CAB79694.1. Sequence problems. AY072133 mRNA. Translation: AAL59955.1. AY096465 mRNA. Translation: AAM20105.1. AY088354 mRNA. Translation: AAM65893.1.
IPI	IPI00528724. IPI00541859.
PIR	F85342.
RefSeq	NP_849556.1.
UniGene	At.31933
3D structure databases
HSSP	HSSP built from PDB template 1AQ0 based on UniProtKB P12257.
ModBase	Search...
Protein family/group databases
CAZy	CBM43. Carbohydrate-Binding Module Family 43. GH17. Glycoside Hydrolase Family 17.
Proteomic databases
PRIDE	Q8VYE5.
Genome annotation databases
GeneID	829057.
GenomeReviews	Gene locus AT4G29360 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.20906.
Organism-specific databases
TAIR	At4g29360.
Enzyme and pathway databases
BRENDA	3.2.1.39. 302.
Gene expression databases
GermOnline	AT4G29360. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000490. Glyco_hydro_17. IPR013781. Glyco_hydro_sg_catalytic. IPR012946. X8. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00332. Glyco_hydro_17. 1 hit. PF07983. X8. 1 hit. [Graphical view]
SMART	SM00768. X8. 1 hit. [Graphical view]
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E1312_ARATH

Accession

Primary (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:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)