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Q8VZR2 (ASD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-L-arabinofuranosidase 2

Short name=AtASD2
EC=3.2.1.55
Alternative name(s):
Beta-D-xylosidase
EC=3.2.1.-
Gene names
Name:ASD2
Synonyms:ARAF2
Ordered Locus Names:At5g26120
ORF Names:T1N24.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in the coordinated dissolution of the cell wall matrix during abscission and in the secondary cell wall formation in xylem vessels. Ref.5

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Subcellular location

Secretedextracellular spaceextracellular matrix Potential.

Tissue specificity

High expression in flowers, siliques and stems. Observed in the vasculature of older root tissue, at the tip of anthers and in the petal blade of fully developed flowers, in floral abscission zones and in silique replum tissue. Expressed in the cambium and phloem, but not in the xylem or in the vascular system of floral tissues. Ref.1 Ref.5

Induction

Not induced by hormones or during leaf senescence. Ref.1

Disruption phenotype

No visible phenotype, even in asd1 and asd2 double mutant. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Sequence caution

The sequence AAD40132.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 674650Alpha-L-arabinofuranosidase 2
PRO_0000384372

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5481N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8VZR2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C9FD37B9F397890B

FASTA67475,439
        10         20         30         40         50         60 
MDMETSWRFL RSVCLLSFIL GSFSVYQTLC LVDAQEDAIV TLQVDASNVT RRPIPETLFG 

        70         80         90        100        110        120 
IFFEEINHAG AGGLWAELVS NRGFEAGGQI IPSNIWPWSI IGDESSIYVV TDRSSCFERN 

       130        140        150        160        170        180 
KIALRMEVLC DSNSCPLGGV GVYNPGYWGM NIEEGKKYKV VLYVRSTGDI DVSVSFTSSN 

       190        200        210        220        230        240 
GSVTLASENI IALASDLLNW TKKEMLLEAN GTDNGARLQF TTTKKGSIWF DQVSAMPMDT 

       250        260        270        280        290        300 
YKGHGFRNDL FQMMVDLKPR FIRFPGGCFV EGDWLGNAFR WKETVRAWEE RPGHYGDVWK 

       310        320        330        340        350        360 
YWTDDGLGHF EFFQLAEDLG ASPIWVFNNG ISHNDQVETK NVMPFVQEAI DGIEFARGDS 

       370        380        390        400        410        420 
NSTWGSVRAA MGHPEPFELK YVAVGNEDCF KSYYRGNYLE FYNAIKKAYP DIKIISNCDA 

       430        440        450        460        470        480 
SAKPLDHPAD YFDYHIYTLA RDLFSKSHDF DNTPRNGPKA FVSEYAVNKA DAKNGNLLAA 

       490        500        510        520        530        540 
LGEAAFLLGL EKNSDIVEMV SYAPLFVNTN DRRWIPDAIV FNSSHLYGTP SYWVQHFFTE 

       550        560        570        580        590        600 
SSGATLLNST LKGKTSSVEA SAISFQTNGK DYIQIKAVNF GEQSVNLKVA VTGLMAKFYG 

       610        620        630        640        650        660 
SKKKVLTSAS VMDENSFSNP NMIVPQESLL EMTEQEDLMF VLPPHSFSSF DLLTESENVI 

       670 
KMPISDSYKK TSTM 

« Hide

References

« Hide 'large scale' references
[1]"Two alpha-L-arabinofuranosidase genes in Arabidopsis thaliana are differentially expressed during vegetative growth and flower development."
Fulton L.M., Cobbett C.S.
J. Exp. Bot. 54:2467-2477(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY HORMONES.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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].
Strain: cv. Columbia.
[5]"Cell wall modifications in Arabidopsis plants with altered alpha-L-arabinofuranosidase activity."
Chavez Montes R.A., Ranocha P., Martinez Y., Minic Z., Jouanin L., Marquis M., Saulnier L., Fulton L.M., Cobbett C.S., Bitton F., Renou J.-P., Jauneau A., Goffner D.
Plant Physiol. 147:63-77(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY243510 mRNA. Translation: AAO92262.1.
AF149413 Genomic DNA. Translation: AAD40132.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93527.1.
AY063925 mRNA. Translation: AAL36281.1.
BT006062 mRNA. Translation: AAP04047.1.
RefSeqNP_197984.2. NM_122513.3.
UniGeneAt.27144.

3D structure databases

ProteinModelPortalQ8VZR2.
SMRQ8VZR2. Positions 228-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G26120.1-P.

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Proteomic databases

PaxDbQ8VZR2.
PRIDEQ8VZR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G26120.1; AT5G26120.1; AT5G26120.
GeneID832681.
KEGGath:AT5G26120.

Organism-specific databases

TAIRAT5G26120.

Phylogenomic databases

eggNOGCOG3534.
HOGENOMHOG000115340.
InParanoidQ8VZR2.
KOK01209.
OMAHNDQVET.
PhylomeDBQ8VZR2.

Enzyme and pathway databases

BioCycARA:AT5G26120-MONOMER.

Gene expression databases

GenevestigatorQ8VZR2.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR010720. Alpha-L-AF_C.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASD2_ARATH
AccessionPrimary (citable) accession number: Q8VZR2
Secondary accession number(s): Q9XH04
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names