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Q94AA9 (XGD1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Xylogalacturonan beta-1,3-xylosyltransferase

EC=2.4.2.41
Alternative name(s):
Protein XYLOGALACTURONAN DEFICIENT 1
Gene names
Name:XGD1
Ordered Locus Names:At5g33290
ORF Names:F19N2.10
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pectin biosynthesis. Catalyzes the transfer of xylose from UDP-xylose onto oligogalacturonides and endogenous acceptors. Ref.5

Catalytic activity

Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose linkage. Ref.5

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Tissue specificity

Highly expressed in adult leaves. Lower levels in young leaves, stems and roots. Ref.5

Induction

Up-regulated by biotic and abiotic stresses and senescence. Down-regulated by cytokinin and nematodes or Agrobacterium infection. Ref.5

Disruption phenotype

Decreased cell wall xylose. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Sequence caution

The sequence AAK83577.1 differs from that shown. Reason: Intron retention.

The sequence BX831739 differs from that shown. Reason: Frameshift at position 210.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Xylogalacturonan beta-1,3-xylosyltransferase
PRO_0000392291

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 500470Lumenal Potential
Compositional bias47 – 10862Ser-rich

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis471 – 50030VLNRP…LRLGT → LIKLTNCGGPKKKKKKKKKK in xgd1-2; loss of activity. Ref.5
Sequence conflict591N → D in BX831739. Ref.4
Sequence conflict1021K → E in BX831739. Ref.4
Sequence conflict110 – 1112KI → RV in BX831739. Ref.4
Sequence conflict2101D → E in BX831739. Ref.4
Sequence conflict2841V → E in AAL62020. Ref.3
Sequence conflict2841V → E in AAK83577. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q94AA9 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: CF7446BDE554CE0A

FASTA50056,600
        10         20         30         40         50         60 
MAAPRSRRCS LSLLTLFSIT LILISVSLFV STKPANKPFL DYRNQFSISI SISSPLEQNT 

        70         80         90        100        110        120 
TNTSFVSASP PLSPLGQSNT TNTILASSSS SSSFSDHQNQ NKSPSPTSKK IVIRKRSGLD 

       130        140        150        160        170        180 
KIESDLAKAR AAIKKAASTQ NYVSSLYKNP AAFHQSHTEM MNRFKVWTYT EGEVPLFHDG 

       190        200        210        220        230        240 
PVNDIYGIEG QFMDEMCVDG PKSRSRFRAD RPENAHVFFI PFSVAKVIHF VYKPITSVEG 

       250        260        270        280        290        300 
FSRARLHRLI EDYVDVVATK HPYWNRSQGG DHFMVSCHDW APDVIDGNPK LFEKFIRGLC 

       310        320        330        340        350        360 
NANTSEGFRP NVDVSIPEIY LPKGKLGPSF LGKSPRVRSI LAFFAGRSHG EIRKILFQHW 

       370        380        390        400        410        420 
KEMDNEVQVY DRLPPGKDYT KTMGMSKFCL CPSGWEVASP REVEAIYAGC VPVIISDNYS 

       430        440        450        460        470        480 
LPFSDVLNWD SFSIQIPVSR IKEIKTILQS VSLVRYLKMY KRVLEVKQHF VLNRPAKPYD 

       490        500 
VMHMMLHSIW LRRLNLRLGT 

« Hide

References

« Hide 'large scale' references
[1]"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: 11130714] [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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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: 14993207] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Identification of a xylogalacturonan xylosyltransferase involved in pectin biosynthesis in Arabidopsis."
Jensen J.K., Sorensen S.O., Harholt J., Geshi N., Sakuragi Y., Moller I., Zandleven J., Bernal A.J., Jensen N.B., Sorensen C., Pauly M., Beldman G., Willats W.G., Scheller H.V.
Plant Cell 20:1289-1302(2008) [PubMed: 18460606] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF 471-VAL--THR-500, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC051625 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93892.1.
AY049234 mRNA. Translation: AAK83577.1. Sequence problems.
AY072629 mRNA. Translation: AAL62020.1.
BX831739 mRNA. No translation available.
IPIIPI00518752.
RefSeqNP_198314.2. NM_122853.3.
UniGeneAt.19950.
At.74966.

3D structure databases

ProteinModelPortalQ94AA9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ94AA9.

Protein family/group databases

CAZyGT47. Glycosyltransferase Family 47.

Proteomic databases

PRIDEQ94AA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G33290.1; AT5G33290.1; AT5G33290.
GeneID833302.
GenomeReviewsGene locus AT5G33290 in contig BA000015_GR.
KEGGath:AT5G33290.

Organism-specific databases

TAIRAt5g33290.

Phylogenomic databases

eggNOGKOG1021.
GeneTreeEPGT00070000028243.
HOGENOMHBG744139.
InParanoidQ94AA9.
OMAFFAGRSH.
PhylomeDBQ94AA9.
ProtClustDBCLSN2918632.

Enzyme and pathway databases

BioCycMetaCyc:AT5G33290-MONOMER.

Gene expression databases

GenevestigatorQ94AA9.

Family and domain databases

InterProIPR004263. Exostosin.
[Graphical view]
PfamPF03016. Exostosin. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXGD1_ARATH
AccessionPrimary (citable) accession number: Q94AA9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: December 14, 2011
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families