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Q9SXC4 (IRX9H_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. 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:
Probable beta-1,4-xylosyltransferase IRX9H

EC=2.4.2.-
Alternative name(s):
Protein IRREGULAR XYLEM 9 homolog
Xylan xylosyltransferase IRX9H
Gene names
Name:IRX9H
Ordered Locus Names:At1g27600
ORF Names:T17H3.10, T22C5.4
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone. Ref.5 Ref.6

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Probable Ref.5.

Tissue specificity

Expressed in developing interfascicular fibers and xylem cells in stems and developing secondary xylem in roots. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 43 family.

Sequence caution

The sequence AAD45998.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF24965.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAM64331.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Probable beta-1,4-xylosyltransferase IRX9H
PRO_0000407564

Regions

Topological domain1 – 6464Cytoplasmic Potential
Transmembrane65 – 8521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain86 – 394309Lumenal Potential

Amino acid modifications

Modified residue91Phosphoserine Ref.3
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SXC4 [UniParc].

Last modified May 3, 2011. Version 2.
Checksum: B6D2C629147BA6E5

FASTA39445,187
        10         20         30         40         50         60 
MASIRRTLSP MYHDRSHENG GSHKGFTIGG SSSKHNSSQF LSYLTKLLGV TSDPKSSRRG 

        70         80         90        100        110        120 
PWRRPFYQFL VFFLLGFVLG LTPFGKMEDV NGSDRFSFEI KQPYVEERLE NRKREEAAVD 

       130        140        150        160        170        180 
AVSFVAETEN GKKEVNFVPK KLLIVVTPTY NRAMQAYYLN RVAQTLRLVE SPVLWIVVEG 

       190        200        210        220        230        240 
NVASFETSEI LRKTGVMYRH LVCKRNMTSI KDRGVHQRNT ALEHIELHKL DGIVYFADDD 

       250        260        270        280        290        300 
NIYSLELFQS LRQISRFGTW PVAMLAQSKN KAILEGPVCN GSQVIGWHTN EKSKRLRRFH 

       310        320        330        340        350        360 
VDMSGFAFNS TILWDPKRWR RPFSHPTRQL DTVKEGFQET SFIEQVVADE SEMEGVPPAC 

       370        380        390 
SSILNWHLHL DALDVPYPQG WAIQKNLQAL ITMK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 11130712] [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]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[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] OF 78-394.
[5]"The Arabidopsis family GT43 glycosyltransferases form two functionally nonredundant groups essential for the elongation of glucuronoxylan backbone."
Lee C., Teng Q., Huang W., Zhong R., Ye Z.H.
Plant Physiol. 153:526-541(2010) [PubMed: 20335400] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Analysis of the Arabidopsis IRX9/IRX9-L and IRX14/IRX14-L pairs of glycosyltransferase genes reveals critical contributions to biosynthesis of the hemicellulose glucuronoxylan."
Wu A.M., Hoernblad E., Voxeur A., Gerber L., Rihouey C., Lerouge P., Marchant A.
Plant Physiol. 153:542-554(2010) [PubMed: 20424005] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC005916 Genomic DNA. Translation: AAD45998.1. Sequence problems.
AC012375 Genomic DNA. Translation: AAF24965.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30852.1.
CP002684 Genomic DNA. Translation: AEE30853.1.
AY086258 mRNA. Translation: AAM64331.1. Different initiation.
IPIIPI00525685.
RefSeqNP_564290.2. NM_102525.2.
NP_973922.1. NM_202193.1.
UniGeneAt.41047.
At.41048.

3D structure databases

HSSPHSSP built from PDB template 1KWS based on UniProtKB O94766.
ProteinModelPortalQ9SXC4.
SMRQ9SXC4. Positions 141-389.
ModBaseSearch...

Protein family/group databases

CAZyGT43. Glycosyltransferase Family 43.

Proteomic databases

PRIDEQ9SXC4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G27600.1; AT1G27600.1; AT1G27600.
AT1G27600.2; AT1G27600.2; AT1G27600.
GeneID839652.
GenomeReviewsGene locus AT1G27600 in contig CT485782_GR.
KEGGath:AT1G27600.

Organism-specific databases

TAIRAt1g27600.

Phylogenomic databases

GeneTreeEPGT00050000027792.
InParanoidQ9SXC4.
OMAADESEME.

Gene expression databases

GenevestigatorQ9SXC4.

Family and domain databases

InterProIPR005027. Glyco_trans_43.
[Graphical view]
PANTHERPTHR10896. Glyco_trans_43. 1 hit.
PfamPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIRX9H_ARATH
AccessionPrimary (citable) accession number: Q9SXC4
Secondary accession number(s): Q8LD18, Q9SFZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: December 14, 2011
This is version 44 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