IRX9_ARATH
ID IRX9_ARATH Reviewed; 351 AA.
AC Q9ZQC6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Beta-1,4-xylosyltransferase IRX9 {ECO:0000305};
DE EC=2.4.2.24 {ECO:0000269|PubMed:22080591};
DE AltName: Full=Protein IRREGULAR XYLEM 9 {ECO:0000303|PubMed:17944810};
DE AltName: Full=Xylan xylosyltransferase IRX9 {ECO:0000305};
GN Name=IRX9 {ECO:0000303|PubMed:17944810};
GN OrderedLocusNames=At2g37090 {ECO:0000312|Araport:AT2G37090};
GN ORFNames=T2N18.15 {ECO:0000312|EMBL:AAD18150.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15980264; DOI=10.1105/tpc.105.031542;
RA Brown D.M., Zeef L.A.H., Ellis J., Goodacre R., Turner S.R.;
RT "Identification of novel genes in Arabidopsis involved in secondary cell
RT wall formation using expression profiling and reverse genetics.";
RL Plant Cell 17:2281-2295(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17944810; DOI=10.1111/j.1365-313x.2007.03307.x;
RA Brown D.M., Goubet F., Wong V.W., Goodacre R., Stephens E., Dupree P.,
RA Turner S.R.;
RT "Comparison of five xylan synthesis mutants reveals new insight into the
RT mechanisms of xylan synthesis.";
RL Plant J. 52:1154-1168(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17322407; DOI=10.1105/tpc.106.049320;
RA Pena M.J., Zhong R., Zhou G.K., Richardson E.A., O'Neill M.A.,
RA Darvill A.G., York W.S., Ye Z.H.;
RT "Arabidopsis irregular xylem8 and irregular xylem9: implications for the
RT complexity of glucuronoxylan biosynthesis.";
RL Plant Cell 19:549-563(2007).
RN [9]
RP FUNCTION.
RX PubMed=17938130; DOI=10.1093/pcp/pcm135;
RA Lee C., O'Neill M.A., Tsumuraya Y., Darvill A.G., Ye Z.H.;
RT "The irregular xylem9 mutant is deficient in xylan xylosyltransferase
RT activity.";
RL Plant Cell Physiol. 48:1624-1634(2007).
RN [10]
RP FUNCTION.
RX PubMed=20335400; DOI=10.1104/pp.110.155309;
RA Lee C., Teng Q., Huang W., Zhong R., Ye Z.H.;
RT "The Arabidopsis family GT43 glycosyltransferases form two functionally
RT nonredundant groups essential for the elongation of glucuronoxylan
RT backbone.";
RL Plant Physiol. 153:526-541(2010).
RN [11]
RP FUNCTION.
RX PubMed=20424005; DOI=10.1104/pp.110.154971;
RA Wu A.M., Hoernblad E., Voxeur A., Gerber L., Rihouey C., Lerouge P.,
RA Marchant A.;
RT "Analysis of the Arabidopsis IRX9/IRX9-L and IRX14/IRX14-L pairs of
RT glycosyltransferase genes reveals critical contributions to biosynthesis of
RT the hemicellulose glucuronoxylan.";
RL Plant Physiol. 153:542-554(2010).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22080591; DOI=10.1093/pcp/pcr158;
RA Lee C., Zhong R., Ye Z.H.;
RT "Arabidopsis family GT43 members are xylan xylosyltransferases required for
RT the elongation of the xylan backbone.";
RL Plant Cell Physiol. 53:135-143(2012).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-150; GLY-215;
RP 215-GLY-LEU-216; GLU-252 AND CYS-333.
RX PubMed=25118690; DOI=10.1371/journal.pone.0105014;
RA Ren Y., Hansen S.F., Ebert B., Lau J., Scheller H.V.;
RT "Site-directed mutagenesis of IRX9, IRX9L and IRX14 proteins involved in
RT xylan biosynthesis: glycosyltransferase activity is not required for IRX9
RT function in Arabidopsis.";
RL PLoS ONE 9:E105014-E105014(2014).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls
CC (PubMed:15980264, PubMed:16844780, PubMed:17322407, PubMed:17938130,
CC PubMed:17944810, PubMed:20335400, PubMed:20424005). Xylan
CC xylosyltransferase that acts cooperatively with IRX14 to achieve the
CC successive addition of xylosyl residues during xylan backbone
CC elongation (PubMed:22080591, PubMed:25118690).
CC {ECO:0000269|PubMed:15980264, ECO:0000269|PubMed:16844780,
CC ECO:0000269|PubMed:17322407, ECO:0000269|PubMed:17938130,
CC ECO:0000269|PubMed:17944810, ECO:0000269|PubMed:20335400,
CC ECO:0000269|PubMed:20424005, ECO:0000269|PubMed:22080591,
CC ECO:0000269|PubMed:25118690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-xylan](n) + UDP-alpha-D-xylose = [(1->4)-beta-
CC D-xylan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:15289, Rhea:RHEA-
CC COMP:9548, Rhea:RHEA-COMP:9549, ChEBI:CHEBI:15378, ChEBI:CHEBI:15447,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223; EC=2.4.2.24;
CC Evidence={ECO:0000269|PubMed:22080591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15290;
CC Evidence={ECO:0000269|PubMed:22080591};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:17322407}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:17322407}.
CC -!- TISSUE SPECIFICITY: Expressed in developing interfascicular fibers,
CC primary and secondary xylem in stems and developing secondary xylem in
CC roots. {ECO:0000269|PubMed:17322407}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. Collapsed xylem vessels and
CC reduced xylan content in cell wall. {ECO:0000269|PubMed:15980264,
CC ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:17322407,
CC ECO:0000269|PubMed:17944810, ECO:0000269|PubMed:25118690}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AC006260; AAD18150.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09350.1; -; Genomic_DNA.
DR EMBL; BT015044; AAT71916.1; -; mRNA.
DR EMBL; BT015838; AAU94401.1; -; mRNA.
DR PIR; D84788; D84788.
DR RefSeq; NP_181246.1; NM_129265.3.
DR AlphaFoldDB; Q9ZQC6; -.
DR SMR; Q9ZQC6; -.
DR STRING; 3702.AT2G37090.1; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR PaxDb; Q9ZQC6; -.
DR PRIDE; Q9ZQC6; -.
DR ProteomicsDB; 247295; -.
DR EnsemblPlants; AT2G37090.1; AT2G37090.1; AT2G37090.
DR GeneID; 818285; -.
DR Gramene; AT2G37090.1; AT2G37090.1; AT2G37090.
DR KEGG; ath:AT2G37090; -.
DR Araport; AT2G37090; -.
DR TAIR; locus:2061748; AT2G37090.
DR eggNOG; KOG1476; Eukaryota.
DR HOGENOM; CLU_044006_2_0_1; -.
DR InParanoid; Q9ZQC6; -.
DR OMA; TRGVSIW; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9ZQC6; -.
DR BioCyc; ARA:AT2G37090-MON; -.
DR BRENDA; 2.4.2.24; 399.
DR PRO; PR:Q9ZQC6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQC6; baseline and differential.
DR Genevisible; Q9ZQC6; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047517; F:1,4-beta-D-xylan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IEA:InterPro.
DR GO; GO:0042285; F:xylosyltransferase activity; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IGI:TAIR.
DR GO; GO:0010413; P:glucuronoxylan metabolic process; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IMP:TAIR.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Beta-1,4-xylosyltransferase IRX9"
FT /id="PRO_0000407563"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..351
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 80..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 150
FT /note="W->A: Complements irregular xylem phenotype of irx9
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 215..216
FT /note="GL->DD: Complements irregular xylem phenotype of
FT irx9 mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 215
FT /note="G->W: Complements irregular xylem phenotype of irx9
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 252
FT /note="E->A: Complements irregular xylem phenotype of irx9
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 333
FT /note="C->A: Complements irregular xylem phenotype of irx9
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
SQ SEQUENCE 351 AA; 40059 MW; 1F0F48D43B8A3DA1 CRC64;
MGSLERSKKK AQVWKKAVIH FSLCFVMGFF TGFAPAGKAS FFSNFETTSY TSTKSPIPPQ
PFENATYTQH SLLNRTLINS QSQAPAPAES REAEGETRSL SEKEDENQVK VTPRGLVIVV
TPIITKDRYK NVLLRRMANT LRLVPPPLLW IVVEKHSDGE EKSSSTMLRK TGIMYRRIVF
KEDFTSLESE LDHQRNLALR HIEHHKLSGI VHFAGLNNIY DLDFFVKIRD IEVFGTWPMA
LLSANRKRVV VEGPVCESSQ VLGWHLRKIN NETETKPPIH ISSFAFNSSI LWDPERWGRP
SSVEGTKQDS IKYVKQVVLE DDTKLKGLPA QDCSKIMLWR LKFPTRTRLS T
