IRX10_ARATH
ID IRX10_ARATH Reviewed; 412 AA.
AC Q9FZJ1; W8PVA7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable beta-1,4-xylosyltransferase IRX10;
DE EC=2.4.2.-;
DE AltName: Full=Glucuronoxylan glucuronosyltransferase 1;
DE Short=AtGUT1;
DE AltName: Full=Glucuronoxylan glucuronosyltransferase 2;
DE AltName: Full=Protein IRREGULAR XYLEM 10;
DE AltName: Full=Xylan xylosyltransferase IRX10;
GN Name=IRX10; Synonyms=GUT1, GUT2; OrderedLocusNames=At1g27440;
GN ORFNames=F17L21.23;
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 [MRNA], WEB RESOURCE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP 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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18980649; DOI=10.1111/j.1365-313x.2008.03724.x;
RA Wu A.-M., Rihouey C., Seveno M., Hoernblad E., Singh S.K., Matsunaga T.,
RA Ishii T., Lerouge P., Marchant A.;
RT "The Arabidopsis IRX10 and IRX10-LIKE glycosyltransferases are critical for
RT glucuronoxylan biosynthesis during secondary cell wall formation.";
RL Plant J. 57:718-731(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18980662; DOI=10.1111/j.1365-313x.2008.03729.x;
RA Brown D.M., Zhang Z., Stephens E., Dupree P., Turner S.R.;
RT "Characterization of IRX10 and IRX10-like reveals an essential role in
RT glucuronoxylan biosynthesis in Arabidopsis.";
RL Plant J. 57:732-746(2009).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls. Probably
CC involved in the elongation of glucuronoxylan xylosyl backbone,
CC especially in the formation of GlcUA side chain of xylans.
CC {ECO:0000269|PubMed:18980649, ECO:0000269|PubMed:18980662,
CC ECO:0000269|PubMed:20424005}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ZUV3}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9ZUV3}.
CC -!- TISSUE SPECIFICITY: Limited to xylem cells. Expressed in the root tip,
CC xylem cells of roots, and in the vasculature of roots, cotyledons and
CC leaves. {ECO:0000269|PubMed:18980649, ECO:0000269|PubMed:20424005}.
CC -!- DEVELOPMENTAL STAGE: In flowers, restricted to anthers.
CC {ECO:0000269|PubMed:18980649}.
CC -!- DISRUPTION PHENOTYPE: Moderate IRX phenotype. Slight reduction of
CC secondary wall thickness and xylan content in cell wall
CC (PubMed:15980264, PubMed:18980662). Specific loss of the GlcUA side
CC chain in xylans. Slightly short inflorescence and reduced fertility
CC (PubMed:18980649). {ECO:0000269|PubMed:15980264,
CC ECO:0000269|PubMed:18980649, ECO:0000269|PubMed:18980662}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=JBEI Glycosyltransferase (GT) Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
CC -!- WEB RESOURCE: Name=CAZY, the Carbohydrate Active enZYmes database;
CC URL="http://www.cazy.org/GT64_all.html";
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DR EMBL; KJ138982; AHL38922.1; -; mRNA.
DR EMBL; AC004557; AAF99743.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30830.1; -; Genomic_DNA.
DR EMBL; BT022053; AAY25465.1; -; mRNA.
DR EMBL; BT025555; ABF58973.1; -; mRNA.
DR RefSeq; NP_174064.1; NM_102508.3.
DR AlphaFoldDB; Q9FZJ1; -.
DR BioGRID; 24870; 9.
DR IntAct; Q9FZJ1; 9.
DR STRING; 3702.AT1G27440.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9FZJ1; -.
DR PRIDE; Q9FZJ1; -.
DR ProteomicsDB; 247050; -.
DR EnsemblPlants; AT1G27440.1; AT1G27440.1; AT1G27440.
DR GeneID; 839635; -.
DR Gramene; AT1G27440.1; AT1G27440.1; AT1G27440.
DR KEGG; ath:AT1G27440; -.
DR Araport; AT1G27440; -.
DR TAIR; locus:2016004; AT1G27440.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_039682_1_0_1; -.
DR InParanoid; Q9FZJ1; -.
DR OMA; DINNDPE; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9FZJ1; -.
DR BioCyc; ARA:AT1G27440-MON; -.
DR PRO; PR:Q9FZJ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZJ1; baseline and differential.
DR Genevisible; Q9FZJ1; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047517; F:1,4-beta-D-xylan synthase activity; IDA:TAIR.
DR GO; GO:0080116; F:glucuronoxylan glucuronosyltransferase activity; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..412
FT /note="Probable beta-1,4-xylosyltransferase IRX10"
FT /id="PRO_0000407576"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 412 AA; 46843 MW; 37F694D052F80D39 CRC64;
MKIHSCLSAI LLFLFFSASS AKQNVRTERI SGSAGDVLED DPVGKLKVYV YELPSKYNKK
LLQKDPRCLT HMFAAEIFMH RFLLSSPVRT RNPDEADWFY TPIYPTCDLT PTGLPLPFKS
PRMMRSSIQL ISSNWPYWNR TEGADHFFVV PHDFGACFHY QEEKAIERGI LPLLQRATLV
QTFGQRNHVC LDEGSITIPP FAPPQKMQAH FIPPDIPRSI FVYFRGLFYD VNNDPEGGYY
ARGARAAVWE NFKNNPLFDI STDHPTTYYE DMQRAIFCLC PLGWAPWSPR LVEAVVFGCI
PVIIADDIVL PFADAIPWEE IGVFVAEKDV PELDTILTSI PTEVILRKQR LLANPSMKRA
MLFPQPAQPG DAFHQILNGL ARKLPHDKSI YLKTGEKALN WTAGPVADLK PW
