IRX7_ARATH
ID IRX7_ARATH Reviewed; 448 AA.
AC Q9ZUV3; Q8RXC5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable glucuronoxylan glucuronosyltransferase IRX7;
DE EC=2.4.1.-;
DE AltName: Full=Protein FRAGILE FIBER 8;
DE AltName: Full=Protein IRREGULAR XYLEM 7;
GN Name=IRX7; Synonyms=FRA8; OrderedLocusNames=At2g28110; ORFNames=F24D13.10;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16272433; DOI=10.1105/tpc.105.035501;
RA Zhong R., Pena M.J., Zhou G.K., Nairn C.J., Wood-Jones A., Richardson E.A.,
RA Morrison W.H. III, Darvill A.G., York W.S., Ye Z.H.;
RT "Arabidopsis fragile fiber8, which encodes a putative
RT glucuronyltransferase, is essential for normal secondary wall synthesis.";
RL Plant Cell 17:3390-3408(2005).
RN [2]
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 [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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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.
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 [7]
RP FUNCTION.
RX PubMed=17991630; DOI=10.1093/pcp/pcm155;
RA Lee C., Zhong R., Richardson E.A., Himmelsbach D.S., McPhail B.T., Ye Z.H.;
RT "The PARVUS gene is expressed in cells undergoing secondary wall thickening
RT and is essential for glucuronoxylan biosynthesis.";
RL Plant Cell Physiol. 48:1659-1672(2007).
RN [8]
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).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls. Probably
CC involved in the synthesis of the glycosyl sequence at the
CC glucuronoxylan reducing end. {ECO:0000269|PubMed:15980264,
CC ECO:0000269|PubMed:16272433, ECO:0000269|PubMed:17938130,
CC ECO:0000269|PubMed:17944810, ECO:0000269|PubMed:17991630}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:16272433}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:16272433}.
CC -!- TISSUE SPECIFICITY: Expressed in developing interfascicular fibers and
CC xylem cells in stems and developing secondary xylem in roots.
CC {ECO:0000269|PubMed:16272433}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. Strong reduction of secondary
CC wall thickness, collapsed xylem vessels and reduced xylan content in
CC cell wall. {ECO:0000269|PubMed:15980264, ECO:0000269|PubMed:16272433,
CC ECO:0000269|PubMed:17944810}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL91236.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ182567; ABA60868.1; -; mRNA.
DR EMBL; DQ182568; ABA60869.1; -; Genomic_DNA.
DR EMBL; AC005851; AAC98455.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08081.1; -; Genomic_DNA.
DR EMBL; AY081347; AAL91236.1; ALT_FRAME; mRNA.
DR EMBL; BT006256; AAP13364.1; -; mRNA.
DR PIR; H84680; H84680.
DR RefSeq; NP_850113.2; NM_179782.4.
DR AlphaFoldDB; Q9ZUV3; -.
DR BioGRID; 2707; 1.
DR STRING; 3702.AT2G28110.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9ZUV3; -.
DR PRIDE; Q9ZUV3; -.
DR ProteomicsDB; 247053; -.
DR EnsemblPlants; AT2G28110.1; AT2G28110.1; AT2G28110.
DR GeneID; 817357; -.
DR Gramene; AT2G28110.1; AT2G28110.1; AT2G28110.
DR KEGG; ath:AT2G28110; -.
DR Araport; AT2G28110; -.
DR TAIR; locus:2046163; AT2G28110.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_039682_1_0_1; -.
DR InParanoid; Q9ZUV3; -.
DR OMA; KWIIWIS; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9ZUV3; -.
DR BioCyc; ARA:AT2G28110-MON; -.
DR PRO; PR:Q9ZUV3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUV3; baseline and differential.
DR Genevisible; Q9ZUV3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:0015020; F:glucuronosyltransferase activity; ISS: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..448
FT /note="Probable glucuronoxylan glucuronosyltransferase
FT IRX7"
FT /id="PRO_0000407574"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..448
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 448 AA; 51694 MW; 0C71F7FDD8F0C425 CRC64;
MTTHKHRRTE KNLCFKQYYK WILCFILTLY FFASFFVDHD QDHRSSTSIS KHLLTNHKPK
LFASRAMFES KIHDHKLGFT SQQPNIKTDV FNNLKIYVYD LPSKFNKDWL ANDRCTNHLF
AAEVALHKAF LSLEGDVRTE DPYEADFFFV PVYVSCNFST INGFPAIGHA RSLINDAIKL
VSTQYPFWNR TSGSDHVFTA THDFGSCFHT MEDRAIADGV PIFLRNSIIL QTFGVTFNHP
CQEVENVVIP PYISPESLHK TQKNIPVTKE RDIWVFFRGK MELHPKNISG RFYSKRVRTN
IWRSYGGDRR FYLQRQRFAG YQSEIARSVF CLCPLGWAPW SPRLVESVAL GCVPVIIADG
IRLPFPSTVR WPDISLTVAE RDVGKLGDIL EHVAATNLSV IQRNLEDPSV RRALMFNVPS
REGDATWQVL EALSKKLNRS VRRSNSFL
