RGXT2_ARATH
ID RGXT2_ARATH Reviewed; 367 AA.
AC Q9ZSJ0; A0PGM9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Rhamnogalacturonan xylosyltransferase 2 {ECO:0000305};
GN Name=RGXT2 {ECO:0000303|PubMed:17056709}; OrderedLocusNames=At4g01750;
GN ORFNames=T15B16.9, T7B11.1;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Chevalier V., Bruyant P., Pagny S., Morvan C., Gomord V.;
RT "Arabidopsis thaliana putative xylosyltransferase mRNA.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17056709; DOI=10.1105/tpc.105.036566;
RA Egelund J., Petersen B.L., Motawia M.S., Damager I., Faik A., Olsen C.E.,
RA Ishii T., Clausen H., Ulvskov P., Geshi N.;
RT "Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-
RT xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-
RT II.";
RL Plant Cell 18:2593-2607(2006).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18755189; DOI=10.1016/j.febslet.2008.08.015;
RA Egelund J., Damager I., Faber K., Olsen C.E., Ulvskov P., Petersen B.L.;
RT "Functional characterisation of a putative rhamnogalacturonan II specific
RT xylosyltransferase.";
RL FEBS Lett. 582:3217-3222(2008).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19455420; DOI=10.1007/s10719-009-9242-0;
RA Petersen B.L., Egelund J., Damager I., Faber K., Jensen J.K., Yang Z.,
RA Bennett E.P., Scheller H.V., Ulvskov P.;
RT "Assay and heterologous expression in Pichia pastoris of plant cell wall
RT type-II membrane anchored glycosyltransferases.";
RL Glycoconj. J. 26:1235-1246(2009).
CC -!- FUNCTION: Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose
CC onto L-fucose. Probably involved in the biosynthesis of
CC rhamnogalacturonan II (RG-II) through xylosylation of the internal
CC fucose moiety of the A-chain of RG-II, a structurally complex pectic
CC polysaccharide of the primary cell wall. RG-II is essential for the
CC cell wall integrity of rapidly growing tissues such as roots and pollen
CC tube growth and elongation. {ECO:0000269|PubMed:17056709,
CC ECO:0000269|PubMed:19455420}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17056709};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17056709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for UDP-xylose {ECO:0000269|PubMed:18755189,
CC ECO:0000269|PubMed:19455420};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18755189,
CC ECO:0000269|PubMed:19455420};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:17056709}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:17056709}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems and
CC flowers. {ECO:0000269|PubMed:17056709}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17056709}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:17056709}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; AC007138; AAD22637.1; -; Genomic_DNA.
DR EMBL; AF104919; AAC72859.1; -; Genomic_DNA.
DR EMBL; AL161492; CAB77745.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82073.1; -; Genomic_DNA.
DR EMBL; AY065071; AAL38247.1; -; mRNA.
DR EMBL; BT002558; AAO00918.1; -; mRNA.
DR EMBL; AY826518; AAX32892.1; -; mRNA.
DR EMBL; BK005830; DAA05812.1; -; mRNA.
DR PIR; T02000; T02000.
DR RefSeq; NP_192084.1; NM_116405.6.
DR AlphaFoldDB; Q9ZSJ0; -.
DR BioGRID; 13196; 1.
DR IntAct; Q9ZSJ0; 1.
DR STRING; 3702.AT4G01750.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9ZSJ0; -.
DR PRIDE; Q9ZSJ0; -.
DR ProteomicsDB; 236169; -.
DR EnsemblPlants; AT4G01750.1; AT4G01750.1; AT4G01750.
DR GeneID; 827905; -.
DR Gramene; AT4G01750.1; AT4G01750.1; AT4G01750.
DR KEGG; ath:AT4G01750; -.
DR Araport; AT4G01750; -.
DR TAIR; locus:2133457; AT4G01750.
DR eggNOG; ENOG502QT5X; Eukaryota.
DR HOGENOM; CLU_051257_0_0_1; -.
DR InParanoid; Q9ZSJ0; -.
DR OMA; KYRIITH; -.
DR OrthoDB; 819015at2759; -.
DR PhylomeDB; Q9ZSJ0; -.
DR PRO; PR:Q9ZSJ0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSJ0; baseline and differential.
DR Genevisible; Q9ZSJ0; 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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0010306; P:rhamnogalacturonan II biosynthetic process; IMP:TAIR.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03407; Nucleotid_trans; 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..367
FT /note="UDP-D-xylose:L-fucose alpha-1,3-D-
FT xylosyltransferase"
FT /id="PRO_0000423714"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 196..198
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 74
FT /note="S -> C (in Ref. 4; AAX32892)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> F (in Ref. 4; AAX32892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41799 MW; 081700576D044471 CRC64;
MAQKQQTLHQ QRPFSSSPRS YSSISNRPIF LLSRNGLLLV LLALFLLLGV FLPWPGSPLL
LFPNKVSSPS YASSLSPHAK SEWRNYTLAQ AAKFVATNGT VIVCAVSSPF LPFLNNWLIS
VSRQKHQEKV LVIAEDYITL YKVNEKWPGH AVLIPPALDS KTAYSFGSQG FFNFTARRPQ
HLLQILELGY NVMYNDVDMV WLQDPFQYLE GSHDAYFTDD MPQIKPLNHS HDLPAPDQNG
ETYICSCMIY LRPTNGAKLL MKKWSEELQS QAWSESIRFK ANDQPAFNLA LNKTAHQVDL
YLLSQVAFPT GGLYFNDAAW VKETKGKHVI VHNNYIIGYD RKMRRFQDYG LWLVDDHALE
SPLGKLQ
