RGXT1_ARATH
ID RGXT1_ARATH Reviewed; 361 AA.
AC Q9ZSJ2; Q6DYB4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Rhamnogalacturonan xylosyltransferase 1 {ECO:0000305};
GN Name=RGXT1 {ECO:0000303|PubMed:17056709}; OrderedLocusNames=At4g01770;
GN ORFNames=T15B16.8, T7B11.3;
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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (AUG-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=60 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, cauline leaves
CC and stems. {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; AAD22639.1; -; Genomic_DNA.
DR EMBL; AF104919; AAC72867.1; -; Genomic_DNA.
DR EMBL; AL161492; CAB77747.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82075.1; -; Genomic_DNA.
DR EMBL; AY924810; AAX23885.1; -; mRNA.
DR EMBL; AY630791; AAT67590.1; -; mRNA.
DR EMBL; BK005829; DAA05811.1; -; mRNA.
DR PIR; T01998; T01998.
DR RefSeq; NP_192086.1; NM_116407.4.
DR AlphaFoldDB; Q9ZSJ2; -.
DR STRING; 3702.AT4G01770.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9ZSJ2; -.
DR PRIDE; Q9ZSJ2; -.
DR ProteomicsDB; 236930; -.
DR EnsemblPlants; AT4G01770.1; AT4G01770.1; AT4G01770.
DR GeneID; 828129; -.
DR Gramene; AT4G01770.1; AT4G01770.1; AT4G01770.
DR KEGG; ath:AT4G01770; -.
DR Araport; AT4G01770; -.
DR TAIR; locus:2133392; AT4G01770.
DR eggNOG; ENOG502QT5X; Eukaryota.
DR HOGENOM; CLU_051257_0_0_1; -.
DR InParanoid; Q9ZSJ2; -.
DR OMA; MDDKTTI; -.
DR PhylomeDB; Q9ZSJ2; -.
DR PRO; PR:Q9ZSJ2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSJ2; baseline and differential.
DR Genevisible; Q9ZSJ2; 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..361
FT /note="UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
FT 1"
FT /id="PRO_0000423713"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..361
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 190..192
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 353
FT /note="L -> P (in Ref. 4; AAT67590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41174 MW; DDCAACD4883E6A19 CRC64;
MEQKQHILKQ STFSSSPSSY SSISDRPISL LSRNGLLLLL LALVLLLGVL LPWPGSPLFL
FPNRLSSSLS PSPQSKWRDY TLAQAARFVA KNGTVIVCAV SSPFLPFLNN WLISVSRQKH
QDKVLVIAED YITLYKVNEK WPGHAVLIPP ALDSKTAFSF GSQGFFNFTA RRPQHLLQIL
ELGYNVMYND VDMVWLQDPF LYLEGSHDAY FTDDMPQIKP LNHSHDLPHP DRNGETYICS
CMIYLRPTNG AKLLMKKWSE ELQSQAWSES IRFKANDQPA FNLALNKTAH QVDLYLLSQV
AFPTGGLYFK NEAWVQETKG KHVIVHNNYI IGYDRKMKRF QDYGLWLVDD HALESPLGKL
E
