RGXT3_ARATH
ID RGXT3_ARATH Reviewed; 383 AA.
AC Q9FXA7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Rhamnogalacturonan xylosyltransferase 3 {ECO:0000305};
GN Name=RGXT3 {ECO:0000303|PubMed:18755189}; OrderedLocusNames=At1g56550;
GN ORFNames=F25P12.100;
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=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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
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).
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:18755189}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for UDP-xylose {ECO:0000269|PubMed:18755189};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed around trichome support cells in the
CC adaxial epidermis of rosette leaves, in cauline leaves, petals and both
CC the proximal and distal ends of siliques.
CC {ECO:0000269|PubMed:18755189}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18755189}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; AC009323; AAG09108.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33406.1; -; Genomic_DNA.
DR EMBL; AK117396; BAC42064.1; -; mRNA.
DR EMBL; BT005111; AAO50644.1; -; mRNA.
DR PIR; B96607; B96607.
DR RefSeq; NP_176048.1; NM_104532.4.
DR AlphaFoldDB; Q9FXA7; -.
DR STRING; 3702.AT1G56550.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9FXA7; -.
DR ProteomicsDB; 236902; -.
DR EnsemblPlants; AT1G56550.1; AT1G56550.1; AT1G56550.
DR GeneID; 842108; -.
DR Gramene; AT1G56550.1; AT1G56550.1; AT1G56550.
DR KEGG; ath:AT1G56550; -.
DR Araport; AT1G56550; -.
DR TAIR; locus:2027605; AT1G56550.
DR eggNOG; ENOG502QT5X; Eukaryota.
DR HOGENOM; CLU_051257_0_0_1; -.
DR InParanoid; Q9FXA7; -.
DR OrthoDB; 819015at2759; -.
DR PhylomeDB; Q9FXA7; -.
DR PRO; PR:Q9FXA7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXA7; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
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..383
FT /note="UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
FT 3"
FT /id="PRO_0000423715"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..383
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 180..182
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 383 AA; 43910 MW; EC207CC6EE3E7DD2 CRC64;
MAQQSQRPIS NRHISLLNRN GLILLLLLAL FVILGVFLPL TKSSLFMFPN TTSSSLSPSS
SLSVSDWRDY SLAQAVKFVA KNETVIVCAV SYPFLPFLNN WLISISRQKH QEKVLVIAED
YATLYKVNEK WPGHAVLIPP ALDPQSAHKF GSQGFFNLTS RRPQHLLNIL ELGYNVMYND
VDMVWLQDPF DYLQGSYDAY FMDDMIAIKP LNHSHDLPPL SRSGVTYVCS CMIFLRSTDG
GKLLMKTWVE EIQAQPWNNT QAKKPHDQPA FNRALHKTAN QVKVYLLPQS AFPSGGLYFR
NETWVNETRG KHVIVHNNYI IGYDKKMKRF QDFSLWLVDD HALESPLGKL EIYQEQNTTT
EGKNLTKIVR KQRKNRGKKH KLP