XGD1_ARATH
ID XGD1_ARATH Reviewed; 500 AA.
AC Q94AA9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Xylogalacturonan beta-1,3-xylosyltransferase;
DE EC=2.4.2.41;
DE AltName: Full=Protein XYLOGALACTURONAN DEFICIENT 1;
GN Name=XGD1; OrderedLocusNames=At5g33290; ORFNames=F19N2.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF
RP 471-VAL--THR-500, AND DISRUPTION PHENOTYPE.
RX PubMed=18460606; DOI=10.1105/tpc.107.050906;
RA Jensen J.K., Sorensen S.O., Harholt J., Geshi N., Sakuragi Y., Moller I.,
RA Zandleven J., Bernal A.J., Jensen N.B., Sorensen C., Pauly M., Beldman G.,
RA Willats W.G., Scheller H.V.;
RT "Identification of a xylogalacturonan xylosyltransferase involved in pectin
RT biosynthesis in Arabidopsis.";
RL Plant Cell 20:1289-1302(2008).
CC -!- FUNCTION: Involved in pectin biosynthesis. Catalyzes the transfer of
CC xylose from UDP-xylose onto oligogalacturonides and endogenous
CC acceptors. {ECO:0000269|PubMed:18460606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a xylosyl residue from UDP-D-xylose to a D-galactose
CC residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose
CC linkage.; EC=2.4.2.41; Evidence={ECO:0000269|PubMed:18460606};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult leaves. Lower levels in
CC young leaves, stems and roots. {ECO:0000269|PubMed:18460606}.
CC -!- INDUCTION: Up-regulated by biotic and abiotic stresses and senescence.
CC Down-regulated by cytokinin and nematodes or Agrobacterium infection.
CC {ECO:0000269|PubMed:18460606}.
CC -!- DISRUPTION PHENOTYPE: Decreased cell wall xylose.
CC {ECO:0000269|PubMed:18460606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK83577.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BX831739; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC051625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93892.1; -; Genomic_DNA.
DR EMBL; AY049234; AAK83577.1; ALT_SEQ; mRNA.
DR EMBL; AY072629; AAL62020.1; -; mRNA.
DR EMBL; BX831739; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_198314.2; NM_122853.4.
DR AlphaFoldDB; Q94AA9; -.
DR BioGRID; 18560; 1.
DR STRING; 3702.AT5G33290.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q94AA9; -.
DR PRIDE; Q94AA9; -.
DR ProteomicsDB; 242490; -.
DR EnsemblPlants; AT5G33290.1; AT5G33290.1; AT5G33290.
DR GeneID; 833302; -.
DR Gramene; AT5G33290.1; AT5G33290.1; AT5G33290.
DR KEGG; ath:AT5G33290; -.
DR Araport; AT5G33290; -.
DR TAIR; locus:2145924; AT5G33290.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_025166_1_4_1; -.
DR InParanoid; Q94AA9; -.
DR OMA; DEMCVDG; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q94AA9; -.
DR BioCyc; MetaCyc:AT5G33290-MON; -.
DR BRENDA; 2.4.2.41; 399.
DR PRO; PR:Q94AA9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AA9; baseline and differential.
DR Genevisible; Q94AA9; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0102983; F:xylogalacturonan beta-1,3-xylosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0010398; P:xylogalacturonan metabolic process; IMP:TAIR.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 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..500
FT /note="Xylogalacturonan beta-1,3-xylosyltransferase"
FT /id="PRO_0000392291"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..500
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 62..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 471..500
FT /note="VLNRPAKPYDVMHMMLHSIWLRRLNLRLGT->LIKLTNCGGPKKKKKKKKKK
FT : In xgd1-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:18460606"
FT CONFLICT 59
FT /note="N -> D (in Ref. 4; BX831739)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="K -> E (in Ref. 4; BX831739)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="KI -> RV (in Ref. 4; BX831739)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="D -> E (in Ref. 4; BX831739)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="V -> E (in Ref. 3; AAL62020/AAK83577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56600 MW; CF7446BDE554CE0A CRC64;
MAAPRSRRCS LSLLTLFSIT LILISVSLFV STKPANKPFL DYRNQFSISI SISSPLEQNT
TNTSFVSASP PLSPLGQSNT TNTILASSSS SSSFSDHQNQ NKSPSPTSKK IVIRKRSGLD
KIESDLAKAR AAIKKAASTQ NYVSSLYKNP AAFHQSHTEM MNRFKVWTYT EGEVPLFHDG
PVNDIYGIEG QFMDEMCVDG PKSRSRFRAD RPENAHVFFI PFSVAKVIHF VYKPITSVEG
FSRARLHRLI EDYVDVVATK HPYWNRSQGG DHFMVSCHDW APDVIDGNPK LFEKFIRGLC
NANTSEGFRP NVDVSIPEIY LPKGKLGPSF LGKSPRVRSI LAFFAGRSHG EIRKILFQHW
KEMDNEVQVY DRLPPGKDYT KTMGMSKFCL CPSGWEVASP REVEAIYAGC VPVIISDNYS
LPFSDVLNWD SFSIQIPVSR IKEIKTILQS VSLVRYLKMY KRVLEVKQHF VLNRPAKPYD
VMHMMLHSIW LRRLNLRLGT
