XYLT_ARATH
ID XYLT_ARATH Reviewed; 534 AA.
AC Q9LDH0; Q9LKK7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Beta-1,2-xylosyltransferase {ECO:0000303|PubMed:10781814};
DE Short=AtXYLT {ECO:0000303|PubMed:22024534};
DE EC=2.4.2.38 {ECO:0000269|PubMed:10781814, ECO:0000269|PubMed:22024534};
GN Name=XYLT {ECO:0000303|PubMed:10781814};
GN OrderedLocusNames=At5g55500 {ECO:0000312|Araport:AT5G55500};
GN ORFNames=MTE17.21 {ECO:0000312|EMBL:BAB08567.1};
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10781814; DOI=10.1016/s0014-5793(00)01443-5;
RA Strasser R., Mucha J., Mach L., Altmann F., Wilson I.B.H., Gloessl J.,
RA Steinkellner H.;
RT "Molecular cloning and functional expression of beta 1,2-xylosyltransferase
RT cDNA from Arabidopsis thaliana.";
RL FEBS Lett. 472:105-108(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bakker H.;
RT "Arabidopsis cDNA for beta1,2-xylosyltransferase.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Gomord V., Baltresca V., Kiefer-Meyer M.-C., Faye L.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12175019; DOI=10.1023/a:1016061815748;
RA Dirnberger D., Bencur P., Mach L., Steinkellner H.;
RT "The Golgi localization of Arabidopsis thaliana beta1,2-xylosyltransferase
RT in plant cells is dependent on its cytoplasmic and transmembrane
RT sequences.";
RL Plant Mol. Biol. 50:273-281(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-51 AND ASN-301, AND
RP MUTAGENESIS OF SER-53 AND THR-303.
RX PubMed=12943552; DOI=10.1046/j.0960-7412.2002.01604.x;
RA Pagny S., Bouissonnie F., Sarkar M., Follet-Gueye M.L., Driouich A.,
RA Schachter H., Faye L., Gomord V.;
RT "Structural requirements for Arabidopsis beta1,2-xylosyltransferase
RT activity and targeting to the Golgi.";
RL Plant J. 33:189-203(2003).
RN [9]
RP FUNCTION.
RX PubMed=15013764; DOI=10.1016/s0014-5793(04)00150-4;
RA Strasser R., Altmann F., Mach L., Gloessl J., Steinkellner H.;
RT "Generation of Arabidopsis thaliana plants with complex N-glycans lacking
RT beta1,2-linked xylose and core alpha1,3-linked fucose.";
RL FEBS Lett. 561:132-136(2004).
RN [10]
RP FUNCTION, AND GLYCOSYLATION AT ASN-51; ASN-301 AND ASN-479.
RX PubMed=15686448; DOI=10.1042/bj20042091;
RA Bencur P., Steinkellner H., Svoboda B., Mucha J., Strasser R., Kolarich D.,
RA Hann S., Koellensperger G., Gloessl J., Altmann F., Mach L.;
RT "Arabidopsis thaliana beta1,2-xylosyltransferase: an unusual
RT glycosyltransferase with the potential to act at multiple stages of the
RT plant N-glycosylation pathway.";
RL Biochem. J. 388:515-525(2005).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22024534; DOI=10.1016/j.jbiosc.2011.09.011;
RA Kajiura H., Okamoto T., Misaki R., Matsuura Y., Fujiyama K.;
RT "Arabidopsis beta1,2-xylosyltransferase: substrate specificity and
RT participation in the plant-specific N-glycosylation pathway.";
RL J. Biosci. Bioeng. 113:48-54(2012).
CC -!- FUNCTION: Glycosyltransferase involved in the xylosylation of N-glycans
CC (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448).
CC Possesses beta-1,2-xylosyltransferase activity, transferring xylose
CC from UDP-xylose to the core beta-linked mannose of N-glycans
CC (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448).
CC Involved in the biosynthesis of glycoprotein bound N-glycans
CC (PubMed:15686448, PubMed:22024534). Does not require metal ions for its
CC activity (PubMed:15686448). {ECO:0000269|PubMed:10781814,
CC ECO:0000269|PubMed:12943552, ECO:0000269|PubMed:15013764,
CC ECO:0000269|PubMed:15686448, ECO:0000269|PubMed:22024534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-alpha-D-xylose = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CC alpha-D-Man-(1->6)]-[beta-D-Xyl-(1->2)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:10612, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13530,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137186; EC=2.4.2.38;
CC Evidence={ECO:0000269|PubMed:10781814, ECO:0000269|PubMed:22024534};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12175019, ECO:0000269|PubMed:12943552}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:12175019,
CC ECO:0000269|PubMed:12943552}. Note=Localizes in medial cisternae of
CC Golgi apparatus. {ECO:0000269|PubMed:12943552}.
CC -!- PTM: Glycosylation at least at one of the two sites Asn-51 and Asn-301
CC is necessary for enzyme stability and activity.
CC {ECO:0000269|PubMed:12943552}.
CC -!- MISCELLANEOUS: Renders plant glycoproteins immunogenic and allergenic
CC in human. This is due to the presence of beta-1,2-xylose and/or core
CC alpha-1,3-fucose which are not found in mammalian proteins, and which
CC constitute epitopes for carbohydrate-reactive antibodies.
CC {ECO:0000305|PubMed:10781814}.
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DR EMBL; AJ272121; CAB90610.1; -; mRNA.
DR EMBL; AJ277603; CAB89489.1; -; mRNA.
DR EMBL; AF272852; AAF77064.1; -; mRNA.
DR EMBL; AB015479; BAB08567.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96635.1; -; Genomic_DNA.
DR EMBL; AF411785; AAL06475.1; -; mRNA.
DR EMBL; AY143907; AAN28846.1; -; mRNA.
DR PIR; T52649; T52649.
DR RefSeq; NP_568825.1; NM_124932.4.
DR AlphaFoldDB; Q9LDH0; -.
DR BioGRID; 20887; 2.
DR STRING; 3702.AT5G55500.1; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR iPTMnet; Q9LDH0; -.
DR PaxDb; Q9LDH0; -.
DR PRIDE; Q9LDH0; -.
DR ProteomicsDB; 242556; -.
DR EnsemblPlants; AT5G55500.1; AT5G55500.1; AT5G55500.
DR GeneID; 835643; -.
DR Gramene; AT5G55500.1; AT5G55500.1; AT5G55500.
DR KEGG; ath:AT5G55500; -.
DR Araport; AT5G55500; -.
DR TAIR; locus:2173892; AT5G55500.
DR eggNOG; KOG4698; Eukaryota.
DR HOGENOM; CLU_026674_0_0_1; -.
DR InParanoid; Q9LDH0; -.
DR OMA; WRSCEGY; -.
DR OrthoDB; 567582at2759; -.
DR PhylomeDB; Q9LDH0; -.
DR BioCyc; ARA:AT5G55500-MON; -.
DR BioCyc; MetaCyc:AT5G55500-MON; -.
DR BRENDA; 2.4.2.38; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LDH0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LDH0; baseline and differential.
DR Genevisible; Q9LDH0; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050513; F:glycoprotein 2-beta-D-xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042285; F:xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:TAIR.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:TAIR.
DR GO; GO:0048367; P:shoot system development; IEA:EnsemblPlants.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..534
FT /note="Beta-1,2-xylosyltransferase"
FT /id="PRO_0000080576"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..534
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12943552,
FT ECO:0000269|PubMed:15686448"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12943552,
FT ECO:0000269|PubMed:15686448"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15686448"
FT MUTAGEN 53
FT /note="S->A: Abolishes stability and activity; when
FT associated with A-303."
FT /evidence="ECO:0000269|PubMed:12943552"
FT MUTAGEN 303
FT /note="T->A: Abolishes stability and activity; when
FT associated with A-53."
FT /evidence="ECO:0000269|PubMed:12943552"
FT CONFLICT 54
FT /note="A -> S (in Ref. 3; AAF77064)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> S (in Ref. 3; AAF77064)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="Missing (in Ref. 3; AAF77064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 60235 MW; A7DCA7FDE8365874 CRC64;
MSKRNPKILK IFLYMLLLNS LFLIIYFVFH SSSFSPEQSQ PPHIYHVSVN NQSAIQKPWP
ILPSYLPWTP PQRNLPTGSC EGYFGNGFTK RVDFLKPRIG GGGEGSWFRC FYSETLQSSI
CEGRNLRMVP DRIVMSRGGE KLEEVMGRKE EEELPAFRQG AFEVAEEVSS RLGFKRHRRF
GGGEGGSAVS RRLVNDEMLN EYMQEGGIDR HTMRDLVASI RAVDTNDFVC EEWVEEPTLL
VTRFEYANLF HTVTDWYSAY VSSRVTGLPN RPHVVFVDGH CTTQLEETWT ALFSGIRYAK
NFTKPVCFRH AILSPLGYET ALFKGLSGEI DCKGDSAHNL WQNPDDKRTA RISEFGEMIR
AAFGLPVNRH RSLEKPLSSS SSSASVYNVL FVRREDYLAH PRHGGKVQSR LINEEEVFDS
LHHWVATGST GLTKCGINLV NGLLAHMSMK DQVRAIQDAS VIIGAHGAGL THIVSATPNT
TIFEIISVEF QRPHFELIAK WKGLEYHAMH LANSRAEPTA VIEKLTEIMK SLGC
