GT18_ARATH
ID GT18_ARATH Reviewed; 517 AA.
AC F4K6F1; Q9LVB4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Xyloglucan galactosyltransferase XLT2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Glycosyltransferase 18 {ECO:0000303|PubMed:15020758};
DE Short=AtGT18 {ECO:0000303|PubMed:15020758};
DE AltName: Full=Protein XYLOGLUCAN L-SIDE CHAIN GALACTOSYLTRANSFERASE POSITION 2 {ECO:0000303|PubMed:22474179};
GN Name=XLT2 {ECO:0000303|PubMed:22474179};
GN Synonyms=GT18 {ECO:0000303|PubMed:15020758};
GN OrderedLocusNames=At5g62220 {ECO:0000312|Araport:AT5G62220};
GN ORFNames=MMI9.5 {ECO:0000312|EMBL:BAA97186.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15020758; DOI=10.1104/pp.103.036285;
RA Li X., Cordero I., Caplan J., Moelhoej M., Reiter W.D.;
RT "Molecular analysis of 10 coding regions from Arabidopsis that are
RT homologous to the MUR3 xyloglucan galactosyltransferase.";
RL Plant Physiol. 134:940-950(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22474179; DOI=10.1093/mp/sss032;
RA Jensen J.K., Schultink A., Keegstra K., Wilkerson C.G., Pauly M.;
RT "RNA-Seq analysis of developing nasturtium seeds (Tropaeolum majus):
RT identification and characterization of an additional galactosyltransferase
RT involved in xyloglucan biosynthesis.";
RL Mol. Plant 5:984-992(2012).
RN [6]
RP FUNCTION, INTERACTION WITH CSLC4; FUT1; XXT2 AND XXT5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25392066; DOI=10.1093/pcp/pcu161;
RA Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
RT "Protein-protein interactions among xyloglucan-synthesizing enzymes and
RT formation of Golgi-localized multiprotein complexes.";
RL Plant Cell Physiol. 56:255-267(2015).
CC -!- FUNCTION: Functions in xyloglucan synthesis by adding side chains to
CC the xylosylated glucan backbone. Involved in galactosylating
CC hemicellulose xyloglucan (XyG) at the second position of the XXXG motif
CC to form XLXG (PubMed:22474179). Associates with other xyloglucan-
CC synthesizing enzymes to form multiprotein complexes for xyloglucan
CC synthesis in the Golgi (PubMed:25392066). {ECO:0000269|PubMed:22474179,
CC ECO:0000269|PubMed:25392066}.
CC -!- SUBUNIT: Interacts with CSLC4, FUT1, XXT2 and XXT5.
CC {ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22474179, ECO:0000269|PubMed:25392066}; Single-pass
CC type II membrane protein {ECO:0000305|PubMed:25392066}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, cotyledons, leaves,
CC stems and flowers. {ECO:0000269|PubMed:15020758}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138630; AHL38570.1; -; mRNA.
DR EMBL; AB019235; BAA97186.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97582.1; -; Genomic_DNA.
DR RefSeq; NP_201028.1; NM_125616.2.
DR AlphaFoldDB; F4K6F1; -.
DR STRING; 3702.AT5G62220.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR iPTMnet; F4K6F1; -.
DR PaxDb; F4K6F1; -.
DR PRIDE; F4K6F1; -.
DR ProteomicsDB; 230164; -.
DR EnsemblPlants; AT5G62220.1; AT5G62220.1; AT5G62220.
DR GeneID; 836343; -.
DR Gramene; AT5G62220.1; AT5G62220.1; AT5G62220.
DR KEGG; ath:AT5G62220; -.
DR Araport; AT5G62220; -.
DR TAIR; locus:2167933; AT5G62220.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_4_2_1; -.
DR InParanoid; F4K6F1; -.
DR OMA; AVDCRGT; -.
DR OrthoDB; 585148at2759; -.
DR PRO; PR:F4K6F1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K6F1; baseline and differential.
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:0008378; F:galactosyltransferase activity; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0009969; P:xyloglucan biosynthetic 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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..517
FT /note="Xyloglucan galactosyltransferase XLT2"
FT /id="PRO_0000435999"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..517
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 517 AA; 59645 MW; 5CB6115C7A4DC0BC CRC64;
MLPVSNPSSP EHLLKKSRTP DSTTSIDRKN SFNSLHSVGN RSSYIAASRS HCTWLILSLL
SLQLILFLTL RSIPFPHRHI PENFPSPAAV VTTTVTTTVI SAASSNPPLS SSSSDERCDS
GRVFVYDMPK IFNEVILQQC DNLNPWSSRC DALSNDGFGQ EATSLSNVIP KDLVQSWFWT
DQFVTEIIFH NRILNHRCRT LDPESATAFY IPFYAGLAVG QYLWSNYAAA DRDRHCKMMT
QWVKNQPYWN RSNGWDHFIT MGRITWDFRR SKDEDWGSNC IYIPGMRNIT RLLIERNSWD
HFDVGVPYPT GFHPRSDSDV VNWQDFVRNR RRETLFCFAG APRAGIVNDF RGLLLRHCEE
SRGKCRTVDC TVGKCSNGSS AILETFLGSD FCLQPRGDSF TRRSIFDCML AGSIPVFFWR
RSAYMQYQWF LPDKPDSYSV FIDRNEVTNG TTSIKEVLER YSKEDVRKMR ERVIDLIPNL
VYAKSPNGLE TFKDAFDVAI DGVFRRFKEQ EKWYKWR
