XXT2_ARATH
ID XXT2_ARATH Reviewed; 461 AA.
AC O22775; Q9SYY3; W8QNH8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Xyloglucan 6-xylosyltransferase 2;
DE Short=AtXT2;
DE EC=2.4.2.39;
DE AltName: Full=Putative glycosyltransferase 2;
DE Short=AtGT2;
DE EC=2.4.-.-;
GN Name=XXT2; Synonyms=GT2, GTL5, XT2; OrderedLocusNames=At4g02500;
GN ORFNames=T10P11.20, T14P8.23;
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;
RA Mogelsvang S., Dupree P.;
RT "A novel Arabidopsis Golgi glycosyltransferase.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lao J., Oikawa A., Bromley J.R., Smith-Moritz A.M., Chiu T.-Y.,
RA Christiansen K.M., Hansen S.F., Suttangkakul A., Ebert B., Yang F.,
RA Vega-Sanchez M.E., Stonebloom S., Morrison S., McInerney P., Hadi M.,
RA Adams P.D., Ronald P.C., Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for high-throughput
RT functional genomics.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12032363; DOI=10.1073/pnas.102644799;
RA Faik A., Price N.J., Raikhel N.V., Keegstra K.;
RT "An Arabidopsis gene encoding an alpha-xylosyltransferase involved in
RT xyloglucan biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7797-7802(2002).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16982611; DOI=10.1074/jbc.m606379200;
RA Cavalier D.M., Keegstra K.;
RT "Two xyloglucan xylosyltransferases catalyze the addition of multiple
RT xylosyl residues to cellohexaose.";
RL J. Biol. Chem. 281:34197-34207(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18544630; DOI=10.1105/tpc.108.059873;
RA Cavalier D.M., Lerouxel O., Neumetzler L., Yamauchi K., Reinecke A.,
RA Freshour G., Zabotina O.A., Hahn M.G., Burgert I., Pauly M., Raikhel N.V.,
RA Keegstra K.;
RT "Disrupting two Arabidopsis thaliana xylosyltransferase genes results in
RT plants deficient in xyloglucan, a major primary cell wall component.";
RL Plant Cell 20:1519-1537(2008).
RN [9]
RP NOMENCLATURE.
RX PubMed=18557833; DOI=10.1111/j.1365-313x.2008.03580.x;
RA Zabotina O.A., van de Ven W.T., Freshour G., Drakakaki G., Cavalier D.,
RA Mouille G., Hahn M.G., Keegstra K., Raikhel N.V.;
RT "Arabidopsis XXT5 gene encodes a putative alpha-1,6-xylosyltransferase that
RT is involved in xyloglucan biosynthesis.";
RL Plant J. 56:101-115(2008).
RN [10]
RP INTERACTION WITH XXT1; XXT2 AND XXT5, AND SUBCELLULAR LOCATION.
RX PubMed=22665445; DOI=10.1104/pp.112.199356;
RA Chou Y.H., Pogorelko G., Zabotina O.A.;
RT "Xyloglucan xylosyltransferases XXT1, XXT2, and XXT5 and the glucan
RT synthase CSLC4 form Golgi-localized multiprotein complexes.";
RL Plant Physiol. 159:1355-1366(2012).
RN [11]
RP FUNCTION, INTERACTION WITH FUT1 AND XLT2, AND SUBCELLULAR 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: Xylosyltransferase specific to UDP-D-xylose that accepts both
CC cellopentaose and cellohexaose as substrates, with a better use of
CC cellohexaose, to produce xyloglucan. Adds preferentially the first
CC xylosyl residue to the fourth glucosyl residue from the reducing end of
CC both acceptors. Transfer one xylose mainly to the second glucose
CC residue from the non-reducing end. The acceptor should have a minimum
CC of four glucose residues (PubMed:16982611, PubMed:18544630). Associates
CC with other xyloglucan-synthesizing enzymes to form multiprotein
CC complexes for xyloglucan synthesis in the Golgi (PubMed:25392066).
CC {ECO:0000269|PubMed:16982611, ECO:0000269|PubMed:18544630,
CC ECO:0000269|PubMed:25392066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a
CC glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-
CC glucose linkage.; EC=2.4.2.39;
CC Evidence={ECO:0000269|PubMed:16982611};
CC -!- SUBUNIT: Homodimer (PubMed:22665445). Interacts with XXT1 and XXT5
CC (PubMed:22665445). Interacts with FUT1 and XLT2 (PubMed:25392066).
CC {ECO:0000269|PubMed:22665445, ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22665445, ECO:0000269|PubMed:25392066}; Single-pass
CC type II membrane protein {ECO:0000305|PubMed:25392066}.
CC -!- DISRUPTION PHENOTYPE: Reduced xyloglucan content.
CC {ECO:0000269|PubMed:18544630}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ245571; CAC01674.1; -; mRNA.
DR EMBL; KJ138768; AHL38708.1; -; mRNA.
DR EMBL; AC002330; AAC78266.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF069298; AAC19271.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80743.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82181.1; -; Genomic_DNA.
DR EMBL; AY057598; AAL14393.1; -; mRNA.
DR EMBL; AY140029; AAM98170.1; -; mRNA.
DR EMBL; BT006601; AAP31945.1; -; mRNA.
DR PIR; H85031; H85031.
DR PIR; T01300; T01300.
DR RefSeq; NP_567241.1; NM_116484.3.
DR AlphaFoldDB; O22775; -.
DR SMR; O22775; -.
DR BioGRID; 13231; 7.
DR STRING; 3702.AT4G02500.1; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR PaxDb; O22775; -.
DR PRIDE; O22775; -.
DR ProteomicsDB; 242408; -.
DR EnsemblPlants; AT4G02500.1; AT4G02500.1; AT4G02500.
DR GeneID; 827940; -.
DR Gramene; AT4G02500.1; AT4G02500.1; AT4G02500.
DR KEGG; ath:AT4G02500; -.
DR Araport; AT4G02500; -.
DR TAIR; locus:2132293; AT4G02500.
DR eggNOG; KOG4748; Eukaryota.
DR HOGENOM; CLU_034328_1_1_1; -.
DR InParanoid; O22775; -.
DR OMA; NRRVEPH; -.
DR OrthoDB; 1223199at2759; -.
DR PhylomeDB; O22775; -.
DR BioCyc; ARA:AT4G02500-MON; -.
DR BioCyc; MetaCyc:AT4G02500-MON; -.
DR BRENDA; 2.4.2.39; 399.
DR PRO; PR:O22775; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22775; baseline and differential.
DR Genevisible; O22775; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0033843; F:xyloglucan 6-xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:TAIR.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0010411; P:xyloglucan metabolic process; IDA:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31311; PTHR31311; 1.
DR Pfam; PF05637; Glyco_transf_34; 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..461
FT /note="Xyloglucan 6-xylosyltransferase 2"
FT /id="PRO_0000215170"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..461
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 461 AA; 53095 MW; A5B98B5BCF110F98 CRC64;
MIERCLGAYR CRRIQRALRQ LKVTILCLLL TVVVLRSTIG AGKFGTPEQD LDEIRQHFHA
RKRGEPHRVL EEIQTGGDSS SGDGGGNSGG SNNYETFDIN KIFVDEGEEE KPDPNKPYTL
GPKISDWDEQ RSDWLAKNPS FPNFIGPNKP RVLLVTGSAP KPCENPVGDH YLLKSIKNKI
DYCRLHGIEI FYNMALLDAE MAGFWAKLPL IRKLLLSHPE IEFLWWMDSD AMFTDMAFEL
PWERYKDYNL VMHGWNEMVY DQKNWIGLNT GSFLLRNNQW ALDLLDTWAP MGPKGKIREE
AGKVLTRELK DRPVFEADDQ SAMVYLLATQ RDAWGNKVYL ESGYYLHGYW GILVDRYEEM
IENYHPGLGD HRWPLVTHFV GCKPCGKFGD YPVERCLKQM DRAFNFGDNQ ILQIYGFTHK
SLASRKVKRV RNETSNPLEM KDELGLLHPA FKAVKVQTNQ V
