ID   GXM2_ARATH              Reviewed;         290 AA.
AC   Q9T0F7;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Glucuronoxylan 4-O-methyltransferase 2;
DE            EC=2.1.1.112;
GN   Name=GXM2; OrderedLocusNames=At4g09990; ORFNames=T5L19.120;
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, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23045523; DOI=10.1093/pcp/pcs138;
RA   Lee C., Teng Q., Zhong R., Yuan Y., Haghighat M., Ye Z.H.;
RT   "Three Arabidopsis DUF579 domain-containing GXM proteins are
RT   methyltransferases catalyzing 4-O-methylation of glucuronic acid on
RT   xylan.";
RL   Plant Cell Physiol. 53:1934-1949(2012).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=21288268; DOI=10.1111/j.1365-313x.2010.04475.x;
RA   Jensen J.K., Kim H., Cocuron J.C., Orler R., Ralph J., Wilkerson C.G.;
RT   "The DUF579 domain containing proteins IRX15 and IRX15-L affect xylan
RT   synthesis in Arabidopsis.";
RL   Plant J. 66:387-400(2011).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=21251108; DOI=10.1111/j.1365-313x.2011.04501.x;
RA   Brown D., Wightman R., Zhang Z., Gomez L.D., Atanassov I., Bukowski J.P.,
RA   Tryfona T., McQueen-Mason S.J., Dupree P., Turner S.;
RT   "Arabidopsis genes IRREGULAR XYLEM (IRX15) and IRX15L encode DUF579-
RT   containing proteins that are essential for normal xylan deposition in the
RT   secondary cell wall.";
RL   Plant J. 66:401-413(2011).
CC   -!- FUNCTION: Methyltransferase catalyzing 4-O-methylation of glucuronic
CC       acid side chains on xylan. {ECO:0000269|PubMed:23045523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronoxylan D-glucuronate + n S-adenosyl-L-methionine =
CC         glucuronoxylan 4-O-methyl-D-glucuronate + n H(+) + n S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:20413, Rhea:RHEA-COMP:14499, Rhea:RHEA-
CC         COMP:14500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:140335, ChEBI:CHEBI:140336; EC=2.1.1.112;
CC         Evidence={ECO:0000269|PubMed:23045523};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:23045523}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:23045523}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves and stems.
CC       {ECO:0000269|PubMed:21288268, ECO:0000269|PubMed:23045523}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during secondary cell wall
CC       deposition. {ECO:0000269|PubMed:21251108}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC       GXM1 and GXM3. Gxm2 and gxm3 double mutants show reduced stem
CC       mechanical strength. {ECO:0000269|PubMed:21251108,
CC       ECO:0000269|PubMed:23045523}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; JX914595; AFU91593.1; -; mRNA.
DR   EMBL; AL049481; CAB39623.1; -; Genomic_DNA.
DR   EMBL; AL161516; CAB78122.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82826.1; -; Genomic_DNA.
DR   EMBL; BT030090; ABN04828.1; -; mRNA.
DR   PIR; T04003; T04003.
DR   RefSeq; NP_192737.1; NM_117067.4.
DR   AlphaFoldDB; Q9T0F7; -.
DR   STRING; 3702.AT4G09990.1; -.
DR   PaxDb; Q9T0F7; -.
DR   PRIDE; Q9T0F7; -.
DR   ProteomicsDB; 247156; -.
DR   EnsemblPlants; AT4G09990.1; AT4G09990.1; AT4G09990.
DR   GeneID; 826590; -.
DR   Gramene; AT4G09990.1; AT4G09990.1; AT4G09990.
DR   KEGG; ath:AT4G09990; -.
DR   Araport; AT4G09990; -.
DR   TAIR; locus:2140518; AT4G09990.
DR   eggNOG; ENOG502QST5; Eukaryota.
DR   HOGENOM; CLU_053427_0_0_1; -.
DR   InParanoid; Q9T0F7; -.
DR   OMA; FFITNTE; -.
DR   OrthoDB; 1130631at2759; -.
DR   PhylomeDB; Q9T0F7; -.
DR   PRO; PR:Q9T0F7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T0F7; baseline and differential.
DR   Genevisible; Q9T0F7; AT.
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:0030775; F:glucuronoxylan 4-O-methyltransferase activity; IDA:TAIR.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IBA:GO_Central.
DR   GO; GO:0045492; P:xylan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045491; P:xylan metabolic process; IMP:TAIR.
DR   InterPro; IPR006514; IRX15/IRX15L/IGXM.
DR   InterPro; IPR021148; Polysacc_synth_dom.
DR   PANTHER; PTHR31444; PTHR31444; 1.
DR   Pfam; PF04669; Polysacc_synt_4; 1.
DR   TIGRFAMs; TIGR01627; A_thal_3515; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Membrane; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..290
FT                   /note="Glucuronoxylan 4-O-methyltransferase 2"
FT                   /id="PRO_0000420838"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   290 AA;  32837 MW;  2F64327D2E6BFEAF CRC64;
     MRNKSQSFIS SKLIFICCSI LVLFILFLKR ASFSSNSTAT IRDEYHQKSK CPSTPQQCTK
     LPTSLSDALV HYVTSEITPQ QTFDEVSVSK RVLDKKSPCN FLVFGLGHDS LMWASLNHGG
     RTLFLEEDEA WIETVTKKFP NLESYHVVYD TKVKDSNKLM ELKRTEDCKA VSDPRDSKCA
     LSLKGFPADV YETQWDVIMV DAPTGYHDEA PGRMSAIYTA GLLARNRYDG GETDVFVHDI
     NRPVEDEFSV AFLCGGYMKE QQGRLRHFNI PSHRASFGTP FCPADISRRF