GXM3_ARATH
ID GXM3_ARATH Reviewed; 297 AA.
AC Q9LQ32;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glucuronoxylan 4-O-methyltransferase 3;
DE EC=2.1.1.112;
GN Name=GXM3; OrderedLocusNames=At1g33800; ORFNames=F14M2.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 hypocotyls, roots, rosette leaves,
CC stems and siliques. {ECO:0000269|PubMed:21288268,
CC 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 GXM2. Reduced levels of methylated glucuronic acids. Gxm2 and
CC gxm3 double mutants show reduced stem mechanical strength.
CC {ECO:0000269|PubMed:21251108, ECO:0000269|PubMed:23045523}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; JX914596; AFU91594.1; -; mRNA.
DR EMBL; AC010164; AAF97282.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31626.1; -; Genomic_DNA.
DR EMBL; AY070772; AAL50109.1; -; mRNA.
DR EMBL; AY097395; AAM19911.1; -; mRNA.
DR EMBL; AY084664; AAM61226.1; -; mRNA.
DR PIR; E86461; E86461.
DR RefSeq; NP_564428.1; NM_103099.2.
DR AlphaFoldDB; Q9LQ32; -.
DR BioGRID; 25504; 4.
DR IntAct; Q9LQ32; 5.
DR STRING; 3702.AT1G33800.1; -.
DR PaxDb; Q9LQ32; -.
DR PRIDE; Q9LQ32; -.
DR ProteomicsDB; 247278; -.
DR EnsemblPlants; AT1G33800.1; AT1G33800.1; AT1G33800.
DR GeneID; 840272; -.
DR Gramene; AT1G33800.1; AT1G33800.1; AT1G33800.
DR KEGG; ath:AT1G33800; -.
DR Araport; AT1G33800; -.
DR TAIR; locus:2012728; AT1G33800.
DR eggNOG; ENOG502QST5; Eukaryota.
DR HOGENOM; CLU_053427_0_0_1; -.
DR InParanoid; Q9LQ32; -.
DR OMA; WIAIVTK; -.
DR OrthoDB; 1130631at2759; -.
DR PhylomeDB; Q9LQ32; -.
DR PRO; PR:Q9LQ32; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ32; baseline and differential.
DR Genevisible; Q9LQ32; 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:0009808; P:lignin metabolic process; IMP: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:0005976; P:polysaccharide metabolic process; IDA:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IBA:GO_Central.
DR GO; GO:0045491; P:xylan metabolic process; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR006514; IRX15/IRX15L/IGXM.
DR InterPro; IPR021148; Polysacc_synth_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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..297
FT /note="Glucuronoxylan 4-O-methyltransferase 3"
FT /id="PRO_0000420835"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 35..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 33670 MW; 826749A8E9FE638C CRC64;
MRTKSPSSLN LKVIFIGSSI LILIIIYLAR SNISSSSSKP ISKTNLSQEE EETQHKQEGC
PTTQQCTKMP LSLSDALVHY VTSNVTPQQT FDEVSVSKRV LDKKSPCNFL VFGLGHDSLM
WASLNHGGRT LFIEEDQAWI AIVTKKFPNL ESYHVVYDTK VKDSDKLMEL GRSEECRSVS
DPRNSKCDLA LKDFPADFYE TKWDLIMVDA PTGYHEEAPG RMSAIYTAGL LARNREDGET
DVFVHDVNRP VEDEFSATFL CKGYMREQNG RLRHFTIPSH RARAGRPFCP VEVDRRR
