RWA3_ARATH
ID RWA3_ARATH Reviewed; 540 AA.
AC Q66GQ5; F4IHV6; O64704;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein REDUCED WALL ACETYLATION 3 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
DE EC=2.3.1.- {ECO:0000305};
GN Name=RWA3 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
GN OrderedLocusNames=At2g34410 {ECO:0000312|EMBL:AEC08969.1};
GN ORFNames=F13P17.23 {ECO:0000312|EMBL:AAM14946.1};
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 {ECO:0000312|EMBL:AAU05470.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21673009; DOI=10.1093/pcp/pcr075;
RA Lee C., Teng Q., Zhong R., Ye Z.H.;
RT "The four Arabidopsis reduced wall acetylation genes are expressed in
RT secondary wall-containing cells and required for the acetylation of
RT xylan.";
RL Plant Cell Physiol. 52:1289-1301(2011).
RN [9]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21212300; DOI=10.1104/pp.110.168989;
RA Manabe Y., Nafisi M., Verhertbruggen Y., Orfila C., Gille S.,
RA Rautengarten C., Cherk C., Marcus S.E., Somerville S., Pauly M., Knox J.P.,
RA Sakuragi Y., Scheller H.V.;
RT "Loss-of-function mutation of REDUCED WALL ACETYLATION2 in Arabidopsis
RT leads to reduced cell wall acetylation and increased resistance to Botrytis
RT cinerea.";
RL Plant Physiol. 155:1068-1078(2011).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE FAMILY.
RX PubMed=24019426; DOI=10.1104/pp.113.225193;
RA Manabe Y., Verhertbruggen Y., Gille S., Harholt J., Chong S.-L.,
RA Pawar P.M.-A., Mellerowicz E.J., Tenkanen M., Cheng K., Pauly M.,
RA Scheller H.V.;
RT "Reduced wall acetylation proteins play vital and distinct roles in cell
RT wall O-acetylation in Arabidopsis.";
RL Plant Physiol. 163:1107-1117(2013).
CC -!- FUNCTION: Probable O-acetyltransferase involved in the acetylation of
CC xylan during secondary wall biosynthesis. {ECO:0000269|PubMed:21673009,
CC ECO:0000269|PubMed:24019426}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21673009}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66GQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66GQ5-2; Sequence=VSP_057928;
CC -!- TISSUE SPECIFICITY: Expressed in cells undergoing secondary wall
CC thickeningin a SND1-dependent manner, such as xylem cells and
CC interfascicular fibers. Mostly expressed in the middle and bottom parts
CC of the inflorescence stems (PubMed:21673009). Mainly observed in the
CC more mature parts of inflorescence stems, but present ubiquitously
CC (PubMed:21212300). {ECO:0000269|PubMed:21212300,
CC ECO:0000269|PubMed:21673009}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype on cell wall acetylation in
CC single mutant (PubMed:21212300). Severe growth phenotypes (e.g. dwarf
CC and abnormal flower organs) associated with reduction in the secondary
CC wall thickening and the stem mechanical strength in the quadruple
CC mutant rwa1 rwa2 rwa3 rwa4 and characterized by reduced xylan
CC acetylation and altered ratio of non-methylated to methylated
CC glucuronic acid side chains. Absence of interfascicular fibers and
CC xylem cells differentiation (PubMed:21673009, PubMed:24019426). The
CC triple mutants rwa1 rwa2 rwa3, rwa1 rwa3 rwa4 and rwa2 rwa3 rwa4 are
CC also dwarfs with abnormal morphology. Altered O-acetylated xyloglucans
CC (XyG) oligosaccharides (XyGOs) composition (PubMed:24019426).
CC {ECO:0000269|PubMed:21212300, ECO:0000269|PubMed:21673009,
CC ECO:0000269|PubMed:24019426}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26714.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM14946.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004077; AAC26714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004481; AAM14946.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08969.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08970.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08971.1; -; Genomic_DNA.
DR EMBL; AK316994; BAH19689.1; -; mRNA.
DR EMBL; BT015347; AAU05470.1; -; mRNA.
DR EMBL; BT020218; AAV59284.1; -; mRNA.
DR EMBL; AK221547; BAD94920.1; -; mRNA.
DR EMBL; AK228823; BAF00719.1; -; mRNA.
DR PIR; C84756; C84756.
DR RefSeq; NP_001031478.1; NM_001036401.3. [Q66GQ5-1]
DR RefSeq; NP_001031479.2; NM_001036402.3. [Q66GQ5-2]
DR RefSeq; NP_180988.3; NM_128993.4. [Q66GQ5-1]
DR AlphaFoldDB; Q66GQ5; -.
DR STRING; 3702.AT2G34410.2; -.
DR iPTMnet; Q66GQ5; -.
DR PaxDb; Q66GQ5; -.
DR PRIDE; Q66GQ5; -.
DR ProteomicsDB; 226616; -. [Q66GQ5-1]
DR EnsemblPlants; AT2G34410.1; AT2G34410.1; AT2G34410. [Q66GQ5-1]
DR EnsemblPlants; AT2G34410.2; AT2G34410.2; AT2G34410. [Q66GQ5-1]
DR EnsemblPlants; AT2G34410.3; AT2G34410.3; AT2G34410. [Q66GQ5-2]
DR GeneID; 818004; -.
DR Gramene; AT2G34410.1; AT2G34410.1; AT2G34410. [Q66GQ5-1]
DR Gramene; AT2G34410.2; AT2G34410.2; AT2G34410. [Q66GQ5-1]
DR Gramene; AT2G34410.3; AT2G34410.3; AT2G34410. [Q66GQ5-2]
DR KEGG; ath:AT2G34410; -.
DR Araport; AT2G34410; -.
DR TAIR; locus:2062340; AT2G34410.
DR eggNOG; KOG1699; Eukaryota.
DR InParanoid; Q66GQ5; -.
DR OMA; WIKASIV; -.
DR PhylomeDB; Q66GQ5; -.
DR PRO; PR:Q66GQ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q66GQ5; baseline and differential.
DR Genevisible; Q66GQ5; 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:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:1990937; P:xylan acetylation; IGI:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IMP:UniProtKB.
DR GO; GO:0045491; P:xylan metabolic process; IMP:UniProtKB.
DR GO; GO:0010411; P:xyloglucan metabolic process; IBA:GO_Central.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR Pfam; PF07779; Cas1_AcylT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="Protein REDUCED WALL ACETYLATION 3"
FT /id="PRO_0000434397"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 107..120
FT /note="MAEFGAILFYFYIS -> I (in isoform 2)"
FT /id="VSP_057928"
SQ SEQUENCE 540 AA; 63331 MW; E9283833E8D93618 CRC64;
MADSQPITPG QVSFLLGVIP VFIAWIYSEF LEYKRSSLHS KVHSDNNLVE LGEVKNKEDE
GVVLLEGGLP RSVSTKFYNS PIKTNLIRFL TLEDSFLIEN RATLRAMAEF GAILFYFYIS
DRTSLLGESK KNYNRDLFLF LYCLLIIVSA MTSLKKHNDK SPITGKSILY LNRHQTEEWK
GWMQVLFLMY HYFAAAEIYN AIRVFIAAYV WMTGFGNFSY YYIRKDFSLA RFTQMMWRLN
LFVAFSCIIL NNDYMLYYIC PMHTLFTLMV YGALGIFSRY NEIPSVMALK IASCFLVVIV
MWEIPGVFEI FWSPLTFLLG YTDPAKPELP LLHEWHFRSG LDRYIWIIGM IYAYFHPTVE
RWMEKLEECD AKRKMSIKTS IIAISSFVGY LWYEYIYKLD KVTYNKYHPY TSWIPITVYI
CLRNSTQQLR NFSMTLFAWL GKITLETYIS QFHIWLRSNV PNGQPKWLLC IIPEYPMLNF
MLVTAIYVLV SHRLFELTNT LKSVFIPTKD DKRLLHNVLA GAAISFCLYL TSLILLQIPH
