RWA2_ARATH
ID RWA2_ARATH Reviewed; 545 AA.
AC Q0WW17; B3H643; Q67YS5; Q9C8Z6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein REDUCED WALL ACETYLATION 2 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
DE EC=2.3.1.- {ECO:0000305};
GN Name=RWA2 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
GN OrderedLocusNames=At3g06550 {ECO:0000312|EMBL:AEE74412.1};
GN ORFNames=F5E6.12 {ECO:0000312|EMBL:AAG51327.1};
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:BAE98681.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 3).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY 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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP 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 [8]
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 cell wall polymers (both pectic and nonpectic polysaccharides) and of
CC xylan during secondary wall biosynthesis. Catalyzes the O-acetylation
CC of xyloglucan. {ECO:0000269|PubMed:21212300,
CC ECO:0000269|PubMed:21673009, ECO:0000269|PubMed:24019426}.
CC -!- FUNCTION: Seems required for infection by the necrotrophic fungal
CC pathogen Botrytis cinerea. {ECO:0000269|PubMed:21212300}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21673009}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21212300}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q0WW17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WW17-2; Sequence=VSP_057925;
CC Name=3;
CC IsoId=Q0WW17-3; Sequence=VSP_057925, VSP_057926;
CC Name=4;
CC IsoId=Q0WW17-4; Sequence=VSP_057927;
CC -!- TISSUE SPECIFICITY: Expressed in cells undergoing secondary wall
CC thickeningin a SND1-dependent manner, such as xylem cells. Slightly
CC elevated in the inflorescence stems (PubMed:21673009). Mainly observed
CC in leaves and inflorescence stem tops, but present ubiquitously
CC (PubMed:21212300). {ECO:0000269|PubMed:21212300,
CC ECO:0000269|PubMed:21673009}.
CC -!- DISRUPTION PHENOTYPE: Decreased levels of acetylated cell wall polymers
CC and lower amounts of acetic acid in single mutant. Increased tolerance
CC toward the necrotrophic fungal pathogen Botrytis cinerea
CC (PubMed:21212300). Severe growth phenotypes (e.g. dwarf and abnormal
CC flower organs) associated with reduction in the secondary wall
CC thickening and the stem mechanical strength in the quadruple mutant
CC rwa1 rwa2 rwa3 rwa4 and characterized by reduced xylan acetylation and
CC altered ratio of non-methylated to methylated glucuronic acid side
CC chains. Absence of interfascicular fibers and xylem cells
CC differentiation (PubMed:21673009, PubMed:24019426). The double mutant
CC rwa2 rwa4 and triple mutants rwa2 rwa3 rwa4, rwa1 rwa2 rwa3 and rwa1
CC rwa2 rwa4 are also dwarfs with abnormal morphology. Altered O-
CC acetylated xyloglucans (XyG) oligosaccharides (XyGOs) composition
CC (PubMed:24019426). {ECO:0000269|PubMed:21212300,
CC ECO:0000269|PubMed:21673009, ECO:0000269|PubMed:24019426}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC020580; AAG51327.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74412.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74413.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74414.1; -; Genomic_DNA.
DR EMBL; AK176393; BAD44156.1; -; mRNA.
DR EMBL; BT012556; AAS99700.1; -; mRNA.
DR EMBL; AK226542; BAE98681.1; -; mRNA.
DR RefSeq; NP_001078116.1; NM_001084647.5. [Q0WW17-4]
DR RefSeq; NP_001118592.1; NM_001125120.1. [Q0WW17-2]
DR RefSeq; NP_187307.3; NM_111531.5. [Q0WW17-1]
DR AlphaFoldDB; Q0WW17; -.
DR STRING; 3702.AT3G06550.2; -.
DR iPTMnet; Q0WW17; -.
DR PaxDb; Q0WW17; -.
DR PRIDE; Q0WW17; -.
DR ProMEX; Q0WW17; -.
DR ProteomicsDB; 228032; -. [Q0WW17-1]
DR EnsemblPlants; AT3G06550.1; AT3G06550.1; AT3G06550. [Q0WW17-1]
DR EnsemblPlants; AT3G06550.2; AT3G06550.2; AT3G06550. [Q0WW17-4]
DR EnsemblPlants; AT3G06550.3; AT3G06550.3; AT3G06550. [Q0WW17-2]
DR GeneID; 819834; -.
DR Gramene; AT3G06550.1; AT3G06550.1; AT3G06550. [Q0WW17-1]
DR Gramene; AT3G06550.2; AT3G06550.2; AT3G06550. [Q0WW17-4]
DR Gramene; AT3G06550.3; AT3G06550.3; AT3G06550. [Q0WW17-2]
DR KEGG; ath:AT3G06550; -.
DR Araport; AT3G06550; -.
DR TAIR; locus:2084279; AT3G06550.
DR eggNOG; KOG1699; Eukaryota.
DR HOGENOM; CLU_020608_0_0_1; -.
DR OMA; QSLLHEW; -.
DR OrthoDB; 120492at2759; -.
DR PhylomeDB; Q0WW17; -.
DR PRO; PR:Q0WW17; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WW17; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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: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:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0005976; P:polysaccharide metabolic process; 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; IMP:UniProtKB.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR Pfam; PF07779; Cas1_AcylT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Oxidoreductase; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..545
FT /note="Protein REDUCED WALL ACETYLATION 2"
FT /id="PRO_0000434396"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66GQ5"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 43
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_057925"
FT VAR_SEQ 420..545
FT /note="Missing (in isoform 3)"
FT /id="VSP_057926"
FT VAR_SEQ 545
FT /note="V -> VSQNFIFLCGRKLFFPWYLSSLIC (in isoform 4)"
FT /id="VSP_057927"
SQ SEQUENCE 545 AA; 63612 MW; AA16CA7F04AA670D CRC64;
MASSSPVTPG LMSVVFGIVP VIVAWLYSEY LHYAKYSVSA KTRHSDVNLV EIAKDFVKED
DKALLIEDGG GLQSASPRAK GPTTHSPLIR FVLLDESFLV ENRLTLRAII EFAVLMVYFY
ICDRTDVFNS SKKSYNRDLF LFLYFLLIIV SAITSFTIHT DKSPFSGKAI MYLNRHQTEE
WKGWMQVLFL MYHYFAAAEY YNAIRVFIAC YVWMTGFGNF SYYYIRKDFS LARFAQMMWR
LNFLVIFSCI VLNNSYMLYY ICPMHTLFTL MVYGALGIMS KYNEMGSVIA AKFFACFVVV
IIVWEIPGVF EWIWSPFTLL MGYNDPAKPQ LPLLHEWHFR SGLDRYIWII GMLYAYYHPT
VESWMDKLEE AEMKFRVAIK TSVALIALTV GYFWYEYIYK MDKLTYNKYH PYTSWIPITV
YICLRNITQS FRGYSLTLLA WLGKITLETY ISQFHIWLRS GVPDGQPKLL LSLVPDYPLL
NFMLTTSIYV AISYRLFELT NTLKTAFIPT KDDKRLVYNT ISALIICTCL YFFSFILITI
PQKLV
