RWA1_ARATH
ID RWA1_ARATH Reviewed; 540 AA.
AC Q8L7C8; Q944Q8; Q9FL27;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein REDUCED WALL ACETYLATION 1 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
DE EC=2.3.1.- {ECO:0000305};
GN Name=RWA1 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
GN OrderedLocusNames=At5g46340 {ECO:0000312|EMBL:AED95371.1};
GN ORFNames=MPL12.14 {ECO:0000312|EMBL:BAB11089.1};
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:AAM97005.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
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 [4]
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 [5]
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 [6]
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 -!- 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 rwa1 rwa2 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=BAB11089.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010698; BAB11089.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95371.1; -; Genomic_DNA.
DR EMBL; AY136339; AAM97005.1; -; mRNA.
DR EMBL; AF424606; AAL11600.1; -; mRNA.
DR RefSeq; NP_568662.1; NM_124004.3.
DR AlphaFoldDB; Q8L7C8; -.
DR STRING; 3702.AT5G46340.1; -.
DR iPTMnet; Q8L7C8; -.
DR PaxDb; Q8L7C8; -.
DR PRIDE; Q8L7C8; -.
DR ProteomicsDB; 232722; -.
DR EnsemblPlants; AT5G46340.1; AT5G46340.1; AT5G46340.
DR GeneID; 834677; -.
DR Gramene; AT5G46340.1; AT5G46340.1; AT5G46340.
DR KEGG; ath:AT5G46340; -.
DR Araport; AT5G46340; -.
DR TAIR; locus:2170493; AT5G46340.
DR eggNOG; KOG1699; Eukaryota.
DR HOGENOM; CLU_020608_0_0_1; -.
DR InParanoid; Q8L7C8; -.
DR OMA; MEDIKAC; -.
DR OrthoDB; 120492at2759; -.
DR PhylomeDB; Q8L7C8; -.
DR PRO; PR:Q8L7C8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7C8; baseline and differential.
DR Genevisible; Q8L7C8; 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 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="Protein REDUCED WALL ACETYLATION 1"
FT /id="PRO_0000434395"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
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 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:0000250|UniProtKB:Q66GQ5"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 476
FT /note="P -> R (in Ref. 3; AAL11600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 63336 MW; B2BC61E6D2321CAB CRC64;
MVDPGPITPG QVSFLLGVIP IFVGWIYSEL LEYRKSWVPL KPHSDNNLVE LGDVAEKDDD
KADLLEGGLA RSPSVKFHNS SIRTNIIRFL SMEDSFLLEH RATLRAMSEF GAILIYFYIC
DRTELLGDST KNYNRDLFLF LYVLLIIVSA MTSLRKHNDK SPISGKSILY LNRHQTEEWK
GWMQVLFLMY HYFAAAEIYN AIRIFIAAYV WMTGFGNFSY YYVRKDFSVA RFAQMMWRLN
FFVAFCCIVL NNDYMLYYIC PMHTLFTLMV YGALGIFSKY NEIGSVMALK IFSCFLVVFL
LWEIPGAFEI FWGPLTFLLG YNDPAKPDLH RLHEWHFRSG LDRYIWIIGM IYAYYHPTVE
RWMEKLEDCE TKKRLSIKAA IVTITVLVGY VWYECIYKLD RTSYNMYHPY TSWIPITVYI
CLRNFTHQLR SVSLTLFAWL GKITLETYIS QFHIWLRSNM PDGQPKWLLS IIPGYPMLNF
MLTTAIYVLV SHRLFELTNT LKTVFVPTKD NKRLFSNFIA GIAIALPLYC FSFVLLQIHR
