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RWA4_ARATH
ID   RWA4_ARATH              Reviewed;         540 AA.
AC   Q9FXG3; F4I360; F4I361;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein REDUCED WALL ACETYLATION 4 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
DE            EC=2.3.1.- {ECO:0000305};
GN   Name=RWA4 {ECO:0000303|PubMed:21212300, ECO:0000303|PubMed:21673009};
GN   OrderedLocusNames=At1g29890 {ECO:0000312|EMBL:AEE31147.1};
GN   ORFNames=F1N18.7 {ECO:0000312|EMBL:AAG10607.1};
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|Proteomes:UP000006548};
RN   [1]
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   [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 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9FXG3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FXG3-2; Sequence=VSP_057929;
CC       Name=3;
CC         IsoId=Q9FXG3-3; Sequence=VSP_057930, VSP_057931;
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       double mutant rwa2 rwa4 and triple mutants rwa2 rwa3 rwa4, rwa1 rwa3
CC       rwa4 and rwa1 rwa2 rwa4 are also dwarfs with abnormal morphology.
CC       Altered O-acetylated xyloglucans (XyG) oligosaccharides (XyGOs)
CC       composition (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG10607.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC008030; AAG10607.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31146.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31147.1; -; Genomic_DNA.
DR   EMBL; BX814013; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; E86422; E86422.
DR   RefSeq; NP_001031111.1; NM_001036034.2. [Q9FXG3-3]
DR   RefSeq; NP_174282.2; NM_102729.3. [Q9FXG3-2]
DR   AlphaFoldDB; Q9FXG3; -.
DR   STRING; 3702.AT1G29890.2; -.
DR   iPTMnet; Q9FXG3; -.
DR   PRIDE; Q9FXG3; -.
DR   ProteomicsDB; 232863; -. [Q9FXG3-1]
DR   EnsemblPlants; AT1G29890.1; AT1G29890.1; AT1G29890. [Q9FXG3-2]
DR   EnsemblPlants; AT1G29890.2; AT1G29890.2; AT1G29890. [Q9FXG3-3]
DR   EnsemblPlants; AT1G29890.3; AT1G29890.3; AT1G29890.
DR   GeneID; 839867; -.
DR   Gramene; AT1G29890.1; AT1G29890.1; AT1G29890. [Q9FXG3-2]
DR   Gramene; AT1G29890.2; AT1G29890.2; AT1G29890. [Q9FXG3-3]
DR   Gramene; AT1G29890.3; AT1G29890.3; AT1G29890.
DR   KEGG; ath:AT1G29890; -.
DR   Araport; AT1G29890; -.
DR   TAIR; locus:2019307; AT1G29890.
DR   eggNOG; KOG1699; Eukaryota.
DR   OMA; IQMMWRL; -.
DR   OrthoDB; 120492at2759; -.
DR   PRO; PR:Q9FXG3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FXG3; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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   Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW   Oxidoreductase; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..540
FT                   /note="Protein REDUCED WALL ACETYLATION 4"
FT                   /id="PRO_0000434398"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
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        256..276
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        407..426
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   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         1..87
FT                   /note="MVVSQPITPGQVSFLLGVIPLMIAWLYSEFLEYRRSSFHAKVHSDKNLVELE
FT                   MVTNKEDEGTVLMEGGLPRSASSKFYSSPIKTNLI -> MFSSHNIFLTIGIVFIR
FT                   (in isoform 2)"
FT                   /id="VSP_057929"
FT   VAR_SEQ         1
FT                   /note="M -> MDPVDM (in isoform 3)"
FT                   /id="VSP_057930"
FT   VAR_SEQ         233
FT                   /note="T -> TQVRSTIFDHHSLFSLPCDVLLESTMSFKAQDFYESFYLI (in
FT                   isoform 3)"
FT                   /id="VSP_057931"
SQ   SEQUENCE   540 AA;  63313 MW;  FEBC6D46D6A0BEEF CRC64;
     MVVSQPITPG QVSFLLGVIP LMIAWLYSEF LEYRRSSFHA KVHSDKNLVE LEMVTNKEDE
     GTVLMEGGLP RSASSKFYSS PIKTNLIRFL TLEDSFLLEN RATLRAMAEF GAILLYFYIC
     DRTSLIGQSQ KNYSRDLFLF LFCLLIIVSA MTSLKKHTDK SPITGKSILY LNRHQTEEWK
     GWMQVLFLMY HYFAAVEFYN AIRVFIAGYV WMTGFGNFSY YYIRKDFSLA RFTQMMWRLN
     FFVAFCCIIL NNDYMLYYIC PMHTLFTLMV YGALGIYSQY NEIASVMALK IASCFLVVIL
     MWEIPGVFEI FWSPLAFLLG YTDPAKPDLP RLHEWHFRSG LDRYIWIIGM IYAYFHPTVE
     RWMEKLEECD AKRRMSIKTS IIGISSFAGY LWYEYIYKLD KVTYNKYHPY TSWIPITVYI
     CLRNCTQQLR RFSLTLFAWL GKITLETYIS QFHIWLRSSV PNGQPKLLLS IIPEYPMLNF
     MLTTAIYVLV SVRLFELTNT LKSVFIPTKD DKRLLHNVIA MAAISFCLYI IGLILLLIPH
 
 
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