TBL27_ARATH
ID TBL27_ARATH Reviewed; 416 AA.
AC O04523;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Xyloglucan O-acetyltransferase 1 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
DE AltName: Full=Protein ALTERED XYLOGLUCAN 4 {ECO:0000303|PubMed:22086088};
DE AltName: Full=Protein TRICHOME BIREFRINGENCE-LIKE 27 {ECO:0000303|PubMed:22086088};
GN Name=AXY4 {ECO:0000303|PubMed:22086088};
GN Synonyms=TBL27 {ECO:0000303|PubMed:22086088},
GN XGOAT1 {ECO:0000303|PubMed:30083810};
GN OrderedLocusNames=At1g70230 {ECO:0000312|Araport:AT1G70230};
GN ORFNames=F20P5.5 {ECO:0000312|EMBL:AAB61094.1};
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;
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].
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 GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL Plant J. 49:786-799(2007).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20388664; DOI=10.1104/pp.110.153320;
RA Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA Persson S., Delmer D., Scheible W.R.;
RT "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL Plant Physiol. 153:590-602(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-126, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia, and cv. Ty-0;
RX PubMed=22086088; DOI=10.1105/tpc.111.091728;
RA Gille S., de Souza A., Xiong G., Benz M., Cheng K., Schultink A.,
RA Reca I.B., Pauly M.;
RT "O-acetylation of Arabidopsis hemicellulose xyloglucan requires AXY4 or
RT AXY4L, proteins with a TBL and DUF231 domain.";
RL Plant Cell 23:4041-4053(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PRO-126; GLY-152; ASP-153; SER-154; ASP-367; GLY-368;
RP ASP-390 AND HIS-393.
RX PubMed=30083810; DOI=10.1007/s00425-018-2972-0;
RA Zhong R., Cui D., Ye Z.H.;
RT "Xyloglucan O-acetyltransferases from Arabidopsis thaliana and Populus
RT trichocarpa catalyze acetylation of fucosylated galactose residues on
RT xyloglucan side chains.";
RL Planta 248:1159-1171(2018).
RN [8]
RP 3D-STRUCTURE MODELING.
RX PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA Bischoff V., Selbig J., Scheible W.R.;
RT "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL Plant Signal. Behav. 5:1057-1059(2010).
CC -!- FUNCTION: Xyloglucan acetyltransferase that catalyzes the acetylation
CC of fucosylated Gal residues on xyloglucan side chains
CC (PubMed:30083810). Predominantly catalyze 6-O-monoacetylation of Gal
CC residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan
CC oligomers (PubMed:30083810). Involved in xyloglucan specific O-
CC acetylation in roots and rosette leaves (PubMed:22086088).
CC {ECO:0000269|PubMed:22086088, ECO:0000269|PubMed:30083810}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.63 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=65.4 pmol/min/mg enzyme with xyloglucan oligomer as substrate
CC {ECO:0000269|PubMed:30083810};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Loss of O-acetylated
CC xyloglucan oligosaccharides in roots and rosette leaves, but no effect
CC on xyloglucan O-acetylation in seeds. {ECO:0000269|PubMed:22086088}.
CC -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC it is unlikely that this protein belongs to the catalytically active
CC pectin esterases. {ECO:0000305|PubMed:20657172}.
CC -!- MISCELLANEOUS: A naturally occurring ecotype (cv. Ty-0) lacks AXY4-
CC mediated xyloglucan O-acetylation due to 2 amino acid changes,
CC Asp367Glu and Gly368Lys (PubMed:22086088).
CC {ECO:0000305|PubMed:22086088}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {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; AC002062; AAB61094.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35036.1; -; Genomic_DNA.
DR EMBL; AY080707; AAL85025.1; -; mRNA.
DR EMBL; AY117213; AAM51288.1; -; mRNA.
DR PIR; C96725; C96725.
DR RefSeq; NP_177180.1; NM_105691.5.
DR AlphaFoldDB; O04523; -.
DR SMR; O04523; -.
DR STRING; 3702.AT1G70230.1; -.
DR PaxDb; O04523; -.
DR PRIDE; O04523; -.
DR ProteomicsDB; 234187; -.
DR EnsemblPlants; AT1G70230.1; AT1G70230.1; AT1G70230.
DR GeneID; 843359; -.
DR Gramene; AT1G70230.1; AT1G70230.1; AT1G70230.
DR KEGG; ath:AT1G70230; -.
DR Araport; AT1G70230; -.
DR TAIR; locus:2020628; AT1G70230.
DR eggNOG; ENOG502QQXW; Eukaryota.
DR HOGENOM; CLU_020953_6_0_1; -.
DR InParanoid; O04523; -.
DR OMA; WMDAEMR; -.
DR OrthoDB; 805110at2759; -.
DR PhylomeDB; O04523; -.
DR PRO; PR:O04523; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04523; baseline and differential.
DR Genevisible; O04523; 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:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0010411; P:xyloglucan metabolic process; IMP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR InterPro; IPR029963; XGOAT1.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF302; PTHR32285:SF302; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..416
FT /note="Xyloglucan O-acetyltransferase 1"
FT /id="PRO_0000425392"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..416
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 152..154
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 390..393
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 390
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 79..129
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 100..165
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 109..395
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 318..391
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT MUTAGEN 126
FT /note="P->S: In axy4-1; reduced xyloglucan O-acetylation.
FT Almost abolishes xyloglucan acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22086088,
FT ECO:0000269|PubMed:30083810"
FT MUTAGEN 152
FT /note="G->A: Almost abolishes xyloglucan acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 153
FT /note="D->A: Almost abolishes xyloglucan acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 154
FT /note="S->A: Abolishes xyloglucan acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 367
FT /note="D->E: Abolishes xyloglucan acetyltransferase
FT activity; when associated with K-368."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 368
FT /note="G->K: Abolishes xyloglucan acetyltransferase
FT activity; when associated with E-367."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 390
FT /note="D->A: Abolishes xyloglucan acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30083810"
FT MUTAGEN 393
FT /note="H->A: Abolishes xyloglucan acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30083810"
SQ SEQUENCE 416 AA; 47474 MW; 1998AC0B4E36AC71 CRC64;
MGLNEQQNVP SQRKIIVFIV LAFIPIALFR LCFNNPFSSI KDTSLQDSAA NVVITSFSSS
SQEEESQESF DHIQDEPLCD YTQGNWVRDE IGPLYNGSTC GTIKDGQNCF RHGRPDSGYL
YWKWKPNECD IPRFDSNRFL DLMRDKHLAF IGDSMARNQL ESLLCLLSTV SSPDLVYRNG
EDNKFRRWRF ESHNVTVSVY WSPFLVAGLE KSGNLDHNVL HIDRVDERWG NDLERFDTVV
VSVGHWFLHP AVYYESGSVL GCHSCETSNC TEVGFYDVFR KAIRTTLRAV AGSGREVILT
TFSPSHFEGR PWDSLGACNM TKPYEGKVLE GLDLDMRKIE IEEYTAAAAE VRLEVLDVTA
MSVLRPDGHP GPYMYADPFK NGVPERIPND CLHWCLPGPV DTWNEIMIEM LRRWKV
