TBL22_ARATH
ID TBL22_ARATH Reviewed; 414 AA.
AC Q9LRS2;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=xyloglucan O-acetyltransferase 2 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
DE AltName: Full=Protein ALTERED XYLOGLUCAN 4-like {ECO:0000303|PubMed:22086088};
DE AltName: Full=Protein trichome birefringence-like 22 {ECO:0000303|PubMed:22086088};
GN Name=AXY4L {ECO:0000303|PubMed:22086088};
GN Synonyms=TBL22 {ECO:0000303|PubMed:22086088},
GN XGOAT2 {ECO:0000303|PubMed:30083810};
GN OrderedLocusNames=At3g28150 {ECO:0000312|Araport:AT3G28150};
GN ORFNames=MMG15.18 {ECO:0000312|EMBL:BAB01135.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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, AND DISRUPTION PHENOTYPE.
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 seeds (PubMed:22086088). {ECO:0000269|PubMed:22086088,
CC ECO:0000269|PubMed:30083810}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=55.2 pmol/min/mg enzyme with xyloglucan oligomer as substrate
CC {ECO:0000269|PubMed:30083810};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Loss of O-acetylated
CC xyloglucan oligosaccharides in seeds, but no effect on xyloglucan O-
CC acetylation in roots and rosette leaves. {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 -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; AB028616; BAB01135.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77409.1; -; Genomic_DNA.
DR EMBL; AY070041; AAL49798.1; -; mRNA.
DR EMBL; AY117223; AAM51298.1; -; mRNA.
DR RefSeq; NP_189454.1; NM_113733.6.
DR AlphaFoldDB; Q9LRS2; -.
DR SMR; Q9LRS2; -.
DR STRING; 3702.AT3G28150.1; -.
DR PaxDb; Q9LRS2; -.
DR PRIDE; Q9LRS2; -.
DR ProteomicsDB; 234159; -.
DR EnsemblPlants; AT3G28150.1; AT3G28150.1; AT3G28150.
DR GeneID; 822439; -.
DR Gramene; AT3G28150.1; AT3G28150.1; AT3G28150.
DR KEGG; ath:AT3G28150; -.
DR Araport; AT3G28150; -.
DR TAIR; locus:2091388; AT3G28150.
DR eggNOG; ENOG502QPJ5; Eukaryota.
DR HOGENOM; CLU_020953_6_1_1; -.
DR InParanoid; Q9LRS2; -.
DR OMA; GCAMEKF; -.
DR OrthoDB; 976948at2759; -.
DR PhylomeDB; Q9LRS2; -.
DR PRO; PR:Q9LRS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRS2; baseline and differential.
DR Genevisible; Q9LRS2; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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; IPR029975; XGOAT2.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF262; PTHR32285:SF262; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..414
FT /note="xyloglucan O-acetyltransferase 2"
FT /id="PRO_0000425387"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..414
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 143..145
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 389..392
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 70..120
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 91..156
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 100..394
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 317..390
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 414 AA; 47973 MW; E0BB59B5E9622D53 CRC64;
MKSSSSIFRE TSEKKSERWM MMNIGRFSPF FLSSFCITLF FTGFFVYQNP FKSIADQNVL
SFQPQIDPEC DLFKGHWVPD KRGSLYTNSS CATIPDSKNC IKQGRPDKDF LFWRWKPDGC
DLPRFNPKAF LSMVRGKKMN FIGDSVARNH MESLLCLLSM EETPKDIYKD GEDRNRIWYF
PKHDFTLSTS WTKFLVEERE RRDSNNTGTG LFDLDIGKID EGWFNGLPNT DIAIVSAAHW
FFRPIFIHRG DETLGCIYCN LPNMTQISPE EGFKLVYSAV LRQINECEMC KKDLVTVLRT
ISPAHFENGT WDTGGTCSRT SPFGENKIDL QSNEMKIRKS QIEQLEGITK RGNKAKKFAV
LDVTRVMQMR PDGHPNGYWG NKWMKGYNDC VHWCLPGPID AWNDFLMAII RQLR
