XOATC_ORYSJ
ID XOATC_ORYSJ Reviewed; 503 AA.
AC Q2RBL8; B9G8Z5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Xylan O-acetyltransferase 12 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 2 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL2 {ECO:0000303|PubMed:27864442};
GN Name=XOAT12 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL2 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os11g0107000 {ECO:0000312|EMBL:BAT12325.1},
GN LOC_Os11g01570 {ECO:0000312|EMBL:ABA91093.1};
GN ORFNames=OsJ_32659 {ECO:0000312|EMBL:EEE51501.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29569182; DOI=10.1007/s00425-018-2882-1;
RA Zhong R., Cui D., Dasher R.L., Ye Z.H.;
RT "Biochemical characterization of rice xylan O-acetyltransferases.";
RL Planta 247:1489-1498(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=27864442; DOI=10.1104/pp.16.01618;
RA Gao Y., He C., Zhang D., Liu X., Xu Z., Tian Y., Liu X.H., Zang S.,
RA Pauly M., Zhou Y., Zhang B.;
RT "Two trichome birefringence-like proteins mediate xylan acetylation, which
RT is essential for leaf blight resistance in rice.";
RL Plant Physiol. 173:470-481(2017).
CC -!- FUNCTION: Xylan acetyltransferase required for 2-O- and 3-O-
CC monoacetylation of xylosyl residues in xylan (PubMed:29569182,
CC PubMed:27864442). Catalyzes the 2-O-acetylation of xylan, followed by
CC nonenzymatic acetyl migration to the O-3 position, resulting in
CC products that are monoacetylated at both O-2 and O-3 positions (By
CC similarity). {ECO:0000250|UniProtKB:Q9LY46,
CC ECO:0000269|PubMed:27864442, ECO:0000269|PubMed:29569182}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.18 mM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=51.6 pmol/min/mg enzyme with xylohexaose as substrate
CC {ECO:0000269|PubMed:29569182};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Stunted growth and reduced plant height
CC (PubMed:27864442). The double mutants tbl1 and tbl2 exhibit increased
CC susceptibility to the bacterial pathogen Xanthomonas oryzae pv oryzae
CC (Xoo) (PubMed:27864442). {ECO:0000269|PubMed:27864442}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH037026; AVR54516.1; -; mRNA.
DR EMBL; DP000010; ABA91093.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF27388.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT12325.1; -; Genomic_DNA.
DR EMBL; CM000148; EEE51501.1; -; Genomic_DNA.
DR EMBL; AK065582; BAG89570.1; -; mRNA.
DR RefSeq; XP_015615528.1; XM_015760042.1.
DR AlphaFoldDB; Q2RBL8; -.
DR SMR; Q2RBL8; -.
DR STRING; 4530.OS11T0107000-01; -.
DR PaxDb; Q2RBL8; -.
DR PRIDE; Q2RBL8; -.
DR EnsemblPlants; Os11t0107000-01; Os11t0107000-01; Os11g0107000.
DR GeneID; 4349561; -.
DR Gramene; Os11t0107000-01; Os11t0107000-01; Os11g0107000.
DR KEGG; osa:4349561; -.
DR eggNOG; ENOG502SHUB; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q2RBL8; -.
DR OMA; ACHFLSA; -.
DR OrthoDB; 886886at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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:1990538; F:xylan O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1990937; P:xylan acetylation; IDA:UniProtKB.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 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; Plant defense;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..503
FT /note="Xylan O-acetyltransferase 12"
FT /id="PRO_0000454035"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..77
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..503
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 227..229
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 479..482
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 479
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 153..204
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 175..240
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 184..484
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 400..480
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 503 AA; 57664 MW; B3D4F77AD853D1F6 CRC64;
MWSALFSHLR EVHKRSGVKE EKLIMKSPAA AGEAAGCHKP QATATNKMTV LQSPLGLRTI
LTSLVAFFIV VSSVSLLFDR SQDAQAQLAV AQHQHQEVQL KQKPASAAVG EQKSVFVDQS
SLRSQEAQVQ WTSELQDVAT DSGDGGVDGE EECNWSLGRW VYDNSSRPLY SGLKCSFIFD
EVACDKYGRN DTKYQHWRWQ PHGCNLPRFN ATKFLEKLRN KRLVFVGDSV NRNQWVSMVC
MVEHFIPDGR KMRVYNGSLI SFKAFEYNAT IDFYWSPLLL ESNSDNPIIH RVEYRIIRAD
RIEKHANVWK DADFIVFNSY LWWRKQRDGM TMKVMYGSFE DGDAKLDEVE MVDGYEIALK
KLTEYLGANI NKNKTRIFFA GSSPAHSWAS NWGGDDNNKC LNETEPIQIE DYRSATTDYG
MMDKAKEIFG TLEPKGIHVQ ILNITQLSEY RKDAHPTIFR RQYVPLTKEQ IANPSIYADC
THWCLPGVPD VWNEFLYAYL MHK
