XOAT3_ORYSJ
ID XOAT3_ORYSJ Reviewed; 455 AA.
AC Q2QYW3; B9GBE1; Q0IQR9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Xylan O-acetyltransferase 3 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 9 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL9 {ECO:0000303|PubMed:27864442};
GN Name=XOAT3 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL9 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os12g0104700 {ECO:0000312|EMBL:BAT15478.1},
GN LOC_Os12g01380 {ECO:0000312|EMBL:ABA95597.1};
GN ORFNames=OsJ_34909 {ECO:0000312|EMBL:EEE52598.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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 GENE FAMILY, AND NOMENCLATURE.
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 Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl
CC migration to the O-3 position, resulting in products that are
CC monoacetylated at both O-2 and O-3 positions (By similarity).
CC {ECO:0000250|UniProtKB:Q9LY46, ECO:0000269|PubMed:29569182}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.82 mM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=94 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 -!- TISSUE SPECIFICITY: Highly expressed in leaves. Expressed in roots,
CC stems and inflorescences. {ECO:0000269|PubMed:29569182}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH037017; AVR54507.1; -; mRNA.
DR EMBL; DP000011; ABA95597.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF28946.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15478.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE52598.1; -; Genomic_DNA.
DR EMBL; AK067342; BAG90376.1; -; mRNA.
DR RefSeq; XP_015620622.1; XM_015765136.1.
DR AlphaFoldDB; Q2QYW3; -.
DR SMR; Q2QYW3; -.
DR STRING; 4530.OS12T0104700-01; -.
DR PaxDb; Q2QYW3; -.
DR PRIDE; Q2QYW3; -.
DR EnsemblPlants; Os12t0104700-01; Os12t0104700-01; Os12g0104700.
DR GeneID; 4351254; -.
DR Gramene; Os12t0104700-01; Os12t0104700-01; Os12g0104700.
DR KEGG; osa:4351254; -.
DR eggNOG; ENOG502SJAQ; Eukaryota.
DR HOGENOM; CLU_020953_3_0_1; -.
DR InParanoid; Q2QYW3; -.
DR OMA; ADIKIRR; -.
DR OrthoDB; 834476at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
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: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;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..455
FT /note="Xylan O-acetyltransferase 3"
FT /id="PRO_0000454027"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..455
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 170..172
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 418..421
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT COMPBIAS 11..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 418
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 96..147
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 118..183
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 127..423
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 339..419
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CONFLICT 448..451
FT /note="THPS -> PHPP (in Ref. 6; EEE52598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 52585 MW; 148C4FB6D4BEF9BA CRC64;
MSKPQQQSPP STTTTSPPPP PPSTPPPASS SRSLLSALRR SPVTTLVAAF FLLALFMYGE
DVRTLAELSI DDYLYPDADF YNVSALPPLL LPPPTCDLSR GRWVFDNTSL PAYREKECTF
LTKQVSCLAN GRPDDLWQYW RWQPNNCSLP TFDARRFMEK MRGKRMMFVG DSLNRNQWES
LVCLVQPILS KGRKKIVKRG SFNIFYAKEY RATLEFYWAP FLVESNSDNP NFHHIDQRII
SPERIESHAN NWKDVDYLIF NTYIWWMNNE DIKVRRPNST SWSDHDEVPR IETYGRVFKT
WSTWLEQNVD PARTSVFFMT ISPLHNSPAQ WGNPNGIKCV KETLPVLNYT KPLDLNHDMR
MYDLVAKVAK NMKNVPVSLI DITRMSDYRK DAHTSLYSIR QGKLLTPEQK ADPQKYADCI
HWCLPGVPDV WNQILYTRIL SKSSPPSTHP SLPPQ
