XOAT8_ORYSJ
ID XOAT8_ORYSJ Reviewed; 442 AA.
AC Q10MX4; Q0DSS6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable xylan O-acetyltransferase 8 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 8 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL8 {ECO:0000303|PubMed:27864442};
GN Name=XOAT8 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL8 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os03g0291200 {ECO:0000312|EMBL:BAS83671.1},
GN LOC_Os03g18120 {ECO:0000312|EMBL:ABF95400.1};
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, AND CATALYTIC ACTIVITY.
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(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 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 [7]
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: Probable xylan acetyltransferase required for 2-O- and 3-O-
CC monoacetylation of xylosyl residues in xylan (PubMed:29569182).
CC Possesses extremely low activity in vitro (PubMed:29569182).
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 -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH037022; AVR54512.1; -; mRNA.
DR EMBL; DP000009; ABF95400.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11712.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83671.1; -; Genomic_DNA.
DR EMBL; AK110898; BAG99075.1; -; mRNA.
DR RefSeq; XP_015632090.1; XM_015776604.1.
DR AlphaFoldDB; Q10MX4; -.
DR SMR; Q10MX4; -.
DR STRING; 4530.OS03T0291200-01; -.
DR PaxDb; Q10MX4; -.
DR PRIDE; Q10MX4; -.
DR EnsemblPlants; Os03t0291200-01; Os03t0291200-01; Os03g0291200.
DR GeneID; 4332503; -.
DR Gramene; Os03t0291200-01; Os03t0291200-01; Os03g0291200.
DR KEGG; osa:4332503; -.
DR eggNOG; ENOG502QT29; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q10MX4; -.
DR OMA; DWHLDDC; -.
DR OrthoDB; 697301at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
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:0005886; C:plasma membrane; IEA:EnsemblPlants.
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:0030244; P:cellulose biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009827; P:plant-type cell wall modification; IEA:EnsemblPlants.
DR GO; GO:1990937; P:xylan acetylation; IDA:UniProtKB.
DR GO; GO:0045492; P:xylan biosynthetic process; IEA:EnsemblPlants.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR029972; TBL3/8.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF7; PTHR32285:SF7; 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..442
FT /note="Probable xylan O-acetyltransferase 8"
FT /id="PRO_0000454032"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..442
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 174..176
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 421..424
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 421
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 424
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 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 100..151
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 122..187
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 131..426
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 344..422
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 442 AA; 50255 MW; A8592576B65DCDCA CRC64;
MVQLPAMKRV KGRAPLSVVV AIIGGLALAG IIFTEDLRGL TEVKEKVTDK EKKRTSLRTV
MRTSALLSAD QPPPPAVLSV EPATATPPPA PKMAFNATRC SVTDGYWAYD RSKKLPYTDQ
TCPYVDRQDS CQRNGRPDSD YLYWDWHLDD CLLPRFDPVS MLEKLRGKRI MFVGDSLQLG
QWLSFVCLVN SAVPDTPGAK SMERSRTLSV YTVKEYNASI EFYWAPFLVE SNSDRNIALG
AGGRVLHVDA IEEHGKHWRR ADILVFDSYV WWMTGYRIKS VWGSFGDDGY EELDAWVAYR
LGLKTWANWV DSNVDPATTR VFFMSISTTH MRSEDWGREG GIRCYNETWP ITQRGYRGSG
SDRRMMEVMS DVLGRMRTPV TLLNITQLTE HRVDAHVSVY TETGGLLVTD EEKTDPQRYT
DCIHWCIPGV PDTWNRLLYA HL
