XOAT9_ORYSJ
ID XOAT9_ORYSJ Reviewed; 454 AA.
AC Q5W6Y3; Q0DIW6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable xylan O-acetyltransferase 9 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 4 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL4 {ECO:0000303|PubMed:27864442};
GN Name=XOAT9 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL4 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os05g0356700 {ECO:0000312|EMBL:BAS93573.1},
GN LOC_Os05g28830 {ECO:0000305};
GN ORFNames=OSJNBa0036C12.14 {ECO:0000312|EMBL:AAV43944.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 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; MH037023; AVR54513.1; -; mRNA.
DR EMBL; AC121363; AAV43944.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17207.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93573.1; -; Genomic_DNA.
DR RefSeq; XP_015638348.1; XM_015782862.1.
DR AlphaFoldDB; Q5W6Y3; -.
DR SMR; Q5W6Y3; -.
DR STRING; 4530.OS05T0356700-01; -.
DR PaxDb; Q5W6Y3; -.
DR PRIDE; Q5W6Y3; -.
DR EnsemblPlants; Os05t0356700-01; Os05t0356700-01; Os05g0356700.
DR GeneID; 4338521; -.
DR Gramene; Os05t0356700-01; Os05t0356700-01; Os05g0356700.
DR KEGG; osa:4338521; -.
DR eggNOG; ENOG502QTQP; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q5W6Y3; -.
DR OMA; NASTTTW; -.
DR OrthoDB; 635575at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
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:0009834; P:plant-type secondary cell wall biogenesis; IEA:EnsemblPlants.
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..454
FT /note="Probable xylan O-acetyltransferase 9"
FT /id="PRO_0000454033"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..454
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 175..177
FT /note="GDS motif"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT MOTIF 430..433
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 430
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 101..152
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 123..188
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 132..435
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 352..431
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 454 AA; 50621 MW; 0CC545D60E8B85C9 CRC64;
MKAPPPPSPV AKRARVSPFV FLLVLFLLLF SFLYGEDLKE LLGSQAQARP SLHFNAAAAG
DGIELPAATA ATTEGRTTTR RWRGRLPFAA NGDGEEEEEE CDVFSGRWVR DEAARPLYRE
ADCPYIPAQL ACEAHGRPET AYQRWRWQPR GCALPAFDAA AMLDRLRGKR VMFVGDSLGR
GQFTSLVCLL LAAVPDPAAR SFATSPDQQR SVFTAAAYNA TVEFYWAPFL LQSNADNAAV
HRISDRMVRR GSIGHHGRHW EGADVIVFNT YLWWCTGLQF RILEDGPFDA GGNSSTTTWV
STEEAYAMAF REMLQWAREH MDFATTRVFF TSMSPTHGKS QDWGGGEPGG NCYGETEMIG
DAAYWGSDSR RGVMRAIGEV LDGDGADVPV TFLNVTQLSL YRKDAHTSVY KKQWTPPTPE
QLADPKTYAD CVHWCLPGLQ DTWNELLYTK LFYP
