XOATA_ORYSJ
ID XOATA_ORYSJ Reviewed; 441 AA.
AC Q84TW8; A0A0P0W4X3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable xylan O-acetyltransferase 10 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 5 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL5 {ECO:0000303|PubMed:27864442};
GN Name=XOAT10 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL5 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os03g0817900 {ECO:0000312|EMBL:BAS87061.1},
GN LOC_Os03g60350 {ECO:0000312|EMBL:ABF99561.1};
GN ORFNames=OSJNBa0094J08.9 {ECO:0000312|EMBL:AAO60022.1};
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 TISSUE
RP 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=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 -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems.
CC {ECO:0000269|PubMed:29569182}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH037024; AVR54514.1; -; mRNA.
DR EMBL; AC133007; AAO60022.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99561.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13617.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS87061.1; -; Genomic_DNA.
DR EMBL; AK071479; BAG92516.1; -; mRNA.
DR RefSeq; XP_015629850.1; XM_015774364.1.
DR AlphaFoldDB; Q84TW8; -.
DR SMR; Q84TW8; -.
DR STRING; 4530.OS03T0817900-01; -.
DR PaxDb; Q84TW8; -.
DR PRIDE; Q84TW8; -.
DR EnsemblPlants; Os03t0817900-01; Os03t0817900-01; Os03g0817900.
DR GeneID; 4334575; -.
DR Gramene; Os03t0817900-01; Os03t0817900-01; Os03g0817900.
DR KEGG; osa:4334575; -.
DR eggNOG; ENOG502QTQP; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q84TW8; -.
DR OMA; RSKDWGD; -.
DR OrthoDB; 635575at2759; -.
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: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..441
FT /note="Probable xylan O-acetyltransferase 10"
FT /id="PRO_0000454034"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..441
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 50..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 171..173
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 417..420
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 417
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 420
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 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 97..148
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 119..184
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 128..422
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 341..418
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 441 AA; 49944 MW; C7B4BD8123961535 CRC64;
MMKPQHGGMA GHGGGRTRSP FLTSYALTLA FITFVSVLYF KDFSSTLHQP FLTRPPPHRR
QIARPRAPSH HHGGGSSSGG GDVVPPFAVG AAAAAGCDVG VGEWVYDEAA RPWYEEEECP
YIQPQLTCQA HGRPDTAYQH WRWQPRGCSL PSFNATLMLE MLRGKRMMFV GDSLNRGQYV
SLVCLLHRSI PESSKSMETF DSLTVFRAKN YNATIEFYWA PFLAESNSDD AVVHRIADRI
VRGTALEKHA RFWKGADILV FNSYLWWMTG QKMKILQGSF EDKSKDIVEM ETEEAYGMVL
NAVVRWVENN MNPRNSRVFF VTMSPTHTRS KDWGDDSDGN CYNQTTPIRD LSYWGPGTSK
GLMRVIGEVF STSKVPVGIV NITQLSEYRK DAHTQIYKKQ WNPLTPEQIA NPKSYADCTH
WCLPGLQDTW NELLYSKLFF P
