XOAT4_ORYSJ
ID XOAT4_ORYSJ Reviewed; 476 AA.
AC A0A0P0XXR9; Q0IV91; Q2RBN8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Xylan O-acetyltransferase 4 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 10 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL10 {ECO:0000303|PubMed:27864442};
GN Name=XOAT4 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL10 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os11g0104800 {ECO:0000312|EMBL:BAT12299.1},
GN LOC_Os11g01370 {ECO:0000312|EMBL:ABA91060.1};
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 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=1.63 mM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=79.3 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA91060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF27374.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; MH037018; AVR54508.1; -; mRNA.
DR EMBL; DP000010; ABA91060.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008217; BAF27374.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014967; BAT12299.1; -; Genomic_DNA.
DR RefSeq; XP_015617768.1; XM_015762282.1.
DR AlphaFoldDB; A0A0P0XXR9; -.
DR SMR; A0A0P0XXR9; -.
DR STRING; 4530.OS11T0104800-01; -.
DR PaxDb; A0A0P0XXR9; -.
DR EnsemblPlants; Os11t0104800-01; Os11t0104800-01; Os11g0104800.
DR GeneID; 4349545; -.
DR Gramene; Os11t0104800-01; Os11t0104800-01; Os11g0104800.
DR KEGG; osa:4349545; -.
DR eggNOG; ENOG502SJAQ; Eukaryota.
DR OMA; RYWSEHD; -.
DR OrthoDB; 469326at2759; -.
DR Proteomes; UP000000763; 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: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..476
FT /note="Xylan O-acetyltransferase 4"
FT /id="PRO_0000454028"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..80
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..476
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..193
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 439..442
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT COMPBIAS 15..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 439
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 117..168
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 139..204
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 148..444
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 360..440
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 476 AA; 54715 MW; 15055775C60CC50D CRC64;
MTKPQQQSPP STTATTTTSP PPPPPSTPPP ASSSSSSLAK LPLRLHSLAS SSRSLLSALR
RSPVTTLVAA FFLLALFMYG EDVRTLAELS IDDYLYPDAD FYNVSALPPL LLPPPTCDLS
RGRWVFDNTS LPAYREKECT FLTKQVSCLA NGRPDDLWQY WRWQPNNCSL PTFDARRFME
KMRGKRMMFV GDSLNRNQWE SLVCLVQPIL SKGRKKIVKR GSFNIFYAKE YRATLEFYWA
PFLVESNSDN PNFHHIDQRI ISPERIESHA NNWKDVDYLI FNTYIWWMNN EDIKVRRPNS
TSWSDHDEVP RIETYGRVFK TWSTWLEQNV DPARTSVFFM TISPLHNSPA QWGNPNGIKC
VKETLPVLNY TKPLDLNHDM RMYDLVAKVA KNMKNVPVSL IDITRMSDYR KDAHTSLYSI
RQGKLLTPEQ KADPQKYADC IHWCLPGVPD VWNQILYTRI LSKSSPPSPH PPLPPQ
