XAT2_ORYSJ
ID XAT2_ORYSJ Reviewed; 583 AA.
AC Q6ZFR0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-1,3-arabinosyltransferase XAT2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:22215597};
DE AltName: Full=Xylan arabinosyltransferase 2 {ECO:0000303|PubMed:22215597};
DE Short=OsXAT2 {ECO:0000303|PubMed:22215597};
GN Name=XAT2 {ECO:0000303|PubMed:22215597};
GN OrderedLocusNames=Os02g0330200 {ECO:0000312|EMBL:BAF08634.1},
GN LOC_Os02g22480 {ECO:0000305};
GN ORFNames=OJ1116_E03.2 {ECO:0000312|EMBL:BAD15592.1},
GN OsJ_06523 {ECO:0000312|EMBL:EEE56880.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22215597; DOI=10.1073/pnas.1115858109;
RA Anders N., Wilkinson M.D., Lovegrove A., Freeman J., Tryfona T.,
RA Pellny T.K., Weimar T., Mortimer J.C., Stott K., Baker J.M.,
RA Defoin-Platel M., Shewry P.R., Dupree P., Mitchell R.A.;
RT "Glycosyl transferases in family 61 mediate arabinofuranosyl transfer onto
RT xylan in grasses.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:989-993(2012).
CC -!- FUNCTION: Glycosyltransferase involved in the arabinosylation of xylan,
CC the major hemicellulose (non-cellulosic component) of primary and
CC secondary walls of angiosperms (PubMed:22215597). Possesses alpha-1,3-
CC arabinosyltransferase activity, transferring an arabinofuranose residue
CC to the xylan backbone (PubMed:22215597). {ECO:0000269|PubMed:22215597}.
CC -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:22215597}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
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DR EMBL; AP004177; BAD15592.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08634.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS78435.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE56880.1; -; Genomic_DNA.
DR RefSeq; XP_015622780.1; XM_015767294.1.
DR AlphaFoldDB; Q6ZFR0; -.
DR SMR; Q6ZFR0; -.
DR STRING; 4530.OS02T0330200-01; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q6ZFR0; -.
DR PRIDE; Q6ZFR0; -.
DR EnsemblPlants; Os02t0330200-01; Os02t0330200-01; Os02g0330200.
DR GeneID; 4329205; -.
DR Gramene; Os02t0330200-01; Os02t0330200-01; Os02g0330200.
DR KEGG; osa:4329205; -.
DR eggNOG; KOG4698; Eukaryota.
DR HOGENOM; CLU_016869_3_1_1; -.
DR InParanoid; Q6ZFR0; -.
DR OMA; PPYHEVI; -.
DR OrthoDB; 567582at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052636; F:arabinosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..583
FT /note="Alpha-1,3-arabinosyltransferase XAT2"
FT /id="PRO_0000445786"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..583
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 73..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 583 AA; 66222 MW; 0AEB38E592550C92 CRC64;
MKPVERAKLV RSLRQESRRL RLLVLVIGFF LVTLTFVVIS KPDALLFNLN GRLSVDHAPR
SLLIRQRIHA DSRRSADTFP AAEDPKVVDE DEGAEDATAK GTSEEEKRLL SSEPEQGKNE
EAATASEVLG GGGEEDNKNG EEEGHTQHSK VTLPTVSNYT IRDAEDTDNG KQEDGKPNEK
YEFEMDADKG DNVEPETDNE EWNKKPLCDF SNFRANVCEM RGNIRIHPNA SSVMYMEPAS
SKREEIWKVK PYPRKGDELC LGHITEITVK SSKVAPECSK YHNVPAVVFA LTGYTGNLFH
DFTDVLVPLF TTASEFNGEV QFLITDMAIW WTRKYKVVFD KLSKYPLIDF NNDDQVHCFK
HAIVGLHAYM EFTIDSSKAP HNYSMVDFNR FMRRTYSLPR DFVTALGEIP KAKPRLLIIS
RQRTRMFLNL NEIVAMAEEI GYEVVVEEAN VSSDLSHFGK VVNSVDVMMG VHGAGLTNCV
FLPQNATLIQ IVPWGGLDWI SRIDFGNPAE QMGLRYKQYS IGVHESSLTD QYPLDHEIFT
NPLSFHKHGF EFIRQTFMDK QNVKLDCNRF KPVLLEVLDQ LNQ
